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Réactivités croisées entre Fabacées
dimanche 15 juin 2008, par
La question d’une allergie croisée entre différentes graines de Fabacées est justifiée par la fréquence avec laquelle des tests cutanés sont trouvés positifs chez un même patient pour différentes Fabacées, constatation relayée par les tests in vitro de réactivité croisée.
Cela peut correspondre à au moins 3 cadres de sensibilisation. Il ne sera envisagé ici que celui où, apparemment, le rôle des PR-10 (bouleau) et des LTP ne semble pas prépondérant ou n’a pas été démontré.
Les tableaux ci-dessous dressent un aperçu épidémiologique des co-réactivités aux Fabacées selon le motif de recrutement des patients ? Il va de soi que l’âge (ex. pollinose ou non) et l’origine géographique des patients sont des paramètres importants à considérer par ailleurs.
Associations cliniques et/ou immunologiques entre Fabacées
(hors contexte bouleau ou LTP) :
1- Recrutement = arachide
| Réf. | Nombre patients (Pays) | Recrutement / sélection | Autres allergies / histoires cliniques | Tests cutanés et/ou in vitro |
 |
7 cas (USA) | arachide | HC+ pois 5 | TC+ lupin 5 |
|
24 enfants (France) | arachide (TPO) | lupin : TPO+ 5, TPL+ 2 | TC+ lupin 44% |
|
1 enfant (France) | arachide (anaphylaxie) | TPO+ lupin 4 ans après | |
|
223 enfants (USA) | arachide (pas de TPO chez 64%) | TPO+ soja 5/11 testés (ces 11 avaient un TPO+ arachide = ?) | |
|
86 (France) | RAST classe >=3 arachide | HC+ pois 6 soja 6 lupin 0 |
RAST+ pois 75% soja 86% lupin 83% |
|
142 (93% enfants) (France) | arachide | HC+ soja 2 cas pois 4 cas lentille 2 |
TC+ soja 20 cas pois 13 |
|
72 enfants (France) | arachide | TC+ lupin 17 | |
|
32 enfants (USA) | arachide (TPODA) | TPODA+ soja 1 pois aucun |
|
|
72 (Danemark) | arachide | TPO+ : soja 2/44 lupin 3/9 pois frais 10/52 pois cuit 0/40 |
TC+ natifs : soja 28% lupin 49% pois frais 41% pois cuit 16% |
|
315 enfants et 48 adultes (France) | arachide | TC+ lupin : enfants 17,1% adultes 14,5% | |
|
16 adultes (Espagne) | arachide | TPODA+ : lupin 2 | TC+ et/ou CAP+ : lupin 14 |
|
16 enfants (Japon) | arachide | soja : aucun | |
|
47 enfants (Gde Bretagne) | arachide | TPODA+ lupin 2/9 HC+ soja 13% |
TC+ lupin 34% |
HC+ = histoire clinique positive / TC+ = test cutané positif / CAP+ = test in vitro CAP positif
TPO(DA) = test de provocation par voie orale (en double aveugle) / TPL = test de provocation labiale
2- Recrutement = lupin
| Réf. | Nombre patients (Pays) | Recrutement / sélection | Autres allergies / histoires cliniques | Tests cutanés et/ou in vitro |
|
1 adulte (Espagne) | lupin | HC+ pois chiche, lentille, haricot | TC négatif arachide |
|
1 adulte (France) | lupin (all. respiratoire) | TC négatifs lupin et arachide | |
|
2 adultes (France) | lupin (1 avec anaphylaxie) | tolèrent arachide | |
|
1 enfant (France) | lupin (anaphylaxie) | tolère arachide | TC+ arachide TC négatifs soja, pois, lentille |
|
26 enfants (France) | TC+ lupin | HC+ arachide 17 autre Fabacée 8 |
TC+ arachide 20 |
|
3 adultes (Australie) | lupin | TC+ pois 2 soja 1 arachide 0 | |
|
1 adulte (Allemagne) | lupin (réaction sévère) | TC négatifs pois, haricot CAP négatif arachide | |
|
1 enfant (Suisse) | lupin (anaphylaxie) | tolère arachide | TC+ arachide TC négatif soja |
|
2 adultes (Portugal) | lupin (OAS) | tolèrent arachide | TC négatifs soja, lentille, haricot, arachide |
|
2 adultes (Suisse) | lupin | HC+ arachide 1/2 |
3- Recrutement = soja
| Réf. | Nombre patients (Pays) | Recrutement / sélection | Autres allergies / histoires cliniques | Tests cutanés et/ou in vitro |
|
1 adulte (Espagne) | soja (anaphylaxie) | HC+ arachide (postérieurement) | |
|
1 enfant (France) | soja (tofu) (décès) | HC+ arachide | |
|
2 adultes (Allemagne) | soja (TPO) | HC+ arachide : 1/2 | |
|
24 (Canada) | isolat soja | HC+ arachide (début 3 à 25 ans avant) | TC+ soja : tous |
4- Recrutement = Fabacées diverses
| Réf. | Nombre patients (Pays) | Recrutement / sélection | Autres allergies / histoires cliniques | Tests cutanés et/ou in vitro |
|
69 enfants (USA) | au moins 1 TC+ pour une Fabacée | TPO+/TC+ : arachide 52%* soja 33%* pois 11% haricot vert aucun haricot du cap aucun * seuls 2 patients avec >1 TPO+ |
TC+ : arachide 87% soja 43% pois 26% haricot vert 22% haricot du cap 41% |
|
2 adultes (Inde) | fenugrec (1 par inhalation, 1 par voie cutanée | HC+ fenugrec (all. alim.) et pois chiche | |
|
31 (Inde) | pois chiche (TPODA) | TPODA+ >= 1 autre Fabacée 7 patients | |
|
3 adultes (Pays bas) | pois (2 cas sévères) | HC+ arachide plus tard | |
|
18 enfants + 4 adultes (Espagne) | lentilles (TPO ouv + 1 cas anaphylaxie) | TC+ pois chiche 18 pois 17 arachide 20 soja 15 haricot 13 | |
|
1 adulte (Espagne) | lentilles (anaphylaxie) | TC+ pois | |
|
15 enfants + 3 adultes (Espagne) | pois (TPO ouvert) | TC+ lentille 14 arachide 13 pois chiche 11 haricot 7 soja 5 | |
|
1 enfant (Portugal) | pois chiche (OAS) | TC+ arachide | |
|
1 adulte (Espagne) | pois chiche et lentille (all. alim. et resp.) | tolère arachide, pois, haricot vert | TC+ arachide, pois, haricot vert |
|
2 enfants (France) | fenugrec (TPO) | HC+ arachide | |
|
1 adulte (Portugal) | fève (TPO) | TC négatif pour toutes Fabacées | |
|
1 adulte (Espagne) | fève (TPO) | HC+ pois, pois chiche, lentille, haricot mais pas soja (arachide pas consommée) |
Le travail classique de Bernhisel-Broadbent avait montré qu’il fallait prendre garde aux nombreux tests cutanés positifs non confirmés en TPODA . Ce travail venait notamment en réponse à des résultats antérieurs qui avaient généré une tendance à exclure du régime des Fabacées nutritionellement importantes (haricots, pois, etc..).
L’ensemble des études effectuées depuis la publication de Bernhisel-Broadbent a solidement confirmé le grand excès des tests diagnostiques positifs (cutanés et sériques) sans relevance clinique (cf. les tableaux ci-dessus).
Quelle est l’importance relative des réactions cliniques pour telle ou telle Fabacée quand un patient est allergique à une Fabacée ?
En prenant une moyenne des prévalences des différentes cohortes publiées on peut en avoir une idée (très approximative) :
Dans ce cas :
- l’allergie au lupin est rencontrée chez 23% des patients,
- celle pour le soja chez 3%,
- celle pour le pois chez 2% et
- celle pour les lentilles entre 1 et 2%.
- A noter que dans la majorité des cas il s’agissait d’allergies à l’arachide chez l’enfant, hors contrées méditerranéennes.
Par comparaison, si une pollinose au bouleau est présente, ces proportions pourraient être différentes : une étude a indiqué un fréquence de 35% pour le lupin (TPO) et de 33% pour le pois et 29% pour le soja (sans contrôle par TPO) .
Chez des enfants pour lesquels le diagnostic d’allergie à l’arachide a été écarté, la prévalence d’une allergie au soja était très faible, 0,6%, dans une étude de Rancé en France .
L’allergie à l’arachide augmente donc le risque d’observer une allergie au soja, quelqu’en soit le mécanisme. Mais une allergie au soja peut très bien s’établir par elle-même, indépendamment de l’arachide .
Les relations entre pois et arachide sont souvent à l’avantage de l’arachide mais il a été observé des cas où l’allergie au pois avait débuté avant celle pour l’arachide .
La relation arachide-lupin est plus complexe : dans la plupart des cas l’arachide est capable d’inhiber l’IgE-réactivité du lupin,
- qu’une allergie à l’arachide soit présente
- ou absente chez les patients testés.
Dans une étude portant sur l’allergie aux lentilles cette réactivité croisée n’était pas observée .
Il faut, de plus, envisager le rôle d’une pollinose au bouleau, de sorte qu’une réactivité simultanée au lupin et à l’arachide peut résulter d’une même sensibilisation à des protéines PR-10 . (cf. Fabacées et bouleau).
Le nombre limité d’observations d’allergie au lupin rend délicate l’interprétation des associations, mais quand le motif d’exploration est une allergie au lupin la relation avec l’arachide semble rare : dans 7 cas d’allergie au lupin il n’était relevé qu’un seul cas d’allergie à l’arachide (cf. tableaux ci-dessus).
Si une pollinose au bouleau est présente également on peut trouver une plus forte proportion d’allergiques à l’arachide
Elle semble nettement associée à l’allergie à l’arachide, laquelle est généralement apparue la première.
Peu de différence, ici, entre présence ou absence de pollinose au bouleau : dans les 2 cas l’allergie à l’arachide est très fréquente
– Allergie aux pois, pois chiche, lentille, haricot :
On manque de données détaillées sur le plan épidémiologique mais ces légumineuses ont une allergénicité certaine dans plusieurs régions du monde du fait d’habitudes alimentaires locales (ex. sub-continent indien).
En Espagne, l’ensemble lentille + pois + pois chiche représente la 4ème cause d’allergies alimentaires de l’enfant.
In vitro, des réactivités croisées entre ces 3 Fabacées sont presque constamment retrouvées.
La réactivité croisée entre le pois et d’autres Fabacées est possible du fait de l’homologie entre Pis s 1 et d’autres vicilines (Ara h 1 dans l’arachide, une viciline dans la fève, etc..) et particulièrement celle de lentille, Len c 1 (env. 90% d’identité avec Pis s 1). Cela a reçu confirmation in vitro .
La réalité d’un lien immunologique entre Fabacées a récemment été démontrée à l’aide de tests cellulaires par Bjerremann Jensen .
Des basophiles naïfs ont été passivement activés avec le sérum de patients allergiques à l’arachide, puis ces basophiles ont été mis en contact avec des extraits de légumineuses : le lupin, le soja et le pois parvenaient à dégranuler les basophiles, d’autres Fabacées également mais à un moindre degré.
On retrouve bien, pour ces patients résidant hors des régions méditerranéennes, les 3 principales Fabacées associées à une allergie à l’arachide et on comprend d’autant mieux la fréquence élevée des tests cutanés observés chez ces patients.
Il ne s’agit donc pas que de réactivité croisée in vitro (et de CCD ..).
Pourquoi peu de patients réagissent cliniquement au pois bien qu’ayant un TC positif ? C’est une question qui mériterait d’être élucidée.
En attendant, il faut considérer avec tact et mesure les résultats publiés de réactivité croisée : dans le cas des Fabacées il est encore plus clair que réactivité croisée in vitro ne signifie pas mécaniquement allergie croisée pour le patient.
[1] - Hefle SL, Lemanske RF Jr, Bush RK. Adverse reaction to lupine-fortified pasta. J Allergy Clin Immunol 1994;94:167-172
A 5-year-old girl with peanut sensitivity experienced urticaria and angioedema after ingesting a spaghetti-like pasta fortified with sweet lupine seed flour. The pasta was extracted and used in immunologic studies in patients with peanut sensitivity to determine whether such individuals are at similar risk. Results of skin prick tests with the lupine pasta extract were positive in five of seven subjects; these patients also reported a history of adverse reactions to green peas. In direct RAST studies IgE binding from pooled sera from patients with peanut sensitivity to the lupine pasta extract was 7 times that of a nonallergic control serum, and individual serum samples demonstrated binding from 1 to 6 times that of the negative control. Direct RAST studies of lupine seed flour with serum samples from patients with peanut allergy demonstrated IgE binding 1 to 11 times that of the negative control. Immunoblotting studies of electrophoretically separated pasta extract and lupine seed flour proteins showed IgE-binding protein bands at approximately 21 kd and in the range of 35 to 55 kd molecular weight. We conclude that some peanut-sensitive patients may be at risk for adverse reactions to lupine.
↩[2] - Moneret-Vautrin DA, Guérin L, Kanny G, Flabbee J, Frémont S, Morisset M. Cross-allergenicity of peanut and lupine: the risk of lupine allergy in patients allergic to peanuts. J Allergy Clin Immunol 1999;104:883-888
BACKGROUND: Peanut allergy is common, but cross-allergy between legumes is rare. Proteins from Lupinus albus are increasingly eaten in the form of seeds or additives to wheat flour. The risk of cross-allergenicity is still insufficiently known .
OBJECTIVE: We sought to study the risk of cross-allergy to lupine in patients allergic to peanut and to study lupine allergenicity .
METHODS: Twenty-four patients allergic to peanuts were studied by means of skin prick tests with native lupine flour from Lupinus albus. Double-blind oral challenge tests were performed with lupine flour and peanut in 8 of these patients. Specific IgEs were assayed for peanut, lupine flour, and pollen in 6 sera. RAST inhibition tests for lupine pollen by peanut were performed on 4 of these sera. Peanut and lupine flour immunoblots were carried out for 6 sera, and crossed immunoblot inhibitions for peanut by lupine flour and lupine flour by peanut were carried out for 2 sera .
RESULTS: The skin prick test responses with lupine flour were positive in 11 (44%) subjects. The challenge test responses were positive in 7 of 8 subjects at the same doses as with peanut. The major lupine flour allergen (molecular mass, 43 kd) is present in peanuts. The RAST inhibition and immunoblot tests indicated cross-reactivity of peanut with the lupine flour and pollen .
CONCLUSIONS: The risk of crossed peanut-lupine allergy is high, contrary to the risk with other legumes. The inclusion of 10% lupine flour in wheat flour without mandatory labeling makes lupine a hidden allergen, presenting a major risk of cross-reaction in subjects already allergic to peanut products. A high sensitizing potential can also be postulated for this legume.
↩[3] - Kanny G, Guérin L, Moneret-Vautrin DA. Le risque d'asthme aigu grave à la farine de lupin associé à l'allergie à l'arachide. Rev Med Interne 2000;21:191-194
Lupine flour (lupinus albus), recently authorized in France in human food, cross-reacts with peanuts. We report a case of acute asthma in a patient with allergy to peanuts. EXEGESIS: This patient has a severe allergy to peanuts, presenting as acute asthma. Skin prick-tests to raw and cooked lupine flour were positive. The level of specific-IgE (Allerbio, France) to lupine flour were high. Oral challenge test induced acute asthma at a dose of 965 mg of lupine flour. This quantity may be included in 100 g of bread .
CONCLUSION: This case report points out the fact that lupine flour is a high-risk allergen in patients presenting allergy to peanuts. It is necessary to evaluate the allergenic risk of new foods before their introduction into human daily food intake and to establish a network of allergy vigilance.
↩[4] - Skolnick HS, Conover-Walker MK, Barnes Koerner C, Sampson HA, Wood RA. The natural history of peanut allergy. J Allergy Clin Immunol 2001;107:367-374
BACKGROUND: It has traditionally been assumed that peanut allergy is rarely outgrown.
OBJECTIVE: The goal of this study was to determine the number of children with peanut allergy who become tolerant of peanut. METHODS: Patients aged 4 to 20 years with a diagnosis of peanut allergy were evaluated by questionnaire, skin testing, and a quantitative antibody fluorescent-enzyme immunoassay. Patients who had been reaction free in the past year and had a peanut IgE (PN-IgE) level less than 20 kilounits of antibody per liter (kU(A)/L) were offered an open or double-blind, placebo-controlled peanut challenge.
RESULTS: A total of 223 patients were evaluated, and of those, 85 (PN-IgE < 0.35-20.4 kU(A)/L [median 1.42 kU(A)/L]) participated in an oral peanut challenge. Forty-eight (21.5%) patients had negative challenge results and were believed to have outgrown their peanut allergy (aged 4-17.5 years [median 6 years]; PN-IgE < 0.35-20.4 kU(A)/L [median 0.69 kU(A)/L]). Thirty-seven failed the challenge (aged 4-13 years [median 6.5 years]; RAST < 0.35-18.2 kU(A)/L [median 2.06 kU(A)/L]). Forty-one patients with PN-IgE levels less than 20 kU(A)/L declined to undergo challenge, and 97 were not eligible for challenge because their PN-IgE levels were greater than 20 kU(A)/L or they had had a recent reaction. Sixty-seven percent of patients with PN-IgE levels less than 2 kU(A)/L and 61% with levels less than 5 kU(A)/L had negative challenge results. Of those who underwent challenge, PN-IgE levels for those who passed versus those who failed were different at the time of challenge (P = .009), but not at the time of diagnosis (P = .25). CONCLUSION: This study demonstrates that peanut allergy is outgrown in about 21.5% of patients. Patients with low PN-IgE levels should be offered a peanut challenge in a medical setting to demonstrate whether they can now tolerate peanuts.
↩[5] - André F, Cavagna S, Didierlaurent A, André C. Farine de lupin: un allergène sensibilisant fréquent mais un coupable occasionnel. Communication: 10èmes Journées Parisiennes d'Allergie - Paris 9-11 janvier 2002 ↩
[6] - Moneret-Vautrin DA, Rancé F, Kanny G, Olsewski A, Guéant JL, Dutau G, et al. Food allergy to peanuts in France: evaluation of 142 observations. Clin Exp Allergy 1998;28:1113-1119
BACKGROUND: The increase in frequency of peanut allergy and fatal cases have been reported. OBJECTIVES: The objective of this study is to document the severity of food allergy to peanuts by evaluating the reactive dose of peanuts and to search for the role of peanut oil.
METHODS: This study is carried out on the basis of 142 observations collected according to the same diagnostic methodology in two allergy centres in France. Skin-prick-tests were performed with peanut powder, peanut oil and peanut oil proteinic extract. Labial provocation tests were performed on 121 patients. The reactive dose of peanuts and the role of peanut oil were determined by standardized oral provocation tests in 50 and 62 patients respectively. The data are computerized and the data bank includes 509 food allergic patients.
RESULTS: Allergy to peanuts represents 28% of food allergies and occurs under 1 year of age in 46% of cases, under 15 years of age in 93%. The clinical features were atopic dermatitis (40%), angioedema (37%), asthma (14%), anaphylactic shock (6%) and digestive symptoms (1.4%). The specific IgE were class 3 or higher in 80% of cases. The total reactive dose was less than 100 mg in 25% of cases, from 100 mg to 1 g in 62.5%. All patients reacted to a dose of less than 7.1 g. The threshold of peanut reactivity was lower than the threshold of egg reactivity. An allergy to peanut oil was demonstrated in 14 patients. CONCLUSION: The severity of peanut allergy and the early onset of the occurrence of this allergy is documented. The role of residual allergenic proteins in peanut oil is established by positive skin-prick tests to proteic extracts from peanut oil and by double-blind placebo-controlled challenges to peanut oil. The increased consumption of allergens in the form of peanut oil and fats can contribute to the occurrence or persistence of symptoms and may be suspected to increase the risk of sensitisation.
↩[7] - Mazeyrat R, Ponvert C, Thibault M, Asensi D. Sensibilisation à la farine de lupin: risque pour l'enfant allergique à l'arachide. Rev Fr Allergol Immunol Clin 2004;44:133 ↩
[8] - Bock SA, Atkins FM. The natural history of peanut allergy. J Allergy Clin Immunol 1989;83:900-904
Between 1973 and 1985, 114 children, aged 2 to 14 years, underwent double-blind, placebo-controlled, food challenge (DBPCFC) to peanut. Thirty-two of 46 children with symptoms produced by DBPCFC to peanut were included in this longitudinal evaluation. Contact was made with the 32 subjects 2 to 14 years after their positive DBPCFC to peanut. All 32 subjects had exhibited a positive puncture skin test to peanut at the time of the original evaluation. Sixteen subjects had experienced symptoms caused by accidental peanut ingestion in the year before contact. Eight subjects had reacted to accidental ingestion in more than 1 year but less than 5 years before contact. Eight subjects had completely avoided peanut since the original evaluation and positive DBPCFC. No subjects could be demonstrated to have "outgrown" their peanut reactivity. All subjects tested continued to have skin reactivity to a puncture skin test with peanut extract. It appears uncommon for peanut-sensitive patients to lose their clinical reactivity, even after many years have elapsed. In addition, data were collected concerning reactions to other legumes and other (nonlegume) nuts. Only two patients with DBPCFC to peanut reacted on DBPCFC to soy or pea (one each). None of the subjects with a positive DBPCFC to peanut reacted to nonlegume nuts.
↩[9] - Bjerremann Jensen L, Andersen M, Skov P, Poulsen L, Bindslev-Jensen C. Investigating the common allergic reactivity within the legume botanical family using skin prick test (SPT), specific immunoglobulin E (IgE) and histamine release (HR). EAACI 25th Congress, Vienna, 10-14 June, 2006, Poster n°578
Background: The aim of the study was to investigate possible common allergic reactions between peanut and different foods from the legume family.
Methods: The legumes investigated were peanut, soybean, lupine, and fresh as well as blanched green pea.
Patients were included on the basis of confirmed food allergy to peanut according to EAACI guidelines. SPTs were performed by prick-prick with legumes using as cutoff a wheal with a diameter >3 mm. IgE were determined using the CAP system (Pharmacia, Sweden) with a cutoff of 0.35 kUA/L.
HR was performed by direct stimulation of patient basophils with legume extracts and the released histamine was measured spectrofluorometrically (RefLab ApS, Denmark).
Results: 72 peanut allergic patients were included. The sensitivity for SPT, IgE and HR was 92-97% for peanut. Testing the other legumes with SPT and HR produced most positives for lupine (45%, 80%) and fresh pea (41%, 91%) followed by soybean (28%, 19%) and blanched pea (16%, 5%), whereas soybean produced most positives in IgE (58%) followed by pea (48%) and lupine (47%). Pairwise comparison between the three diagnostic tests in general gave the highest concordance between SPT and HR. A subpopulation of the patients was challenged with the legumes. The most common reported symptom for reactions related to the various foods was the oral allergy syndrome (OAS). 22 patients were challenged with soybean, and of these 2 were positive. 1 of 6 challenges was positive with lupine whereas 0 of 12 was positive with fresh pea. This suggests that clinical coreactivity between peanut and other legumes is substantially lower than indicated by diagnostic tests.
Conclusion: Patients with peanut allergy might in a few cases be clinically allergic to other members of the legume family. However, application of SPT, IgE or HR tests results in an overestimation of the positive reactions.
↩[10] - Gayraud J. Etude par prick-tests chez 5366 patients de la prévalence de la sensibilisation au lupin en France et en Belgique. Alim'Inter 2007;12:249-254 ↩
[11] - Jimenez A, Cabanillas B, Gonzalez A, Crespo JF, Rodriguez J. Reactivity to Lupine in Patients with Clinical Allergy to Peanut, Other Legumes or Tree Nuts. J Allergy Clin Immunol 2008;121:S245
RATIONALE: Lupine is allergenic and potentially cross-reactive with peanut; however the risk of reacting to lupine in adults allergic to other legumes or tree nuts has not been established.
METHODS: Fifty-two adult patients diagnosed of clinical allergy to peanut (n = 16), other legumes (n = 8), and tree nuts (n = 28) were included. Skin prick tests and/or CAP System (FEIA) were performed with lupine in all patients. Clinical reactivity to lupine was routinely assessed by open challenges and when positive, evaluated by DBPCFCs.
RESULTS: Immunologic reactivity to lupine was detected in 88% of 16, 38% of 8, and 61% of 28 patients with actual allergy to peanuts, other legumes, and tree nuts, respectively. Overall, 6 reactions to lupine were confirmed by DBPCFCs. Two reactions had been reported by the patients allergic to peanut and were confirmed by the oral provocations; the remaining reactions were uncovered by routinely performed challenges in patients allergic to other legumes (2) or tree nuts (2), but not to peanut. The rate of clinical reactivity to lupine was 13% (2/16) in patients allergic to peanuts, 25% (2/8) in patients with clinical allergy to other legumes and 7% (2/28) in patients allergic to tree nuts.
CONCLUSIONS: Patients allergic to peanut have an extensive immunologic reactivity to lupine, which elicits clinical reactions in over ten percent of patients. Moreover, the risk of reaction to lupine in patients clinically allergic to other members of the legume family and tree nuts should not be neglected.
↩[12] - Ito K, Takaoka Y, Futamura M, Sakamoto T, Urisu A, Tanaka A. Poor Cross-reactivity to Nut Allergens in Patients with Peanut, Cashew and Walnut Allergies. J Allergy Clin Immunol 2008;121:S243
RATIONALE: The frequency of generally severe and sometimes lifethreatening allergies to peanuts and other tree nuts is increasing among Japanese children, as it is in Europe and the United States. Cross-reactivity among nuts has been suggested, yet most patients seem to be allergic only to one or a few types of nuts.
METHODS: We recruited 27 patients (male: female, 21: 6; mean age, 5.3 years) with a convincing clinical history of immediate-type allergic reactions to peanuts (n = 16), cashews (n = 5) and walnuts (n = 7, one also to peanuts). We measured specific IgE antibodies to peanuts, soy beans, cashews, pistachios, walnuts, pecans, almonds, hazelnuts, Brazil nuts, macadamia nuts and sesame seeds using ImmunoCAP . Clinical reactivity to other nuts was determined from a detailed questionnaire or an oral challenge test.
RESULTS: Levels of IgE antibodies closely correlated between peanuts and soy beans (r=0.801), cashews and pistachios (r=0.979), and walnuts and pecans (r = 0.971). One patient each with a peanut allergy claimed an allergic reaction to almonds, walnuts and sesame seeds. Clinical crossreactions between peanuts and soy were not evident in any of the patients.
Among patients with a walnut allergy, one each claimed a reaction to peanuts, pine nuts and hazelnuts, and none had ever consumed pecans.
None of the patients with a cashew allergy was allergic to any other nuts, but they had never consumed pistachios.
CONCLUSIONS: Clinical and serological cross-reactivity among nut allergies seems less prevalent than previously considered.
↩[13] - Shaw J, Roberts G, Grimshaw K, White S, Hourihane J. Lupin allergy in peanut-allergic children and teenagers. Allergy 2008;63:370-373
BACKGROUND: Lupin has now been introduced into food production in the UK. There is a concern that, on account of cross-reactivity, peanut-allergic children are at high risk for lupin allergy. AIMS: To investigate the prevalence of lupin sensitization and allergy in children with peanut allergy compared with atopic controls .
METHODS: Children (<18 years) were recruited. Peanut-allergic subjects either had a convincing history of peanut allergy with diagnostic peanut skin prick test (SPT) or specific-immunoglobulin E (IgE) results or a positive food challenge. Control subjects were atopic but not peanut-allergic. All subjects had SPT to peanut and lupin. Sensitized subjects were offered a randomized, double-blind, placebo-controlled lupin challenge. Lupin allergy was defined as objective immediate hypersensitivity reaction at food challenge .
RESULTS: Forty-seven peanut-allergic children and 46 atopic controls were recruited. Sixteen peanut-allergic children were sensitized to lupin [34%, 95% confidence interval (CI): 21-49%]. Nine were challenged to lupin. Two reacted (itchy mouth and urticaria; itchy mouth and 20% drop in peak expiratory flow rate) giving a minimum prevalence of lupin allergy in peanut-allergic children of 4.0% (95% CI: 1-15%). Atopic controls were significantly (P = 0.001) less likely to be sensitized to lupin (4%, 95% CI: 1-15%) and had smaller wheals and serum-specific IgE results. None of the atopic controls reacted on lupin challenge, giving a rate of allergy in the atopic controls of 0% (95% CI: 0-8%) .
CONCLUSIONS: A small but significant number of children with peanut allergy are allergic to lupin. Sensitization to lupin is much rarer in nonpeanut-allergic atopic subjects.
↩[14] - Matheu V, de Barrio M, Sierra Z, Gracia-Bara MT, Tornero P, Baeza ML. Lupine-induced anaphylaxis. Ann Allergy Asthma Immunol 1999;83:406-408
Legumes are one of the most common foods causing allergic reactions in children and adults. Cross-reacting antibodies are frequently demonstrated in this family but the real clinical cross-reactivity is uncommon. OBJECTIVE: To report a case of lupine-induced anaphylaxis and to elucidate in vivo and in vitro cross-reactivity with some legumes.
METHODS: Skin prick test (SPT) with some legumes were performed. Cap-IgE, ELISA-IgE, and immunoblotting were carried out. Open oral challenges with some legumes were performed. Cross-reactivity was studied by ELISA and immunoblotting inhibition.
RESULTS: The results demonstrated type-I hypersensitivity reactions with lupine and some other legumes. Cap-IgE with peanut was positive but the SPT and ELISA-IgE were negative and the patient tolerated a peanut challenge. ELISA inhibition revealed a partial inhibition (62%) using lupine as the solid phase. Partial inhibition was demonstrated by immunoblotting inhibition. Open oral challenge with peanut and green bean were negative but positive with pea. CONCLUSION: We present a lupine sensitized patient with positive SPT and in vitro cross-reactivity with other legumes. Clinical cross-reactivity progressively developed over a 5-year period. Discrepancies were found between the clinical aspect and in vitro study of peanut allergy. Factors determining the wide variability in cross-reactivity among individuals are still obscure.
↩[15] - Parisot L, Aparicio C, Moneret-Vautrin DA, Guérin L. Allergy to lupine flour. Allergy 2001;56:918-919 ↩
[16] - Fontaine JF, Capy B, Lavaud F, Lebargy F. Alergie à la farine de lupin: à propos de deux cas sans allergie clinique aux autres légumineuses. Rev Fr Allergol Immunol Clin 2002;42:348 ↩
[17] - Mazeyrat-Nelissen R. Anaphylaxie au lupin révélant une allergie alimentaire potentielle à l'arachide. Alim'Inter 2002;7:20-21 ↩
[18] - Mazeyrat R, Ponvert C, Thibault M, Asensi D. Sensibilisation à la farine de lupin: risque pour l'enfant allergique à l'arachide. Rev Fr Allergol Immunol Clin 2004;44:133 ↩
[19] - Smith WB, Gillis D, Kette FE. Lupin: a new hidden food allergen. Med J Aust 2004;181:219-220 ↩
[21] - Wassenberg J, Hofer M. Lupine-induced anaphylaxis in a child without known food allergy. Ann Allergy Asthma Immunol 2007;98:589-590
BACKGROUND: Lupine allergy is caused by ingestion of the flour of a plant called Lupinus albus, a member of the Leguminosae family. Lupine allergy has been described in adult patients previously known to have peanut allergy (cross-reactivity). OBJECTIVE: To describe the first case of an anaphylactic reaction caused by ingestion of lupine flour in a pediatric patient without a known peanut allergy.
METHODS: Symptom assessment, nutritional history, and skin and blood tests.
RESULTS: An otherwise healthy 8-year-old boy had nose and eye discharge followed by facial edema and difficulty breathing 30 minutes after eating an industrially prepared waffle containing eggs, sugar, and lupine flour. He had no history of food allergy and was eating a normal diet, including peanuts and other legumes. Results of skin prick tests using commercial extracts were positive to peanuts and negative to eggs, soy, and nuts; results of a prick-to-prick test using lupine flour were strongly positive (+ + + +). His total IgE level was 1,237 UI/mL. Specific IgE antibodies were positive to lupine seeds (20.8 kU/L) and peanuts (> 100 kU/L).
CONCLUSIONS: To our knowledge, we describe the first case of an anaphylactic reaction after ingestion of lupine flour in a child without known allergy. In the case of peanut allergy or any anaphylactic reaction without evident cause, especially after industrially prepared food ingestion, lupine should be considered in the list of allergens tested. Lupine is increasingly used in industrially prepared food but is not regularly declared in the composition, leading to difficulties in allergen avoidance.
↩[22] - Quaresma RR, Viseu R, Martins LM, Tomaz E, Inacio F. Allergic primary sensitization to lupine seed. Allergy 2007;62:1473-1474 ↩
[23] - Wüthrich B. Anaphylactic reaction to lupine flour because of a primary sensitization. Allergy 2008;63:476-477 ↩
[24] - Sánchez Alonso A, Méndez Alcalde JD. Allergy to sausages. Alergol Immunol Clin 2000;15:211-215 ↩
[25] - Lecacheux C, Jokic M, Andro MC, Denis A, Moneret-Vautrin DA. Asthme aigu mortel par allergie au soja. Alim'Inter 2002;7:14-16 ↩
[26] - Holzhauser T, Petrovskaya O, Kuehne Y, Wangorsch A, Ballmer-Weber B, Bindslev-Jensen C, et al. Allergenicity of soybean beta-conglycinin versus Gly m Bd 30k in patients with confirmed soybean allergy. EAACI 25th Congress, Vienna, 10-14 June, 2006, Poster n°513
Background: Soybean b-conglycinin and Gly m Bd 30k have been described as IgE-binding proteins, the latter one as putative major soybean allergen.
We aimed at characterising both soybean proteins in regard to their relevance in a European patient group with confirmed soybean allergy.
Methods: Twenty-five adults were included into the study on the basis of a positive DBPCFC or conclusive history of anaphylaxis to soy. Twenty-two children were included upon positive DBPCFC or open oral challenge. Natural b-conglycinin subunits (a, a', b) were extracted from soybean, recombinant subunits expressed in E.coli, and both purified by continuous-elution electrophoresis. Natural Gly m Bd 30k was enriched by an oleosin fractionation of soybean and the recombinant homologue expressed as His-tagged fusion protein in E.coli and purified by IMAC. Protein identity was proven by N-terminal sequencing and/or peptide mass fingerprinting. IgE-reactivity of the purified soy proteins was investigated by IgE-immunoblotting and/or IgE-ELISA with patients' sera. ELISA- and EAST-inhibition, and mediator release from passively sensitized humanized rat basophilic leukaemia cells was performed with selected patients' sera.
Results: b-conglycinin was IgE-reactive in 54 % (12/22) of the children and 20 % (5/25) of the adults. By contrast, enriched natural Gly m Bd 30k bound IgE from less than 50 % of patients‚ sera in immunoblotting, and rGly m Bd 30k did not show any IgE-reactivity. In ELISA-inhibition, IgE-binding to b- conglycinin was fully inhibited by soybean extract and itself. IgE-reactivity to b-conglycinin was almost fully inhibited by peanut extract and purified Ara h 1 in a soybean and peanut allergic patient, however hardly inhibited in a patient allergic to soybean but not to peanut. Similar results were obtained in EAST-inhibition with soybean extract on the solid surface. Specific mediator release confirmed the cross-linking properties of b-conglycinin.
Conclusion: In Europe, soybean b-conglycinin is a major allergen for soy-allergic children and an important minor allergen in adults, whereas the relevance of Gly m Bd 30k in IgE-mediated soybean allergy remains unclear and demands further investigation. In some patients cross-reactivity between peanut and soybean is limited.
↩[27] - Hummel D, Gold M. Reactions to soy protein isolate in patients with peanut allergy. Allergy 2007;62(suppl. 83):25
Introduction: Peanut allergy is common in North America. A number of peanut allergic patients subsequently experience other allergic reactions. We report a group of peanut allergic patients who, despite tolerating most soy products, reacted to foods containing soy protein isolate (SPI). SPI is made from defatted soy meal. Most of the fats and carbohydrates have been removed, yielding a product with 90 percent protein which is often added for increased protein content or improved stability to the food. This concentrated form of protein, and the method by which this is processed, may alter the allergenicity of the soybean.
Methods: Twenty four patients M:F 15:9 with a clinical reaction to both peanut and soy products containing SPI are reported. The initial reaction to peanut occurred between the ages 7 months to 5 years (mean 2.1 yrs). Subsequent reactions to SPI occurred 3 to 25 years later (mean 9 years). Foods containing SPI included the following: tofu, hamburgers, soy butter, soy drinks, hotdogs, pepperoni pizza, chicken fingers, bologna, and fortified energy bar. Skin prick testing (SPT) for SPI was done with soy isolate powder (Supro®) diluted 1:1w/v with normal saline along with commercial peanut and soy bean extracts (1:10). In vitro measurement for IgE was done by ImmunoCAP Results: Reactions to SPI included the following: oropharyngeal symptoms 33% (8/24); gastrointestinal manifestations 13% (3/24); urticaria/angioedema 13% (3/24); respiratory involvement 13% (3/24); generalized allergic reactions* 29% (7/24) (*Two or more systems involved). All patients had positive SPT responses to both peanut and SPI. The SPT for the soy extract were either negative or significantly smaller than the soy isolate preparation in all cases. All individuals had positive ImmunoCAP responses (1-100 kU/L) to peanut and soybean extract.
Conclusions: Peanut allergic patients are at increased risk of developing allergic reactions to foods containing SPI despite previously having tolerated soybean in other forms. It is important to recognize this group of patients, especially because they may not be identified when the commercial allergen extract for soybean is used. We recommend using SPT with soy isolate powder together with in vitro measurements of specific IgE to soy if this condition is suspected.
↩[28] - Bernhisel-Broadbent J, Sampson HA. Cross-allergenicity in the legume botanical family in children with food hypersensitivity. J Allergy Clin Immunol 1989;83:435-440
Sixty-nine patients with one or more positive prick skin tests to legumes (peanut, soybean, green bean, pea, and lima bean) were evaluated for food hypersensitivity with in-hospital oral food challenges. Of the 280 prick skin tests to legumes performed, 130 were positive. Forty-three positive food challenges occurred in 41 patients. The prevalence of legume allergy was not statistically different in those patients (N = 36) with two or more positive legume prick skin test (64% positive) compared to those patients (N = 33) with only one positive legume prick skin test (55% positive; p greater than 0.10). Even in this selected patient population, only two patients had symptomatic hypersensitivity to two legumes. Among patients with a positive prick skin test to peanut (N = 60), the mean wheal size was larger in patients with a positive versus a negative oral food challenge to peanut (p less than 0.001). Results of oral food challenges demonstrate that clinically important cross-reactivity to legumes in children is very rare. Clinical hypersensitivity to one legume does not warrant dietary elimination of all legumes. Results of prick skin tests should not be used to determine prolonged food restriction diets
↩[29] - Patil SP, Niphadkar PV, Bapat MM. Allergy to fenugreek (Trigonella foenum graeccum). Ann Allergy Asthma Immunol 1997;78:297-300
BACKGROUND: Allergic reactions after consumption of spices are well-known. In Asia, fenugreek seeds are consumed as spices and also as medicines. Literature survey carried out does not reveal reports of allergic reactions to fenugreek.
In our survey carried out on patients with food allergy, we found two cases of severe allergy to fenugreek.
METHODS: We report here two cases of immediate allergy following ingestion, inhalation, and external application of fenugreek seed powder. In the first case, inhalation of the fenugreek seed powder resulted in rhinorrhea, wheezing, and fainting. The second case was of a patient with chronic asthma who developed numbness of head, facial angioedema, and wheezing after application of fenugreek paste to her scalp as a treatment for dandruff.
Skin scratch test was performed with fenugreek and other members of the Leguminosae family as fenugreek also belongs to Leguminosae. Objective evidence of the reaction was obtained by conducting double-blind placebo-controlled challenges (DBPCFC). For detecting IgE binding by immunoblotting method, the proteins of the fenugreek extract were resolved using sodium dodecyl sulphate polyacrylamide gel electrophoresis.
RESULTS: Skin scratch tests for the patients revealed strong sensitivity to fenugreek and chickpeas. None of the controls showed such response with fenugreek extract. During DBPCFC, both patients showed > 20% drop in peak flow rate after consumption of fenugreek and chickpea.
Immunoblots demonstrated binding of specific IgE from the patients' sera with the protein from extracts between 20 kD to 70 kD bands. CONCLUSION: This case report has enlarged the list of food allergens with the addition of fenugreek.
↩[30] - Patil SP, Niphadkar PV, Bapat MM. Chickpea: a major food allergen in the Indian subcontinent and its clinical and immunochemical correlation. Ann Allergy Asthma Immunol 2001;87:140-145
BACKGROUND: The food allergy pattern of a country is influenced by the foods most commonly consumed. In India, the majority of the population consumes a vegetarian diet made up of pulse (legumes), cereals, and vegetables. In contrast to many western countries, chickpea preparations are consumed in large quantities in India. This study reports for the first time chickpea hypersensitivity reactions diagnosed with in vivo and in vitro tests.
METHODS: One thousand four hundred patients visiting allergy clinics were randomly selected for the study. Those patients reporting an allergic reaction on every occasion after eating chickpea were considered history-positive. Modified prick tests were performed with chickpea and other members of the legume family on all these patients. The claims of the history-positive patients were verified with double-blind, placebo-controlled food challenges (DBPCFCs). Proteins in chickpea extracts were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and transferred on nitrocellulose paper. Serum specimens from history-positive patients were analyzed by immunoblot and ELISA. To verify the IgE specificity, an immunoblot inhibition assay was also performed.
RESULTS: Of the 1,400 patients screened, 142 patients were history-positive to some food and 59 of these implicated chickpeas. Forty-one patients were skin test-positive and 31 were DBPCFC-positive for chickpea. The predominant symptoms after chickpea ingestion were respiratory. The ELISA results did not correlate well with the DBPCFC results; however, the skin test results correlated with DBPCFC in 75% of patients. Immunoblot analysis showed that 70, 64, 35, and 26 kD proteins were major allergens.
CONCLUSIONS: Chickpea is an important source of allergen that can cause IgE-mediated hypersensitivity reactions ranging from rhinitis to anaphylaxis
↩[31] - Wensing M, Knulst AC, Piersma S, O’Kane F, Knol EF, Koppelman SJ. Patients with anaphylaxis to pea can have peanut allergy caused by crossreactive IgE to vicilin (Ara h 1). J Allergy Clin Immunol 2003;111:420-424
BACKGROUND: Serologic cross-reactivity among legumes has been described; however, it is rarely clinically significant. In this study 3 patients with a history of anaphylaxis to pea are described who subsequently had symptoms after ingestion of peanut .
OBJECTIVE: We investigated whether the peanut-related symptoms were due to cross-reactivity between pea and peanut proteins .
METHODS: Peanut-related symptoms were documented according to case history or double-blind, placebo-controlled food challenge results. Skin prick tests were performed, and specific IgE levels were determined for pea and peanut with the CAP system FEIA. IgE-binding proteins in pea and peanut were identified by using immunoblot analysis. Cross-reactivity was studied by means of immunoblot and ELISA inhibition studies with whole extracts and purified allergens .
RESULTS: Peanut-related symptoms consisted of oral symptoms in all patients, with additional urticaria and dyspnea or angioedema in 2 patients. All patients had a positive skin prick test response and an increased IgE level to pea and peanut. Immunoblotting revealed strong IgE binding to mainly vicilin in pea extract and exclusively to Ara h 1 in crude peanut extract. Immunoblot and ELISA inhibition studies with crude extracts, as well as purified proteins, showed that IgE binding to peanut could be inhibited by pea but not or only partially the other way around .
CONCLUSION: Clinically relevant cross-reactivity between pea and peanut does occur. Vicilin homologues in pea and peanut (Ara h 1) are the molecular basis for this cross-reactivity.
↩[32] - López-Torrejón G, Salcedo G, Martín-Esteban M, Díaz-Perales A, Pascual CY, Sánchez-Monge R. Len c 1, a major allergen and vicilin from lentil seeds: Protein isolation and cDNA cloning. J Allergy Clin Immunol 2003;112:1208-1215
BACKGROUND: Lentils are among the main plant foods causing allergic reactions in pediatric patients in the Mediterranean area and in many Asian communities. However, very few reports have been devoted to identifying lentil allergens. Seed storage proteins of the vicilin family have been characterized as major allergens in several seed legumes and tree nuts .
OBJECTIVE: We sought to evaluate the role of lentil vicilins as food allergens .
METHODS: A serum pool and individual sera from 22 patients with lentil allergy were used in different IgE-binding assays. Mature lentil vicilin was isolated by means of cation-exchange chromatography, followed by reverse-phase HPLC, and characterized by means of N-terminal amino acid sequencing, matrix-assisted laser desorption/ionization mass spectrometry (MALDI) analysis, complex asparagine-linked glycan detection, specific IgE immunodetection with individual sera, and ELISA inhibition assays. Complete cDNAs encoding lentil vicilin variants were isolated by means of PCR with primers based on the amino acid sequence of the allergen .
RESULTS: A major IgE-binding component of approximately 50 kd was detected in lentil extracts. This component was isolated and characterized, showing a single N-terminal amino acid sequence homologous to those of legume vicilins and a broad peak (maximum at 48613 d) in MALDI analysis. The purified allergen was recognized by 77% (17/22) of the individual sera from patients with lentil allergy and reached up to 65% inhibition of the IgE binding to the crude lentil extract. The allergen showed 3 isoforms varying in their degree of N-glycosylation. Two cDNA clones encoding different allergen variants were isolated. The amino acid sequences deduced from both clones (415 and 418 residues; 47.4 and 47.8 kd) showed greater than 50% identity with major peanut (Ara h 1) and soybean (conglutinin subunits) allergens belonging to the vicilin family. Furthermore, these sequences included those of the previously characterized lentil allergen Len c 1.02 (108 amino acid residues of the C-terminal domain) and those of a novel lentil IgE-binding protein of 26 kd .
CONCLUSION: The mature 48-kd lentil vicilin, designated Len c 1.01, is a major allergen. Two of its processing fragments, corresponding to subunits of 12 to 16 kd (previously named Len c 1) and 26 kd, are also relevant lentil IgE-binding proteins. The sequence homology of Len c 1.01 to those of major allergens from peanut, soybean, walnut, and cashew can help to investigate potential cross-reactions among these plant foods.
↩[33] - Armentia A, Barber D, Lombardero M, Martin Santos JM, Martin Gil FJ, Arranz Pena ML, et al. Anaphylaxis associated with antiphospholipid syndrome. Ann Allergy Asthma Immunol 2001;87:54-59
BACKGROUND: To our knowledge, no previously published reports have described food-induced anaphylaxis associated with the antiphospholipid syndrome. OBJECTIVE: We undertook a study of four patients with thrombosis associated with the antiphospholipid syndrome after each patient experienced anaphylaxis attributable to ingestion of vegetal foods.
METHODS: IgE antibody levels to various foods were determined in serum specimens from the study patients, and skin prick tests with the same allergens were conducted to determine their in vivo responses. Hematologic, cardiopulmonary, vascular, and rheumatologic studies were also performed. IgG anticardiolipin antibody levels were determined by ELISA.
RESULTS: All four patients fulfilled the criteria for antiphospholipid syndrome and had high levels of specific IgE antibodies for certain food allergens. By immunoblot analysis, the presence of serum IgE specific for a 45-kD protein band in an almond extract was detected in these four patients who experienced food-related anaphylaxis. No specific IgE was detected in sera from normal subjects. No IgE antibodies specific for the food panallergen lipid transfer proteins were detected.
CONCLUSIONS: This is the first report of severe food-precipitated anaphylaxis associated with the antiphospholipid syndrome and the first description of a patient with allergy to blackberry. The possible involvement of food panallergens distinct from lipid transfer proteins is also discussed
↩[34] - Sanchez-Monge R, Lopez-Torrejon G, Pascual CY, Varela J, Martin-Esteban M, Salcedo G. Vicilin and convicilin are potential major allergens from pea. Clin Exp Allergy 2004;34:1747-1753
BACKGROUND: Allergic reactions to pea (Pisum sativum) ingestion are frequently associated with lentil allergy in the Spanish population. Vicilin have been described as a major lentil allergen .
OBJECTIVE: To identify the main IgE binding components from pea seeds and to study their potential cross-reactivity with lentil vicilin .
METHODS: A serum pool or individual sera from 18 patients with pea allergy were used to detect IgE binding proteins from pea seeds by immunodetection and immunoblot inhibition assays. Protein preparations enriched in pea vicilin were obtained by gel filtration chromatography followed by reverse-phase high-performance liquid chromatography (HPLC). IgE binding components were identified by means of N-terminal amino acid sequencing. Complete cDNAs encoding pea vicilin were isolated by PCR, using primers based on the amino acid sequence of the reactive proteins .
RESULTS: IgE immunodetection of crude pea extracts revealed that convicilin (63 kDa), as well as vicilin (44 kDa) and one of its proteolytic fragments (32 kDa), reacted with more than 50% of the individual sera tested. Additional proteolytic subunits of vicilin (36, 16 and 13 kDa) bound IgE from approximately 20% of the sera. The lentil vicilin allergen Len c 1 strongly inhibited the IgE binding to all components mentioned above. The characterization of cDNA clones encoding pea vicilin has allowed the deduction of its complete amino acid sequence (90% of sequence identity to Len c 1), as well as those of its reactive proteolytic processed subunits .
CONCLUSIONS: Vicilin and convicilin are potential major allergens from pea seeds. Furthermore, proteolytic fragments from vicilin are also relevant IgE binding pea components. All these proteins cross-react with the major lentil allergen Len c 1.
↩[35] - Branco Ferreira M, Pedro E, Meneses Santos J, Pereira dos Santos MC, Palma Carlos ML, Bartolome B, et al. Latex and chickpea (Cicer arietinum) allergy: first description of a new association. Eur Ann Allergy Clin Immunol 2004;36:366-371
In this paper we describe the existence of cross-reactivity between allergens from latex and chickpea, a food from the Leguminosae family, which is common in the Mediterranean diet. We present the case report of a spina bifida boy with a clinical relevant food allergy to chickpea (oral syndrome + dysphonia), developing after the appearance of latex allergy symptoms (lip angioedema + intraoperative anaphylaxis). Specific IgE to latex and chickpea was demonstrated by skin prick tests, measurement of patient's serum specific IgE and IgE-immunoblotting. Cross-reactivity was studied by means of EAST-inhibition and western blotting-inhibition. A strong inhibition was observed in several IgE-binding bands when latex extract was used in solid phase and patient serum was preincubated with chickpea extract (chickpea extract as inhibitor phase). As far as we know, this is the first report of cross-reactivity between latex and chickpea, a food which should therefore be added to the extensive list of latex cross-reactive foods.
↩[36] - Martin JA, Compaired JA, de la Hoz B, Quirce S, Alonso MD, Igea JM, et al. Bronchial asthma induced by chick pea and lentil. Allergy 1992;47:185-187
Allergic reactions to legumes through inhalation have rarely been described. We report the case of a 20-year-old man who experienced asthmatic attacks when exposed to the steam from cooking either chick pea or lentil. Type I hypersensitivity to the antigens in these legumes was demonstrated by means of immediate skin reactivity, histamine release tests, RAST and RAST inhibition. Specific bronchial challenges with the heated (75 degrees for 30 min) extracts of chick pea and lentil elicited isolated immediate responses.
↩[37] - Nicolie B, Leduc V, Drouet M. Allergie alimentaire croisée entre les graines de fenugrec (Trigonella foenum-graecum) et d’arachide. Rev Fr Allergol Immunol Clin 2007;47:283 ↩
[38] - Campina Costa S, Neto M, Trindade M, Bartolome B, Campos Melo A, Pereira Santos MC. Anaphylaxis to fava bean (Vicia fava). Allergy 2007;62(suppl. 83):369
Background: Legume allergy is frequent in Mediterranean countries where their consumption is common and may cause life-threatening reactions in sensitized individuals. They contain multiple allergens with a significant degree of cross-reactivity among different species. It has been suggested that legume allergens are heat-stable and sensitive to the action of acids and enzymes. There is little information about allergy to other legumes besides peanut and soybean. Fava bean (Fb) belongs to the Papilionaceae family of the Fabales botanical order, and until now few data has been published on Fb allergy. We report the clinical case of a 34-year-old woman who suffered from anaphylactic reactions after fresh Fb ingestion. Methods: Skin prick test (SPT) was performed with extracts from common pollens and with Fb, beans, pea, chick-pea, lentil, peanut and soybean (Bial Aristegui®). Prick-prick test was performed to fresh and fronzen Fb, on its raw and boiled forms. Total IgE and specific IgE to these legumes were determined by UniCAP Pharmacia® method. Specific IgE to Fb was measured by enzyme allergo-sorbent test (EAST) and molecular mass of the IgE binding proteins was determined by SDS-PAGE IgE-Immunoblotting assay, (Bial Aristegui®). Glucose 6-phosphate dehydrogenase (G6PD) was measured. Basophil activation test (BAT), using IgE/CD63 double labelling was performed using serial dilution of Fb extract (Bial Aristegui®), and was evaluated by flow-citometry (FACSCALIBUR, Bectan Dickinson). Oral challenge (OC) with boiled frozen and fresh Fb was also carried out. Results: SPT, prick-prick test, specific IgE to Fb as well as to the other legumes tested were all negative. Immunoblotting to Fb did not reveal any IgE-binding band. Total serum IgE was 88,6 kU/L. G6PD was 8,16 UI/gHb. For a stimulation concentration of 2mg/ml Fb extract expression of CD63 above spontaneous expression was <5%, stimulation index <2. OC was positive with boiled fresh Fb however it was negative with boiled frozen Fb. Conclusion: we present a case of anaphylactic reaction after ingestion of fresh Fb. Neither SPT nor specific IgE were able to confirm an IgE mediated mechanism. OC was the unique useful test for the diagnosis of legume allergy in this case, the process of freezing could be responsible for altering the allergenicity of the allergens. The usefulness of BAT as a tool for investigating allergy to Fb is discussed.
↩[39] - Mur Gimeno P, Feo Brito F, Martin Iglesias A, Lombardero Vega M, Bautista Martinez P. Allergic reaction caused by a new hidden food, broad bean flour. Allergy 2007;62:1340-1341 ↩
[40] - Bernhisel-Broadbent J, Sampson HA. Cross-allergenicity in the legume botanical family in children with food hypersensitivity. J Allergy Clin Immunol 1989;83:435-440
Sixty-nine patients with one or more positive prick skin tests to legumes (peanut, soybean, green bean, pea, and lima bean) were evaluated for food hypersensitivity with in-hospital oral food challenges. Of the 280 prick skin tests to legumes performed, 130 were positive. Forty-three positive food challenges occurred in 41 patients. The prevalence of legume allergy was not statistically different in those patients (N = 36) with two or more positive legume prick skin test (64% positive) compared to those patients (N = 33) with only one positive legume prick skin test (55% positive; p greater than 0.10). Even in this selected patient population, only two patients had symptomatic hypersensitivity to two legumes. Among patients with a positive prick skin test to peanut (N = 60), the mean wheal size was larger in patients with a positive versus a negative oral food challenge to peanut (p less than 0.001). Results of oral food challenges demonstrate that clinically important cross-reactivity to legumes in children is very rare. Clinical hypersensitivity to one legume does not warrant dietary elimination of all legumes. Results of prick skin tests should not be used to determine prolonged food restriction diets
↩[41] - Barnett D, Bonham B, Howden ME. Allergenic cross-reactions among legume foods: an in vitro study. J Allergy Clin Immunol 1987;79:433-438
The specific IgE binding by protein extracts of 11 food legumes, including soybean, was examined by RAST and RAST inhibition. Sera from 15 peanut-sensitive patients were, with very few exceptions, positive in the RAST to all the legumes. RAST-inhibition testing of each extract against RAST discs of the other legumes indicated considerable cross-reactivity of IgE binding between the legumes. Cross-allergenicity was demonstrated to be most marked between the extracts of peanut, garden pea, chick pea, and soybean. The results have important implications for selection of effective hypoallergenic diets and for the diagnosis of patients hypersensitive to foods.
↩[42] - Peeters KABM, Koppelman SJ, Penninks AH, Lebens A, Bruijnzeel-Koomen CAFM, Hefle SL et al. Clinical relevance of sensitization to lupine in peanut-sensitized adults. Allergy 2009;64:549-555
BACKGROUND: The use of lupine in food has been increasing during the last decade and allergic reactions to lupine have been reported, especially in peanut-allergic patients. The frequency and the degree of cross-reactivity to other legumes are not known. The aim of the study was to investigate the frequency of sensitization to lupine, and in addition to pea and soy, and its clinical relevance, in peanut-sensitized patients. Furthermore, to determine the eliciting dose (ED) for lupine using double-blind placebo-controlled food challenges (DBPCFC) .
METHODS: Thirty-nine unselected peanut-sensitized patients were evaluated by skin prick tests (SPT) and ImmunoCAP to lupine, pea, and soy. Clinical reactivity was measured by DBPCFC for lupine, and by history for pea and soy .
RESULTS: Eighty-two percent of the study population was sensitized to lupine, 55% to pea, and 87% to soy. Clinically relevant sensitization to lupine, pea, or soy occurred in 35%, 29%, and 33% respectively of the study population. None of the patients was aware of the use of lupine in food. The lowest ED for lupine, inducing mild subjective symptoms, was 0.5 mg, and the no observed adverse effect level (NOAEL) was 0.1 mg. No predictive factors for lupine allergy were found .
CONCLUSION: In peanut-sensitized patients, clinically relevant sensitization to either lupine or to pea or soy occurs frequently. The ED for lupine is low (0.5 mg), which is only fivefold higher than for peanut. Patients are not aware of lupine allergy and the presence of lupine in food, indicating that education is important to build awareness.
↩[43] - Rancé F, Abbal M, Lauwers-Cancès V. Improved screening for peanut allergy by the combined use of skin prick tests and specific IgE assays. J Allergy Clin Immunol 2002;109:1027-1033
BACKGROUND: The diagnosis of peanut allergy must be based on reliable, safe criteria. Double-blind, placebo-controlled food challenges (DBPCFCs) are the gold standard but are costly and dangerous because they can trigger severe reactions .
OBJECTIVE: The aim of this study was to develop a new strategy for diagnosing peanut allergy while reducing the need for DBPCFCs .
METHODS: We studied 363 children referred for an evaluation of suspected food hypersensitivity. They all benefited from the same diagnostic strategy, which included, in order, clinical history, a skin prick test (SPT), and a specific IgE assay. DBPCFCs were performed on all the children by personnel who were unaware of the results of the other tests. To assess the performance characteristics of the SPT (comparing commercial and raw peanut extracts) and the specific IgE assay, we compared the results with those provided by the DBPCFCs. For SPTs and specific IgE assays, we sought to determine the cutoff values required to exclude false-positive and false-negative results .
RESULTS: According to DBPCFC results, 177 children were allergic to peanut, and 186 were not. The performance characteristics of the SPTs were superior with the raw extract because the negative predictive value was 100% (95% confidence interval [CI], 97.5-100). If the skin reaction with the raw extract was less than 3 mm, we could be quite certain that the child was not allergic. On the other hand, if the SPT resulted in a wheal diameter of larger than 3 mm, we could only be 74% certain that the children were allergic. Furthermore, if the SPT resulted in a wheal diameter of 16 mm or larger, we could be quite certain that the child was allergic because the positive predictive value was 100% (95% CI, 86.8-100). Specific IgE concentrations of 57 kU(A)/L or greater were associated with a positive predictive value of 100% (95% CI, 87.2-100). The combined use of the tests resulting in a positive diagnosis if the SPT result was 16 mm or larger or specific IgE concentration was 57 kU(A)/L or greater and in a negative diagnosis if the SPT result was less than 3 mm and the specific IgE concentration was less than 57 kU(A)/L allowed us to classify subjects with almost complete certainty as being allergic or not because the predictive values were 100% .
CONCLUSION: Commercial extracts could not be used to reliably predict tolerance of peanut. Peanut DBPCFCs can be avoided when SPTs with raw extracts resulted in wheals with a largest diameter of less than 3 mm and a specific IgE concentration of less than 57 kU(A)/L and also when wheal diameters were 16 mm or larger or specific IgE values were 57 kU(A)/L or greater. Otherwise, DBPCFCs were indispensable for the unequivocal diagnosis of peanut allergy.
↩[44] - Holzhauser T, Petrovskaya O, Kuehne Y, Wangorsch A, Ballmer-Weber B, Bindslev-Jensen C, et al. Allergenicity of soybean beta-conglycinin versus Gly m Bd 30k in patients with confirmed soybean allergy. EAACI 25th Congress, Vienna, 10-14 June, 2006, Poster n°513
Background: Soybean b-conglycinin and Gly m Bd 30k have been described as IgE-binding proteins, the latter one as putative major soybean allergen.
We aimed at characterising both soybean proteins in regard to their relevance in a European patient group with confirmed soybean allergy.
Methods: Twenty-five adults were included into the study on the basis of a positive DBPCFC or conclusive history of anaphylaxis to soy. Twenty-two children were included upon positive DBPCFC or open oral challenge. Natural b-conglycinin subunits (a, a', b) were extracted from soybean, recombinant subunits expressed in E.coli, and both purified by continuous-elution electrophoresis. Natural Gly m Bd 30k was enriched by an oleosin fractionation of soybean and the recombinant homologue expressed as His-tagged fusion protein in E.coli and purified by IMAC. Protein identity was proven by N-terminal sequencing and/or peptide mass fingerprinting. IgE-reactivity of the purified soy proteins was investigated by IgE-immunoblotting and/or IgE-ELISA with patients' sera. ELISA- and EAST-inhibition, and mediator release from passively sensitized humanized rat basophilic leukaemia cells was performed with selected patients' sera.
Results: b-conglycinin was IgE-reactive in 54 % (12/22) of the children and 20 % (5/25) of the adults. By contrast, enriched natural Gly m Bd 30k bound IgE from less than 50 % of patients‚ sera in immunoblotting, and rGly m Bd 30k did not show any IgE-reactivity. In ELISA-inhibition, IgE-binding to b- conglycinin was fully inhibited by soybean extract and itself. IgE-reactivity to b-conglycinin was almost fully inhibited by peanut extract and purified Ara h 1 in a soybean and peanut allergic patient, however hardly inhibited in a patient allergic to soybean but not to peanut. Similar results were obtained in EAST-inhibition with soybean extract on the solid surface. Specific mediator release confirmed the cross-linking properties of b-conglycinin.
Conclusion: In Europe, soybean b-conglycinin is a major allergen for soy-allergic children and an important minor allergen in adults, whereas the relevance of Gly m Bd 30k in IgE-mediated soybean allergy remains unclear and demands further investigation. In some patients cross-reactivity between peanut and soybean is limited.
↩[45] - Wensing M, Knulst AC, Piersma S, O’Kane F, Knol EF, Koppelman SJ. Patients with anaphylaxis to pea can have peanut allergy caused by crossreactive IgE to vicilin (Ara h 1). J Allergy Clin Immunol 2003;111:420-424
BACKGROUND: Serologic cross-reactivity among legumes has been described; however, it is rarely clinically significant. In this study 3 patients with a history of anaphylaxis to pea are described who subsequently had symptoms after ingestion of peanut .
OBJECTIVE: We investigated whether the peanut-related symptoms were due to cross-reactivity between pea and peanut proteins .
METHODS: Peanut-related symptoms were documented according to case history or double-blind, placebo-controlled food challenge results. Skin prick tests were performed, and specific IgE levels were determined for pea and peanut with the CAP system FEIA. IgE-binding proteins in pea and peanut were identified by using immunoblot analysis. Cross-reactivity was studied by means of immunoblot and ELISA inhibition studies with whole extracts and purified allergens .
RESULTS: Peanut-related symptoms consisted of oral symptoms in all patients, with additional urticaria and dyspnea or angioedema in 2 patients. All patients had a positive skin prick test response and an increased IgE level to pea and peanut. Immunoblotting revealed strong IgE binding to mainly vicilin in pea extract and exclusively to Ara h 1 in crude peanut extract. Immunoblot and ELISA inhibition studies with crude extracts, as well as purified proteins, showed that IgE binding to peanut could be inhibited by pea but not or only partially the other way around .
CONCLUSION: Clinically relevant cross-reactivity between pea and peanut does occur. Vicilin homologues in pea and peanut (Ara h 1) are the molecular basis for this cross-reactivity.
↩[46] - Moneret-Vautrin DA, Guérin L, Kanny G, Flabbee J, Frémont S, Morisset M. Cross-allergenicity of peanut and lupine: the risk of lupine allergy in patients allergic to peanuts. J Allergy Clin Immunol 1999;104:883-888
BACKGROUND: Peanut allergy is common, but cross-allergy between legumes is rare. Proteins from Lupinus albus are increasingly eaten in the form of seeds or additives to wheat flour. The risk of cross-allergenicity is still insufficiently known .
OBJECTIVE: We sought to study the risk of cross-allergy to lupine in patients allergic to peanut and to study lupine allergenicity .
METHODS: Twenty-four patients allergic to peanuts were studied by means of skin prick tests with native lupine flour from Lupinus albus. Double-blind oral challenge tests were performed with lupine flour and peanut in 8 of these patients. Specific IgEs were assayed for peanut, lupine flour, and pollen in 6 sera. RAST inhibition tests for lupine pollen by peanut were performed on 4 of these sera. Peanut and lupine flour immunoblots were carried out for 6 sera, and crossed immunoblot inhibitions for peanut by lupine flour and lupine flour by peanut were carried out for 2 sera .
RESULTS: The skin prick test responses with lupine flour were positive in 11 (44%) subjects. The challenge test responses were positive in 7 of 8 subjects at the same doses as with peanut. The major lupine flour allergen (molecular mass, 43 kd) is present in peanuts. The RAST inhibition and immunoblot tests indicated cross-reactivity of peanut with the lupine flour and pollen .
CONCLUSIONS: The risk of crossed peanut-lupine allergy is high, contrary to the risk with other legumes. The inclusion of 10% lupine flour in wheat flour without mandatory labeling makes lupine a hidden allergen, presenting a major risk of cross-reaction in subjects already allergic to peanut products. A high sensitizing potential can also be postulated for this legume.
↩[47] - Peeters KABM, Nordlee JA, Penninks AH, Chen L, Goodman RE, Bruijnzeel-Koomen CAFM, et al. Lupine allergy: Not simply cross-reactivity with peanut or soy. J Allergy Clin Immunol 2007;120:647-653
BACKGROUND: Reports of lupine allergy are increasing as its use in food products increases. Lupine allergy might be the consequence of cross-reactivity after sensitization to peanut or other legumes or de novo sensitization. Lupine allergens have not been completely characterized .
OBJECTIVES: We sought to identify allergens associated with lupine allergy, evaluate potential cross-reactivity with peanut, and determine eliciting doses (EDs) for lupine allergy by using double-blind, placebo-controlled food challenges .
METHODS: Six patients with a history of allergic reactions to lupine flour were evaluated by using skin prick tests, CAP tests, and double-blind, placebo-controlled food challenges. Three of these patients were also allergic to peanut. Lupine allergens were characterized by means of IgE immunoblotting and peptide sequencing .
RESULTS: In all 6 patients the ED for lupine flour was 3 mg or less for subjective symptoms and 300 mg or more for objective symptoms. The low ED and moderate-to-severe historical symptoms indicate significant allergenicity of lupine flour. Two patients allergic to lupine but not to peanut displayed IgE binding predominantly to approximately 66-kd proteins and weak binding to 14- and 24-kd proteins, whereas patients with peanut allergy and lupine allergy showed weak binding to lupine proteins of about 14 to 21 or 66 kd. Inhibition of binding was primarily species specific .
CONCLUSION: Lupine allergy can occur either separately or together with peanut allergy, as demonstrated by 3 patients who are cosensitized to peanut and lupine. CLINICAL IMPLICATIONS: Lupine flour is allergenic and potentially cross-reactive with peanut allergen, thus posing some risk if used as a replacement for soy flour.
↩[48] - Matheu V, de Barrio M, Sierra Z, Gracia-Bara MT, Tornero P, Baeza ML. Lupine-induced anaphylaxis. Ann Allergy Asthma Immunol 1999;83:406-408
Legumes are one of the most common foods causing allergic reactions in children and adults. Cross-reacting antibodies are frequently demonstrated in this family but the real clinical cross-reactivity is uncommon. OBJECTIVE: To report a case of lupine-induced anaphylaxis and to elucidate in vivo and in vitro cross-reactivity with some legumes.
METHODS: Skin prick test (SPT) with some legumes were performed. Cap-IgE, ELISA-IgE, and immunoblotting were carried out. Open oral challenges with some legumes were performed. Cross-reactivity was studied by ELISA and immunoblotting inhibition.
RESULTS: The results demonstrated type-I hypersensitivity reactions with lupine and some other legumes. Cap-IgE with peanut was positive but the SPT and ELISA-IgE were negative and the patient tolerated a peanut challenge. ELISA inhibition revealed a partial inhibition (62%) using lupine as the solid phase. Partial inhibition was demonstrated by immunoblotting inhibition. Open oral challenge with peanut and green bean were negative but positive with pea. CONCLUSION: We present a lupine sensitized patient with positive SPT and in vitro cross-reactivity with other legumes. Clinical cross-reactivity progressively developed over a 5-year period. Discrepancies were found between the clinical aspect and in vitro study of peanut allergy. Factors determining the wide variability in cross-reactivity among individuals are still obscure.
↩[49] - Parisot L, Aparicio C, Moneret-Vautrin DA, Guérin L. Allergy to lupine flour. Allergy 2001;56:918-919 ↩
[50] - Quaresma RR, Viseu R, Martins LM, Tomaz E, Inacio F. Allergic primary sensitization to lupine seed. Allergy 2007;62:1473-1474 ↩
[51] - Wüthrich B. Anaphylactic reaction to lupine flour because of a primary sensitization. Allergy 2008;63:476-477 ↩
[52] - Cid Sanchez AB, Pascual C.Y, Letran Camacho A, Osorio Galindo A , Sanchez Pastor S, Martin Esteban M. Cross-reactivity between lupine and other legumes. Allergy Clin Immunol Int 2005;17(Suppl. 1):349
Background: Peanut and soybean are the two major legumes involved in food allergy in the United States and the United Kingdom. However, the lentils and chickpeas are the most frequent in the Mediterranean area and many Asian countries. Lupine (Lupinus Albus) another member of legume family is eaten in the form of seeds or as flour used to enrich pasta.
Objective: We sought to study the cross-reactivity between lupine, lentils, peanut and soybean.
Methods: Serum samples were obtained from 25 children (age range, 1 to 11 years) with a history of adverse reactions and sensitization in vitro to lentils.
None of children referred symptoms with lupine o derived products. Specific IgE levels to legumes were quantified by using the CAP-FEIA System (Pharmacia Diagnostic). The SDS-PAGE Immunoblot-inhibition was performed for crude legumes.
Results: 17 was male and 8 female. The most frequent symptoms were oral allergy syndrome (32%) and acute urticaria (48% patients). One patient presented anaphylactic reaction with lentils.
14 patients had allergic reactions to other legumes: 7 at chick peas; 5 at peas and chick peas; 2 at peas. The 64% had sensitization to peanut. Lupine immunoblots with sera from 25 patients allergic to lentils revealed reactive IgE bands between 8 and 67 kD. All sera bind bands at 30, 43, 54 and 67 kD. A 22 kD band was recognized by 92%.
Inhibition of the lupine immunoblots: - By lentils: total in 72% of sera. All the sera had completely inhibited the bands at 14, 20, 22, 43 and 67 kD.
- By soybean: total in 52% of sera and in the rest, the bands are not inhibited at 67, 50, 43, 34, 30, 20, 17 kD.
- By peanut: the inhibition of bands is partial (not inhibited at 67, 43, 30, 17 and 8 kD). The 12 patients with pollinosis did not show special band patterns.
Conclusion: Immunoblot inhibition showed high degree cross-reactivity between lupine and other legumes, particularly with lentils.
↩[53] - Peeters KABM, Nordlee JA, Penninks AH, Chen L, Goodman RE, Bruijnzeel-Koomen CAFM, et al. Lupine allergy: Not simply cross-reactivity with peanut or soy. J Allergy Clin Immunol 2007;120:647-653
BACKGROUND: Reports of lupine allergy are increasing as its use in food products increases. Lupine allergy might be the consequence of cross-reactivity after sensitization to peanut or other legumes or de novo sensitization. Lupine allergens have not been completely characterized .
OBJECTIVES: We sought to identify allergens associated with lupine allergy, evaluate potential cross-reactivity with peanut, and determine eliciting doses (EDs) for lupine allergy by using double-blind, placebo-controlled food challenges .
METHODS: Six patients with a history of allergic reactions to lupine flour were evaluated by using skin prick tests, CAP tests, and double-blind, placebo-controlled food challenges. Three of these patients were also allergic to peanut. Lupine allergens were characterized by means of IgE immunoblotting and peptide sequencing .
RESULTS: In all 6 patients the ED for lupine flour was 3 mg or less for subjective symptoms and 300 mg or more for objective symptoms. The low ED and moderate-to-severe historical symptoms indicate significant allergenicity of lupine flour. Two patients allergic to lupine but not to peanut displayed IgE binding predominantly to approximately 66-kd proteins and weak binding to 14- and 24-kd proteins, whereas patients with peanut allergy and lupine allergy showed weak binding to lupine proteins of about 14 to 21 or 66 kd. Inhibition of binding was primarily species specific .
CONCLUSION: Lupine allergy can occur either separately or together with peanut allergy, as demonstrated by 3 patients who are cosensitized to peanut and lupine. CLINICAL IMPLICATIONS: Lupine flour is allergenic and potentially cross-reactive with peanut allergen, thus posing some risk if used as a replacement for soy flour.
↩[54] - Peeters KABM, Nordlee JA, Penninks AH, Chen L, Goodman RE, Bruijnzeel-Koomen CAFM, et al. Lupine allergy: Not simply cross-reactivity with peanut or soy. J Allergy Clin Immunol 2007;120:647-653
BACKGROUND: Reports of lupine allergy are increasing as its use in food products increases. Lupine allergy might be the consequence of cross-reactivity after sensitization to peanut or other legumes or de novo sensitization. Lupine allergens have not been completely characterized .
OBJECTIVES: We sought to identify allergens associated with lupine allergy, evaluate potential cross-reactivity with peanut, and determine eliciting doses (EDs) for lupine allergy by using double-blind, placebo-controlled food challenges .
METHODS: Six patients with a history of allergic reactions to lupine flour were evaluated by using skin prick tests, CAP tests, and double-blind, placebo-controlled food challenges. Three of these patients were also allergic to peanut. Lupine allergens were characterized by means of IgE immunoblotting and peptide sequencing .
RESULTS: In all 6 patients the ED for lupine flour was 3 mg or less for subjective symptoms and 300 mg or more for objective symptoms. The low ED and moderate-to-severe historical symptoms indicate significant allergenicity of lupine flour. Two patients allergic to lupine but not to peanut displayed IgE binding predominantly to approximately 66-kd proteins and weak binding to 14- and 24-kd proteins, whereas patients with peanut allergy and lupine allergy showed weak binding to lupine proteins of about 14 to 21 or 66 kd. Inhibition of binding was primarily species specific .
CONCLUSION: Lupine allergy can occur either separately or together with peanut allergy, as demonstrated by 3 patients who are cosensitized to peanut and lupine. CLINICAL IMPLICATIONS: Lupine flour is allergenic and potentially cross-reactive with peanut allergen, thus posing some risk if used as a replacement for soy flour.
↩[55] - Sanchez-Monge R, Lopez-Torrejon G, Pascual CY, Varela J, Martin-Esteban M, Salcedo G. Vicilin and convicilin are potential major allergens from pea. Clin Exp Allergy 2004;34:1747-1753
BACKGROUND: Allergic reactions to pea (Pisum sativum) ingestion are frequently associated with lentil allergy in the Spanish population. Vicilin have been described as a major lentil allergen .
OBJECTIVE: To identify the main IgE binding components from pea seeds and to study their potential cross-reactivity with lentil vicilin .
METHODS: A serum pool or individual sera from 18 patients with pea allergy were used to detect IgE binding proteins from pea seeds by immunodetection and immunoblot inhibition assays. Protein preparations enriched in pea vicilin were obtained by gel filtration chromatography followed by reverse-phase high-performance liquid chromatography (HPLC). IgE binding components were identified by means of N-terminal amino acid sequencing. Complete cDNAs encoding pea vicilin were isolated by PCR, using primers based on the amino acid sequence of the reactive proteins .
RESULTS: IgE immunodetection of crude pea extracts revealed that convicilin (63 kDa), as well as vicilin (44 kDa) and one of its proteolytic fragments (32 kDa), reacted with more than 50% of the individual sera tested. Additional proteolytic subunits of vicilin (36, 16 and 13 kDa) bound IgE from approximately 20% of the sera. The lentil vicilin allergen Len c 1 strongly inhibited the IgE binding to all components mentioned above. The characterization of cDNA clones encoding pea vicilin has allowed the deduction of its complete amino acid sequence (90% of sequence identity to Len c 1), as well as those of its reactive proteolytic processed subunits .
CONCLUSIONS: Vicilin and convicilin are potential major allergens from pea seeds. Furthermore, proteolytic fragments from vicilin are also relevant IgE binding pea components. All these proteins cross-react with the major lentil allergen Len c 1.
↩[56] - Bjerremann Jensen L, Torp AM, Pedersen MH, Skov PS, Poulsen LK, Bindslev-Jensen C, et al. Legume sprouts might pose a risk for peanut allergic patients. Allergy 2007;62(suppl. 83):105-106
Imprimer la bibliographieBackground Peanut allergic patients are often advised to avoid all legumes in their diet. Studies have shown that despite an observed in vitro cross-reactivity this does not necessarily reflect a clinically relevant reaction. This might be due to degradation of allergens during cooking. A relatively new source of protein in especially vegetarian meals is legume sprouts, which are often consumed raw and peanut allergic patients have reported symptoms upon ingestion. In this study we report that sera from peanut allergic patients cross-react to extracts of legume sprouts.
Methods Crude extracts of seeds and hypocotyls (part of embryo located below cotyledon attachment) / epicotyls (shoot of embryo above cotyledon) from peanut, soybean, pea, lupine, mung, alfalfa, broad bean and azuki were prepared. Stripped human blood basophils were passively sensitized with sera from 10 peanut allergic patients or a healthy control. The cells were challenged with the legume extracts in 6 concentrations. The released histamine was measured spectrofluorometrically (RefLab). The protein concentration resulting in 20% histamine release (HR) was used as a measure for biologic activity. Enzyme-allergosorbent test (EAST) was performed with MaxisorpTM microtiterplates coated with legume extracts (2µg/ml) and developed by HRP-conjugated anti-human-IgE. Direct EAST was performed with 3 patient sera and inhibition experiments using plates coated with peanut were performed with 8 patient sera. Cutoff was 15% inhibition.
Results Histamine release (HR) experiments indicated an extensive co-reactivity between peanut and the legumes. Most sensitive was lupine, followed by soybean and pea. Surprisingly, hypocotyls/epicotyls from pea, lupine, mung, alfalfa, broad bean, and azuki were more sensitive than the corresponding seeds. Only peanut gave OD>0.1 in direct EAST. EAST inhibition experiments showed that lupine seeds could inhibit peanut reaction with up to 63%, soybean seeds up to 56%, and pea seeds up to 60%. Lupine hypocotyl was the only sprout able to inhibit >15%. Interestingly, lower concentrations of lupine hypocotyl were necessary to induce inhibition compared to lupine seed.
Conclusion Patient sera recognize legume seeds and sprouts in vitro. Interestingly, the sprout extracts were more potent than the seeds in HR. The symptoms reported by peanut allergic patients after legume sprout intake might therefore be caused by cross-reactivity.
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