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La châtaigne
mercredi 14 avril 2010, par
Cet aliment est consommé de façon variable selon les pays.
Par exemple, la châtaigne représente la 3e cause d’allergie alimentaire en Corée. Et dans une série de patients portugais allergiques au latex, la châtaigne arrive devant la banane ou l’avocat 
.
En France, le Réseau d’Allergo-Vigilance a noté l’inverse : 4 cas pour la châtaigne contre 8 pour l’avocat et 8 pour la banane (cf. tableau des déclarations du RAV).
Classiquement, la châtaigne est rattachée au "syndrôme latex-fruits" (cf. latex et aliments). Mais d’autres étiologies sont possibles comme en témoignent les cas d’allergie à la châtaigne sans allergie au latex (8 cas/15 dans la série de Rico ).
La châtaigne peut d’abord se distinguer du kiwi, de l’avocat, etc… sur le plan botanique : l’aliment est ici constitué de la graine et non d’un mésocarpe. En ce sens la châtaigne serait plus proche de la noix ou de l’arachide.
Par exemple, parmi 8 patients positifs en TPODA pour la châtaigne, une étude a montré que 2 étaient TPODA positifs pour la noix et 1 pour le tournesol .
De fait, en plus de sa chitinase Cas s 5, la châtaigne renferme une LTP allergénique (Cas s 8) comme beaucoup d’autres graines.
La châtaigne pourrait aussi contenir une PR-10 IgE-réactive à l’image du couple noisette-noisetier (Cor a 1.04 et Cor a 1.01). Une réactivité croisée châtaigne- châtaignier a été notée , faisant supposer une sensibilisation à la châtaigne induite par ce pollen, lequel contient comme le bouleau et le noisetier une PR-10 (Cas s 1).
Cette communauté moléculaire au sein des Fagales pourrait expliquer aussi l’observation d’une réaction croisée châtaigne-gland de chêne même si les allergènes homologues ne semblent pas être des PR-10.
D’autres protéines pourraient avoir un rôle dans l’allergénicité de la châtaigne, au premier rang desquels une profiline qui n’a pas été identifiée IgE-réactive pour le moment.
Une étude récente apporte pourtant crédit à une profiline IgE-réactive dans la châtaigne . Parmi 19 patients positifs in vitro pour la châtaigne et le latex, 6 s’avéraient mono-réactifs à Hev b 8 (profiline du latex). Ce qui est une observation peu courante.
De plus la châtaigne inhibait le latex chez ces sujets mais pas chez ceux qui, classiquement, étaient positifs pour Hev b 6.01 (pro-hévéine).
En analysant les résultats de cette étude, on peut remarquer que les patients qui avaient une histoire clinique positive pour la châtaigne (n=10) pouvaient être séparés en 2 groupes très distincts,
– soit réactivité pour Hev b 8 et syndrome oral,
– soit réactivité pour Hev b 6.01 et angio-œdème ou anaphylaxie.
Cette cohorte rassemblait donc 2 étiologies : des sujets avec syndrome latex-aliment et des sujets avec sensibilisation profilinique (très vraisemblablement d’origine pollinique). La profiline pourrait donc avoir une relevance clinique pour la châtaigne chez certains patients.
Une cystatine est présente et rappelle qu’une autre cystatine est un allergène dans le kiwi (Act d 4).
Enfin une chitinase de classe 2 a donné des résultats contradictoires , mais globalement ne semble pas avoir d’impact allergénique.
La question principale au sujet de la châtaigne reste donc la part prise par la LTP Cas s 8 dans les réactions cliniques et dans l’origine de la sensibilisation à la châtaigne.
La dissociation châtaigne-latex a été repérée avant tout en Espagne :
- sur 14 tests cutanés positifs châtaigne, seulement 2 sont positifs pour le latex
- parmi 22 patients allergiques à la châtaigne (TPODA ou anaphylaxie) seulement 59 % des tests cutanés sont positifs pour le latex .
Du fait de l’environnement pollinique particulier (absence de bouleaux, importance des sensibilisations aux herbacées), le rôle d’une sensibilisation pollen-induite a été évoqué. Au premier rang des pollens incriminés vient l’armoise, celle-ci possédant une LTP allergénique (Art v 3) :
- 100 % de tests cutanés châtaigne positifs si armoise positive
- 11 sujets/12 positifs pour la LTP de châtaigne (Cas s 8) en même temps que 10/12 avec un test cutané armoise positif .
Il a donc été retenu comme plausible un effet de la sensibilisation à l’armoise sur la réactivité à la châtaigne à travers des LTP .
Cela va-t-il jusqu’à une allergie pollen-induite comme pour la pomme et le bouleau ?
Il est difficile d’en décider car, dans le même temps, la "pression allergénique" de la pêche est certaine dans un pays comme l’Espagne. Ainsi, Blanco trouvait aussi que tous les sujets positifs Cas s 8 étaient sensibilisés à la pêche .
Au total, le rôle des pollens contenant des LTP (armoise, olivier, platane) n’est peut-être qu’additionnel à celui de la pêche (et/ou des fruits sensibilisant aux LTP).
La sélection des patients positifs (voire allergiques) à la châtaigne parmi des sujets LTP+ peut simplement résulter d’un état atopique plus prononcé, boostant des réactivités habituellement non décelables.
Au niveau du diagnostic in vitro, on ne possède pas pour le moment d’allergène purifié ou recombinantde châtaigne en routine.
Il faudra se méfier des CCD. Par exemple, dans une étude japonaise sur l’arachide, un CAP châtaigne positif était vu chez 2 des 10 enfants allergiques à l’arachide contre 6 des 7 enfants avec un CAP arachide positif mais non allergiques à l’arachide .
[1] - Gaspar A, Raulf-Heimsoth M, Pires G, Rihs HP, Yeang HY, Matos V, et al. Latex allergen sensitization patterns in different risk groups and latex-fruit syndrome patients from Portugal. EAACI 23th Congress, Amsterdam, 12-16 June, 2004, Poster n°1188
Background: Latex allergy has been recognized as a clinically important health problem, mainly in some risk groups: spina bifida (SB), other congenital malformations submitted to multiple surgeries (MS) and health care workers (HCW).
Purpose: To study IgE-binding reactivity to latex allergens, by using recombinant and natural allergens, in latex-allergic patients from different risk groups including patients with latex-fruit syndrome (LFS).
Material and Methods: We selected sera of 51 latex-allergic patients within different risk groups: 20 with SB, 10 MS and 21 HCW; all these patients had positive skin prick tests with commercial latex extract (ALK-Abelló) and serum latex-specific IgE determined by UniCAP®(Pharmacia Diagnostics). Sixteen out of the 51 patients had LFS. A panel of single recombinant latex allergens was coupled to ImmunoCAPs (CAP system®) and the isolated natural allergen nHev b 2 was coupled on paper disks (EAST testing). This panel comprised rHev b 1, nHev b 2, rHev b 3, rHev b 5, rHev b 6.01, rHev b 7, rHev b 8, rHev b 9, rHev b 10 and rHev b 11. The recombinant allergens were produced as fusion protein with maltose-binding protein (MBP) in E. coli. MBP coupled on ImmunoCAPs served as control. Specific IgE values of >0.35kU/l were considered positive. Major allergen is defined if produces a positive IgE response in more than 50% of the tested group.
Results: Recombinant Hev b 1 specific IgE antibodies were detected in 70% sera from SB, 30% from MS, 5% from HCW, and in 13% sera from LFS patients. For nHev b 2: SB-69%, MS-71%, HCW-71% and LFS-75%. For rHev b 3: SB-50%, MS-20%, HCW-10% and LFS-13%. For rHev b 5: SB-55%, MS-40%, HCW-62% and LFS-75%. For rHev b 6.01: SB-45%, MS-30%, HCW-76% and LFS-81%. For rHev b 7: SB-33%, MS-0%, HCW-16% and LFS-27%. For rHev b 8: SB-10%, MS-0%, HCW-5% and LFS-6%. For rHev b 9 and rHev b 10: SB-0%, MS-0%, HCW-5% and LFS-7%. For rHev b 11: SB-7%, MS-0%, HCW-5% and LFS-7%.
Conclusions: The different routes of exposure influence the IgE antibody pattern. The major latex allergens identified in SB were Hev b 1, Hev b 2, Hev b 3 and Hev b 5, being Hev b 1 the most important one. The major allergen identified in MS was Hev b 2. For occupational exposure route, the major latex allergens identified in HCW were Hev b 2, Hev b 5 and Hev b 6.01, being prohevein the most important one. Regarding cross-reactivity with foods, the major allergens identified in LFS were Hev b 2, Hev b 5 and Hev b 6.01.
↩[2] - Rodriguez M, Vega F, Garcia MT, Panizo C, Laffond E, Montalvo A, et al. Hypersensitivity to latex, chestnut, and banana. Ann Allergy 1993;70:31-34
The incidence of latex-allergic patients is probably higher than suspected. A spectrum of IgE-dependent allergic reactions to latex products including urticaria, rhinitis, asthma, angioedema, and life-threatening anaphylaxis has been increasingly reported in recent years. We describe three patients with rubber hypersensitivity and allergy to fruit (banana and chestnut). Immediate positive responses were obtained in prick tests with latex, banana, and chestnut extracts. Histamine release was positive and specific IgE antibodies to all three extracts were detected by fluorescence radioimmunoassay. In the RAST-inhibition studies, the extract of latex inhibited the binding of chestnut and banana, but chestnut and banana extracts did not inhibit the binding of latex. These results suggest a sensitivity to crossreacting antigens in latex allergy associated with allergy to certain fruits.
↩[3] - Rico P, Somoza ML, Feliu A, Jimenez A, Crespo JF, Rodriguez J. Clinical features of chestnut allergy objectively confirmed by double-bind pacebo-controlled food challenges (DBPCFC's). EAACI 22th Congress, Paris, 7-11 June, 2003, Poster n°134
Background: Chestnuts (Castanea sativa) belong to the Fagaceae family, genus Castanea. Sensitization to chestnut has been reported in patients with other allergies, particularly in the 'atex-fruit syndrome' However, few studies have focused on chestnut allergy confirmed by DBPCFC‚s. We sought to analyze the clinical features of adult patients with objectively confirmed chestnut allergy.
Methods: Fifteen adult patients diagnosed with chestnut allergy were included in this study. Case histories were evaluated following the diagnostic protocol of the Food Allergy Unit from ŒHospital Universitario 12 de Octubre'; including a detailed clinical history, skin testing by the prick-prick method with fresh foods, and detection of food specific serum IgE (CAP-FEIA, Pharmacia, Uppsala, Sweden). Clinical reactivity to foods was assessed first by open food challenges (OFCs), unless a convincing history of a recent severe anaphylaxis. Positive OFCs reactions were subsequently evaluated by DBPCFCs. All negative results of DBPCFC's were followed by a final open feeding.
Results: The age of chestnut adverse reactions ranged from 15 to 70 years (median=28). The most common symptoms were systemic anaphylaxis (47%), isolated oral symptoms (27%), and generalized acute urticaria (14%). Interestingly, the results of allergy testing (both SPT and detection of specific IgE) were negative in 5 out of 15 patients with clinical reactivity to chestnut. Forty-nine reactions to other 13 different foods of vegetable origin were confirmed by DBPCFCs in patients with chestnut allergy, including banana (6 out of 15 patients), avocado (5/15 pt.) and kiwi (4/15 pt.). In addition, 7 out of 15 (47%) patients having clinical allergy to chestnut were found to be allergic to latex.
Conclusions: Systemic anaphylaxis is a common clinical feature associated to adverse reactions after chestnut ingestion. Latex-associated allergy is found in nearly half of patients reacting to chestnut ingestion. Allergy testing is a poor predictor of clinical reactivity to chestnut.
↩[4] - Rodriguez J, Poza P, Crespo JF. Follow-Up of Immunological Reactivity in 27 Patients Allergic to Nuts and Seeds. J Allergy Clin Immunol 2005;115(2 suppl.):S94
RATIONALE: There is limited information on the natural course of patients with positive skin testing and/or CAP FEIA to peanuts and/or tree nuts, but clinical tolerance. We evaluated if immunological reactivity to nuts developed into clinical reactivity over time
METHODS: Twenty-seven patients (median= 25 yr.) with proven clinical allergy (DBPCFC procedure) to nuts [almond (AL), 3 patients; hazelnut (HN), 13; peanut (PN), 6; chestnut (ChN), 8; walnut (WN), 12; pistachio (P), 2; and sunflower seed (S), 6] were included in the study. Patients underwent skin prick testing and specific IgE determinations (CAP-FEIA) to other nuts with proven tolerance and, if positive, new clinical reactivity to nuts was assessed by phone interview, followed by oral provocations Median follow-up (months) was: AL, 51.5; HZ, 49.5; PN, 43; ChN, 38; WN, 65.5; P, 44.5; and S, 42
RESULTS: A total of 89 immunologic reactivities to nuts were detected (17 to AL, 7 to HZ, 17 to PN, 16 to ChN, 12 to WN, 10 to P, and 11 to S) After the follow- up period, 24 patients (80 immunologic reactions) could be contacted by telephone (89% participants). They reported intentional avoidance of 26 nuts (33%); ingestion with tolerance of 53 nuts (66%), and eating with symptoms to 1 nut (WN) (1%). A further clinical evaluation including DBPCFC confirmed one new case of clinical allergy to WN
CONCLUSIONS: Patients clinically reactive to a nut have also an extensive immunologic reactivity to other nuts, which could be safely consumed, as new cases of clinical allergy seem to be infrequent
↩[5] - Lee SK, Yoon SH, Kim SH, Choi JH, Park HS. Chestnut as a food allergen: identification of major allergens. J Korean Med Sci 2005;20:573-578
Chestnut as a Food Allergen: Identification of Major Allergens To evaluate the clinical significance of chestnut as a food allergen in Korea, skin prick test and ELISA were done in 1,738 patients with respiratory allergies. To identify the IgE binding components, IgE-immunoblotting, 2D IgE-immunoblotting and MALDITOF were performed. To observe the effects of digestive enzymes and a boiling treatment, simulated gastric fluid (SGF) and simulated intestinal fluids (SIF) were incubated with chestnut extracts, and IgE-immunoblotting were then repeated. Skin prick test revealed that 56 (3.2%) patients showed more than 2+ of allergen to histamine ratio to chestnut. Among the 21 IgE binding components, 9 bands were found in more than 50% of the sera tested and the 24 kDa protein had the highest binding intensity. The amino acid sequence of the 24 kDa protein (pI 6.3) had homology with legume protein of oak tree. SGF, SIF and boiling treatment were able to suppress the IgE binding components. In conclusion, chestnut ingestion was shown to induce IgE mediated responses with a 3.2% sensitization rate. Twenty one IgE binding components and one new allergen (the 24 kDa protein) were identified. Digestive enzymes and boiling treatment were able to decrease the allergenic potency.
↩[6] - Zapatero L, Baeza ML, Z. Sierra Z, Molero MIM. Anaphylaxis by fruits of the Fagaceae family: acorn and chestnut. Allergy 2005;60:1542 ↩
[7] - Raulf-Heimsoth M, Kespohl S, Crespo JF, Rodriguez J, Feliu A, Brüning T, et al. Natural rubber latex and chestnut allergy: cross-reactivity or co-sensitization ? Allergy 2007;62:1277-1281
BACKGROUND: Chestnut and natural rubber latex (NRL) allergy are often associated in the latex-fruit syndrome. AIM OF THE STUDY: To establish whether the concurrent NRL and chestnut IgE antibody reactivity are the results of co-sensitization or cross-reactivity .
METHODS: Sera from 19 patients with chestnut- and NRL-specific IgE were selected and tested for reactivity with recombinant (r) latex allergens. Cross-reactivity was explored by IgE-inhibition experiments using chestnut or NRL allergens as solid phase on ImmunoCAP .
RESULTS: IgE-antibodies were detected to rHev b 6.01 (prohevein) in 58% of the sera, to rHev b 5 in 32%, to rHev b 12 in four of 13 sera, to rHev b 7.02 and rHev b 11 in four, and to rHev b 1 in two of 19 sera. rHev b 8-IgE antibodies were found in nine sera (47%), whereas six displayed mono-sensitization to rHev b 8 with regard to our test panel. Three of 16 sera showed IgE to cross-reactive carbohydrate determinants. In most sera recognizing rHev b 5 and/or rHev b 6.01 as major allergens the IgE-reactivity to NRL remained unaffected by chestnut extract and chestnut-IgE remained unaffected by NRL extract. Conversely, in sera with rHev b 8 as dominant allergen IgE-binding to NRL was nearly completely inhibited by chestnut and vice versa. IgE-binding to rHev b 8 was abolished by chestnut extract .
CONCLUSIONS: Although patients have concomitant IgE antibody reactivity to chestnut and NRL, cross-reactivity could be demonstrated mainly in those patients with IgE to Hev b 8 (profilin) from NRL.
↩[8] - Pernas M, Sanchez-Monge R, Salcedo G. Biotic and abiotic stress can induce cystatin expression in chestnut. FEBS Lett 2000;467:206-210
A cysteine proteinase inhibitor (cystatin) from chestnut (Castanea sativa) seeds, designated CsC, has been previously characterized. Its antifungal, acaricide and inhibitory activities have allowed to involve CsC in defence mechanisms. The CsC transcription levels decreased during seed maturation and increased throughout germination, an opposite behavior to that shown by most phytocystatins. No inhibition of endogenous proteinase activity by purified CsC was found during the seed maturation or germination processes. CsC message accumulation was induced in chestnut leaves after fungal infection, as well as by wounding and jasmonic acid treatment. Induction in roots was also observed by the last two treatments. Furthermore, CsC transcript levels strongly raised, both in roots and leaves, when chestnut plantlets were subjected to cold- and saline-shocks, and also in roots by heat stress. All together, these data suggest that chestnut cystatin is not only involved in defence responses to pests and pathogen invasion, but also in those related to abiotic stress.
↩[9] - Diaz-Perales A, Collada C, Blanco C, Sanchez-Monge R, Carrillo T, Aragoncillo C, et al. Class I chitinases with hevein-like domain, but not class II enzymes, are relevant chestnut and avocado allergens. J Allergy Clin Immunol 1998;102:127-133
BACKGROUND: Several foods associated with the latex-fruit syndrome present relevant allergens of around 30 kd. Neither these components nor any other responsible for the reported cross-reactions have been identified and purified. OBJECTIVE: We sought to isolate and characterize the 30 kd allergens from avocado fruit and chestnut seed, two of the main allergenic foods linked with latex allergy.
METHODS: Sera from patients allergic to chestnut and avocado were selected according to clinical symptoms, specific IgE levels, and positive skin prick test responses. Class I and II chitinases were purified by affinity and cation-exchange chromatography and characterized by specific IgE and anti-chitinase immunodetection, immunoblot inhibition assays, enzymatic activity tests, and N-terminal sequencing.
RESULTS: Relevant 32 kd allergens were detected by specific IgE immunodetection in both avocado and chestnut crude extracts. The same bands, together with others of 25 kd, were revealed by a monospecific antiserum against class II chitinases. Purification and characterization of the 32 kd allergens from both plant sources allowed their identification as class I chitinases with an N-terminal hevein-domain. The purified allergens fully inhibited IgE binding by the corresponding crude extract when tested in immunoblot inhibition assays. Highly related 25 kd class II chitinases that lack the hevein-like domain were also isolated from the same protein preparations. No IgE-binding capacity was shown by these class II enzymes. CONCLUSION: Class I chitinases are relevant allergens of avocado and chestnut and could be the panallergens responsible for the latex-fruit syndrome. The hevein-like domain seems to be involved in their allergenic reactivity.
↩[10] - Blanco C, Diaz-Perales A, Collada C, Sanchez-Monge R, Aragoncillo C, Castillo R, et al. Class I chitinases as potential panallergens involved in the latex-fruit syndrome. J Allergy Clin Immunol 1999;103:507-513
BACKGROUND: Latex-fruit cross-sensitization has been fully demonstrated.
However, the antigens responsible for this "latex-fruit syndrome" have not been identified. We have recently shown that class I chitinases are relevant chestnut and avocado allergens. OBJECTIVE: We sought to evaluate the in vivo and in vitro reactions of purified chestnut and avocado chitinases in relation to the latex-fruit syndrome.
METHODS: From a latex-allergic population, eighteen patients allergic to chestnut, avocado, or both were selected. Skin prick tests (SPTs) were performed with crude chestnut and avocado extracts, chitinase-enriched preparations, and purified class I and II chitinases from both fruits. CAP-inhibition assays with the crude extracts and purified proteins were carried out.
Immunodetection with sera from patients with latex-fruit allergy and immunoblot inhibition tests with a latex extract were also performed.
Eighteen subjects paired with our patients and 15 patients allergic to latex but not food were used as control groups.
RESULTS: The chestnut class I chitinase elicited positive SPT responses in 13 of 18 patients with latex-fruit allergy (72%), and the avocado class I chitinase elicited positive responses in 12 of 18 (67%) similarly allergic patients. By contrast, class II enzymes without a hevein-like domain did not show SPT responses in the same patient group. Each isolated class I chitinase reached inhibition values higher than 85% in CAP inhibition assays against the corresponding food extract in solid phase. Immunodetection of the crude extracts and the purified class I chitinases revealed a single 32-kd band for both chestnut and avocado. Preincubation with a natural latex extract fully inhibited the IgE binding to the crude extracts, as well as to the purified chestnut and avocado class I chitinases. CONCLUSION: Chestnut and avocado class I chitinases with an N-terminal hevein-like domain are major allergens that cross-react with latex. Therefore they are probably the panallergens responsible for the latex-fruit syndrome.
↩[11] - Dìaz-Perales A, Sánchez-Monge R, Blanco C, Lombardero M, Carillo T, Salcedo G. What is the role of the hevein-like domain of fruit class I chitinases in their allergenic capacity ? Clin Exp Allergy 2002;32:448-454
Class I chitinases are the major panallergens in fruits associated with the latex-fruit syndrome. These enzymes contain an N-terminal hevein-like domain homologous to latex hevein, and a larger catalytic domain. The role of these domains in their allergenic capacity is still controversial.
Objective : We sought to evaluate the role of both domains of class I chitinases in their IgE-binding properties, using Cas s 5, the major allergen from chestnut, as a model.
Method s : Recombinant Cas s 5 and its deleted form, lacking the hevein-like domain, designated rCat, were expressed in Pichia pastoris using the pPIC 9 vector. Both recombinant products were purified from the supernatants of transformed yeast cultures by gel-filtration and cation-exchange chromatography. The isolated proteins were characterized by N-terminal sequencing, enzymatic activity and N-glycosylation tests, anti-chitinase and specific IgE immunodetection. Immunoblot, RAST and CAP inhibition assays were also performed.
Result s : Both purified rCas s 5 and rCat showed the expected N-terminal amino acid sequences and an enzymatic activity similar to that of their natural counterparts isolated from chestnut seeds, and were strongly recognized by anti-chitinase antibodies. In contrast, only rCas s 5, but not rCat, bound specific IgE from sera of patients suffering from the latex-fruit syndrome, and fully inhibited IgE-binding to natural Cas s 5 in immunoblot inhibition assays. Latex hevein also exerted a strong immunoblot inhibition of IgE-binding to chestnut Cas s 5. RAST and CAP inhibition using whole chestnut extract on the solid phase, rendered inhibition levels around 70-90% for rCas s 5 and 60% for rCat, in contrast to the immunoblotting results.
Conclusions : Recombinant Cas s 5 behaves like natural Cas s 5 in IgE-binding assays in vitro. The hevein-like domain of allergenic class I chitinases seems to include all their main IgE-binding epitopes when tested by immunodetection and immunoblot inhibition experiments. RAST and CAP inhibition assays, on the contrary, suggest that relevant epitopes are also harboured in the catalytic domain of these allergens.
↩[12] - Rodriguez J, Crespo JF, Burks W, Rivas-Plata C, Fernández-Anaya S, Vives R, et al. Randomized, double-blind, crossover challenge study in 53 subjects reporting adverse reactions to melon (Cucumis melo). J Allergy Clin Immunol 2000;106:968-972
BACKGROUND: Few studies have evaluated IgE-mediated hypersensitivity to melon with details of clinical reactions confirmed by double-blind, placebo-controlled, food challenges (DBPCFCs). OBJECTIVE: We sought to investigate clinical features (type and severity of reactions, age at onset, results of skin prick and in vitro tests, and incidence of other allergic diseases and associated food allergies) of acute allergic reactions to melon confirmed by DBPCFCs.
METHODS: Fifty-three consecutive adult patients complaining of adverse reactions to melon were included in the study. Skin prick tests and detection of specific IgE were performed in all patients with melon, avocado, kiwi, banana, chestnut, latex, pollen, and other offending foods. Patients first underwent an open food challenge, unless they had a convincing history of severe anaphylaxis. Positive open food challenge reactions were subsequently evaluated by DBPCFCs.
RESULTS: Actual clinical reactivity was confirmed in 19 (36%) of 53 patients. The most frequent symptom was oral allergy syndrome (n = 14), but two patients experienced life-threatening reactions, including respiratory symptoms and hypotension. The positive predictive value for a skin prick test was 42%, and that for specific IgE measurement was 44%. Forty-five reactions to 15 other foods were confirmed in 18 patients. The most common foods associated with melon allergy were avocado (n = 7), banana (n = 7), kiwi (n = 6), watermelon (n = 6), and peach (n = 5). Onset of melon-induced allergic symptoms occurred from 6 to 45 years (median, 20 years), preceded by seasonal rhinitis, asthma, or both in 88% (15/17). CONCLUSION: About one third of reported reactions to melon are confirmed by means of DBPCFC, which has been proven to be the most reliable procedure in the diagnosis of clinical fruit allergy. Isolated melon allergy is rare, with most patients either having allergic rhinitis, asthma, or both and associated food allergies.
↩[13] - Rico P, Crespo JF, Feliu A, Rodriguez J. Chestnut Allergy: Beyond the Latex-Fruit Syndrome. AAAAI 60th Annual Meeting, San Francisco, 19-23 March 2004, Poster n°494
Rationale Allergy to chestnuts has been widely reported in the latex-fruit syndrome. However, few studies address actual allergy to chestnuts in patients reacting primarily to this food. We report a case series of chestnut-allergic patients to find out clinical and immunologic features. Methods Twenty-two consecutive subjects proven to be clinically reactive to chestnut by a positive DBPCFC result or a convincing history of anaphylaxis were included in the study. Patients underwent SPTs with chestnut, banana, avocado, kiwi, melon, peanut, walnut, hazelnut, latex and aeroallergens, as well as specific IgE determinations. Relevant allergy to the other foods was established by the DBPCFC method. Results The age of onset of reactions to chestnut ranged from 5 to 70 yr. (median=28 yr.), with 8/22 (36%) patients having experienced severe anaphylactic episodes. SPTs with chestnut were positive in 71% and specific IgE was detected in 54% of patients. Besides, 86% and 59% of patients had also positive responses to pollen and latex allergens, respectively. Eighteen patients had actual allergy to other foods; mainly banana, 45% of patients; avocado, 40%; and hazelnut, 32%. There was a significant association between sensitization to latex and clinical reactivity to avocado and/or kiwi (p<0.01); while reactivity to hazelnut was associated with allergy to peanut (p=0.003) and walnut (p<0.001). Conclusion One third of the chestnut-allergic patients experience severe anaphylactic episodes on ingestion. Chestnut reactivity is frequently associated to actual clinical allergy not only to fruits, but also to other tree nuts.
↩[14] - García-Sellés FJ, Díaz-Perales A, Sánchez-Monge R, Alcántara M, Lombardero M, Barber D, et al. Patterns of reactivity to lipid transfer proteins of plant foods and Artemisia pollen: an in vivo study. Int Arch Allergy Immunol 2002;128:115-122
Background: Lipid transfer proteins (LTPs) are major allergens of Rosaceae fruits in the Mediterranean area. IgE-cross-reactivity has been demonstrated in vitro among LTPs from peach, apple, chestnut and Artemisia pollen. The aim of this study was to evaluate the reactivity to LTPs from peach, apple, chestnut and Artemisia pollen by means of skin prick tests (SPTs).
Methods: Forty-seven patients allergic to peach (peach group), 20 patients sensitized to Artemisia pollen with no food allergies (Artemisia group), and 12 control subjects were skin tested with fresh peach, as well as with whole extracts and purified LTPs of peach, apple, chestnut and Artemisia pollen.
Results: The rates of positive SPTs for peach, apple, chestnut and Artemisia LTPs were, respectively, 91, 77, 23, and 36% in the peach group, and 30, 5, 15 and 40% in the Artemisia group. No response was observed in the control subjects. SPTs with peach LTP strongly correlated with SPTs conducted with fresh peach. In the peach group, the most frequent pattern of reactivity to LTPs was the combination peach-apple (45%), followed by peach-apple-Artemisia-chestnut (21%). Significant correlations were found between peach and apple LTPs, and between Artemisia and chestnut LTPs. Positive SPTs to chestnut LTP were only observed in patients with positive SPTs to Artemisia LTP. All the patients with positive case histories to chestnut reacted to chestnut LTP.
Conclusions: LTPs are plant panallergens with different patterns of cross-reactivity. They are major allergens of Rosaceae fruits and seem to be involved in allergic reactions to unrelated foodstuffs such as chestnut, probably through sensitization to the cross-reactive Artemisia LTP. Rosaceae LTPs could be useful tools for in vivo diagnosis of Rosaceae fruit allergy.
↩[15] - Sanchez-Monge R, Blanco C, Lopez-Torrejon G, Cumplido J, Recas M, Figueroa J, et al. Differential allergen sensitization patterns in chestnut allergy with or without associated latex-fruit syndrome. J Allergy Clin Immunol 2006;118:705-710
BackgroundChestnut allergy has been almost exclusively considered in the context of the latex-fruit syndrome. Chestnut allergens not linked to latex hypersensitivity have not been studied.ObjectiveWe sought to explore whether differences in sensitization patterns between chestnut allergy with or without associated latex-fruit syndrome can be detected.MethodsTwelve patients sensitized to chestnut but not to latex and 3 control patients with latex-chestnut allergy were analyzed. A major chestnut allergen was purified and characterized. IgE immunoblotting, specific IgE determination, and skin prick tests with 5 isolated allergens involved in food allergy or latex-fruit syndrome were also performed.ResultsA major 9-kd allergen was detected in chestnut extract, isolated, and identified as lipid transfer protein (LTP) Cas s 8. Specific IgE to this allergen was found in 91% (by means of IgE immunoblotting) and 58% (by means of ELISA) of sera from patients with chestnut but not latex allergy. Moreover, 66% of these p atients had positive skin prick test responses to Cas s 8. Additionally, allergenic LTPs from peach fruit and Artemisia vulgaris pollen were also reactive. In contrast, avocado class I chitinase and latex hevein, allergens associated with the latex-fruit syndrome, showed no reaction. The opposite situation was exhibited by patients with latex-chestnut allergy.ConclusionsPatients with chestnut allergy with or without associated latex hypersensitivity present different patterns of major allergens (LTPs and class I chitinases, respectively).Clinical implicationsLTPs and class I chitinases can be used as diagnostic tools in patients with chestnut allergy to predict whether an associated latex sensitization and a risk of potential cross-reactivity with other plant foods and pollens exist
↩[16] - Roux KH, Teuber SS, Sathe SK. Tree Nut Allergens. Int Arch Allergy Immunol 2003;131:234-244
Allergic reactions to tree nuts can be serious and life threatening. Considerable research has been conducted in recent years in an attempt to characterize those allergens that are most responsible for allergy sensitization and triggering. Both native and recombinant nut allergens have been identified and characterized and, for some, the IgE-reactive epitopes described. Some allergens, such as lipid transfer proteins, profilins, and members of the Bet v 1-related family, represent minor constituents in tree nuts. These allergens are frequently cross-reactive with other food and pollen homologues, and are considered panallergens. Others, such as legumins, vicilins, and 2S albumins, represent major seed storage protein constituents of the nuts. The allergenic tree nuts discussed in this review include those most commonly responsible for allergic reactions such as hazelnut, walnut, cashew, and almond as well as those less frequently associated with allergies including pecan, chestnut, Brazil nut, pine nut, macadamia nut, pistachio, coconut, Nangai nut, and acorn.
↩[17] - Sanchez-Monge R, Blanco C, Lopez-Torrejon G, Cumplido J, Recas M, Figueroa J, et al. Differential allergen sensitization patterns in chestnut allergy with or without associated latex-fruit syndrome. J Allergy Clin Immunol 2006;118:705-710
BackgroundChestnut allergy has been almost exclusively considered in the context of the latex-fruit syndrome. Chestnut allergens not linked to latex hypersensitivity have not been studied.ObjectiveWe sought to explore whether differences in sensitization patterns between chestnut allergy with or without associated latex-fruit syndrome can be detected.MethodsTwelve patients sensitized to chestnut but not to latex and 3 control patients with latex-chestnut allergy were analyzed. A major chestnut allergen was purified and characterized. IgE immunoblotting, specific IgE determination, and skin prick tests with 5 isolated allergens involved in food allergy or latex-fruit syndrome were also performed.ResultsA major 9-kd allergen was detected in chestnut extract, isolated, and identified as lipid transfer protein (LTP) Cas s 8. Specific IgE to this allergen was found in 91% (by means of IgE immunoblotting) and 58% (by means of ELISA) of sera from patients with chestnut but not latex allergy. Moreover, 66% of these p atients had positive skin prick test responses to Cas s 8. Additionally, allergenic LTPs from peach fruit and Artemisia vulgaris pollen were also reactive. In contrast, avocado class I chitinase and latex hevein, allergens associated with the latex-fruit syndrome, showed no reaction. The opposite situation was exhibited by patients with latex-chestnut allergy.ConclusionsPatients with chestnut allergy with or without associated latex hypersensitivity present different patterns of major allergens (LTPs and class I chitinases, respectively).Clinical implicationsLTPs and class I chitinases can be used as diagnostic tools in patients with chestnut allergy to predict whether an associated latex sensitization and a risk of potential cross-reactivity with other plant foods and pollens exist
↩[18] - Ito K, Morishita M, Ohshima M, Sakamoto T, Tanaka A. Cross-reactive Carbohydrate Determinant Contributes to the False Positive IgE Antibody to Peanut. Allergol Int 2005;54:387-392
Imprimer la bibliographieAnti-CCD IgE antibody was suggested to be one of the mechanisms contributing to the false positive detection of peanut IgE. Detection of anti-HRP or anti-bromelain IgE can be a useful tool to recognize the presence of anti-CCD antibodies.
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