Les Astéracées (Composées)

sous-famille	tribu	genre	espèce	anglais	français
Astéroïdées	Anthémidées	Anthemis	arvensis	corn chamomile	fausse camomille
Achillea	millefolium	yarrow	achillée
Artemisia	vulgaris	mugwort	ARMOISE
absinthium	absinthe	absinthe
dracunculus	tarragon	estragon
umbelliformis	alps wormwood	génépi
Chamaemelum	nobile	roman chamomile	camomille romaine
Chrysanthemum	spp.	chrysanthemums	chrysanthèmes
Leucanthemum	vulgare	oxeye daisy	grande marguerite
Matricaria	recutita	german chamomile	camomille sauvage
Tanacetum	vulgare	tansy	tanaisie
parthenium	feverfew	grande camomille
Astérées	Aster	spp.	aster	aster
Baccharis	spp.	false willow	séneçon en arbre
Erigeron	spp.	fleabane	vergerette
Solidago	spp.	goldenrod	verge d’or
Calendulées	Calendula	officinalis	marigold	souci
Coreopsidées	Cosmos	spp.	cosmos	cosmos
Dahlia	spp.	dahlia	dahlia
Héléniées	Gaillardia	spp.	banketflower	gaillarde
Hélianthées	Ambrosia	artemisiifolia = elatior	short ragweed	AMBROISIE élevée
psilostachya coronopifolia	western ragweed	ambroisie à épi grèle
trifida	giant ragweed	ambroisie géante
Helianthus	annuus	sunflower	tournesol
tuberosus	jerusalem artichoke	topinambour
Iva	annua	marshelder	iva
Parthenium	argentatum	guayule	guayule (latex)
hysterophorus	american feverfew	camomille amère
Smallanthus	sonchifolius	yacon	poire de terre
Xanthium	commune	cocklebur	lampourde
Zinnia	spp.	zinnia	zinnia
Milleriées	Guizotia	abyssinica	niger (seed), ramtilla	niger (graine)
Senecionées	Senecio	vulgaris	groundsel	séneçon commun
Jacobaea	vulgaris	ragwort	séneçon jacobée
Cardudoïdées	Carduées	Arctium	lappa	greater burdock	bardane
Carduus	spp.	thistles	chardons
Carthamus	tinctorius	safflower	carthame
Centaurea	spp.	cornflowers	bleuets
Cirsium	spp.	thistles	chardons
Cynara	cardunculus	cardoon	cardon
scolymus	globe artichoke	artichaut
Cichorioïdées	Cichoriées	Cichorium	endivia	endive	scarole, chicorée frisée
intybus sativum	chicory (root)	chicorée (à café)
intybus foliosum	belgian endive, witloof, radicchio	endive, chicon
Lactuca	sativa	lettuce	laitue batavia, romaine
Taraxacum	officinale	dandelion	pissenlit
Tragopogon	porrifolius	salsify	salsifis

Weeds represent a heterogeneous group of plants, usually defined by no commercial or aesthetic value. Important allergenic weeds belong to the plant families Asteraceae, Amaranthaceae, Urticaceae, Euphorbiaceae, and Plantaginaceae. Major allergens from ragweed, mugwort, feverfew, pellitory, goosefoot, Russian thistle, plantain, and Mercurialis pollen have been characterized to varying degrees. Four major families of proteins seem to be the major cause of allergic reactions to weed pollen: the ragweed Amb a 1 family of pectate lyases; the defensin-like Art v 1 family from mugwort, feverfew, and probably also from sunflower; the Ole e 1-like allergens Pla l 1 from plantain and Che a 1 from goosefoot; and the nonspecific lipid transfer proteins Par j 1 and Par j 2 from pellitory. As described for other pollens, weed pollen also contains the panallergens profilin and calcium-binding proteins, which are responsible for extensive cross-reactivity among pollen-sensitized patients.

↩

[3] - Bousquet J, Dhivert H, Clauzel AM, Hewitt B, Michel FB. Occupational allergy to sunflower pollen. J Allergy Clin Immunol 1985;75:70-74

Although the sunflower belongs to the Compositeae family, allergy to sunflower pollen is not common. The occurrence of occupational allergy to this pollen species made it possible to characterize cross-reactive patterns of Compositeae pollens in a human experimental model. A 24-yr-old man developed rhinitis and conjunctivitis over 5 yr of exposure to sunflower pollens, and asthma developed during the fifth year. All respiratory and occular symptoms disappeared after he was removed from exposure, but he had a food allergic reaction while he was eating honey containing 30% sunflower pollens. The diagnosis of occupational allergy was based on history, skin prick tests and RAST to the pollen. Bronchial provocation tests performed after removal from exposure confirmed the sensitivity to sunflower pollens but there was no nonspecific hyperreactivity. It was found by RAST inhibition that sunflower pollen does not cross-react with other Compositeae pollens tested or with sunflower seed. The honey that elicited food intolerance was demonstrated to inhibit significantly sunflower pollen RAST

↩

[4] - Esnal S, Longo N, Audicana M, Uriel O, Fernandez E, Santolaya E. Hypersensitivity to Sunflower pollen. Allergy 2008;63(suppl. 88):448

Background: The sunflower (Heliantus annus) is an herbacea plant from Asteraceae family, used as ornamental because of its yellow flower and that has great economic importance in the food and oil industry. Allergy to sunflower often has been reported in farmers and in people who live near large plantation. We reported 2 cases of occupational sensitisation to sunflower pollen in 2 florists patients. Case 1: A women aged 32, reported long term symptoms of rhinoconjunctivitis related to the handling of the flowers. After 10 years of working in florist, she developed on going bronquial symtoms, angioedema and urticaria in contact with sunflower and also presented urticaria by the use of latex gloves. Case 2: A women aged 39 who complained of rhinoconjunctival symtoms from March to July, reported the same symtoms when handling flowers in her work place. She also reported itching when using latex gloves. Methods: Both patients were estudied by means of skin prick testing with the common inhalants including pollens; prick by prick with the flowers they usually handled; Specific IgE; conjunctival challenge test; bronchial challenge test (only in the first case); CAP-inhibition with latex and sunflower and immunoblotting with sunflower extract. Results: The standard skin prick tests were positive with Compositae, grasses and trees pollen.Prick by prick with sunflower was positive in both cases. The determination of specific IgE was positive to sunflower, other compositae pollen, grasses and some tree pollen. Both patients showed negative skin prick test with latex. Specific IgE determination and the conjunctival challenge test were positive. The bronchial challenge with sunflower pollen extract (Bial-Aristegui) done in the first case was positive. The results of the CAP_inhibition suggested cross-reaction between sunflower pollen and latex allergen, and immunoblotting made with sunflower extract showed a band of low molecular weight that was diminished by incubating the sera with latex extract. Conclusion: We reported 2 cases of professional respiratory allergy in florists with sensitisation to sunflower pollen, in wich sensitisation to latex was also documented. Our results suggest that in these patients cross-reaction between sunflower pollen proteins and latex protein could exist.

↩

[5] - Bains S, Lang DM, Han Y, Hsieh FH. Characterizing the Allergens Contained in Goldenrod (Solidago virgaurea). J Allergy Clin Immunol 2008;121:S175

RATIONALE: Evidence suggests that goldenrod (Solidago virgaurea) has a high latex content (Ann Allergy Asthma Immunol. Dec 2003;91(6):A6).We evaluated a florist with a history suggestive of allergy to both goldenrod and latex. We sought to identify the allergenic proteins contained in goldenrod. METHODS: A florist was seen in our clinic for suspected goldenrod allergy. She described sudden onset of rhinorrhea, sneezing, watery, itchy eyes and contact urticaria associated with dyspnea, wheezing and chest tightness within thirty minutes of handling a large goldenrod shipment. She also reported a pruritic rash after wearing latex gloves on several occasions. Skin testing was performed and RASTwere obtained to both goldenrod and latex. Serum was acquired from the patient for SDS-PAGE IgE immunoblotting in order to detect the presence of goldenrod and latex proteins recognized by patient IgE. RESULTS: Percutaneous skin testing and RAST were positive to both goldenrod and latex. IgE immunoblotting revealed two goldenrod proteins of approximate molecular size of 42 and 70 kDa recognized by IgE in the patient‚s serum. Further experiments are currently underway to determine if there is cross reactivity between latex and goldenrod by IgE immunoblotinhibition. CONCLUSION: This study characterizes the allergenic proteins contained in goldenrod for the first time. Since goldenrod reportedly has a high latex content future experiments seek to determine if sensitization to goldenrod is a risk factor for latex allergy, and whether known latex allergic patients are at risk for reaction when exposed to goldenrod.

↩

[6] - de la Hoz F, Melero JA, Gonzalez R, Carreira J. Isolation and partial characterization of allergens from Helianthus annuus (sunflower) pollen. Allergy 1994;49:848-854

We have purified four allergens from Helianthus annuus (sunflower) pollen, hereafter named as allergens a, b, c, and d. Under native conditions, allergen a has a mol. mass of 32, allergen b has one of 24, and allergens c and d each have one of 55 kDa. At the least, allergens b, c, and d demonstrate charge heterogeneity, and the electrophoretic mobility of allergens c and d increases when these allergens are deglycosylated with trifluoromethanesulfonic acid. Cross-reactivity among the four allergens and with the whole extract is very high, and each allergen recognizes IgE in a high proportion of patients sensitized to sunflower pollen.

↩

[7] - Gruber P, Gadermaier G, Bauer R, Weiss R, Wagner S, Léonard R et al. Role of the polypeptide backbone and post-translational modifications in cross-reactivity of Art v 1, the major mugwort pollen allergen. Biol Chem 2009;390:445-451

Artemisia vulgaris (mugwort) is one of the main causes of late summer pollinosis in Europe, with >95% of patients sensitized to the glycoallergen Art v 1. Despite the importance of this allergen, little is known about its cross-reactive behavior. Here we investigated the occurrence of conserved Art v 1 antigenic determinants in sources known to display clinically relevant cross-reactivity with mugwort pollen. For this purpose, monoclonal antibodies specific for a cysteine-stabilized epitope of the Art v 1 defensin domain and for carbohydrates attached to the proline domain were produced by hybridoma and phage display technologies. Using polyclonal Art v 1-specific rabbit sera and antibodies against both the Art v 1 carbohydrate and polypeptide moieties, we could identify cross-reactive structures in pollen from botanically related Asteraceae weeds (Artemisia absinthium, Helianthus annuus and Ambrosia sp.). Homologous allergens were also recognized by IgE from mugwort-sensitized patients and the reactivity could be decreased by serum pre-incubation with natural and recombinant Art v 1. As no cross-reactive structures could be found in foods associated with mugwort pollinosis, we conclude that Art v 1 is poorly involved in mugwort cross-reactivity to food allergens.

↩

[8] - Asturias JA, Arilla MC, Gomez-Bayon N, Aguirre M, Martinez A, Palacios R, et al. Cloning and immunological characterization of the allergen Hel a 2 (profilin) from sunflower pollen. Mol Immunol 1998;35:469-478

Sunflower (Helianthus annuus) sensitization is not always related with occupational allergy. We have isolated the allergen profilin (Hel a 2) from this Compositae plant, cloned and sequenced five cDNAs encoding for full-length or partial Hel a 2. Natural sunflower profilin reacted with specific IgE in the 121 sera tested, at a frequency of 30.5%. Expression of the cDNA encoding Hel a 2 in Escherichia coli and a simple purification procedure by poly-L-proline chromatography allowed immunological characterization of the recombinant allergen. Binding of monoclonal antibodies against sunflower profilin revealed that some epitopes responsible for antigen-specific IgG production were not present in the recombinant allergen. High cross-reactivity has been found between recombinant Hel a 2 and profilins from other Compositae plants and also from botanically distant plants.

↩

[9] - Vassilopoulou E, Zuidmeer L, Akkerdaas J, Tassios I, Rigby NR, Mills ENC, et al. Severe Immediate Allergic Reactions to Grapes: Part of a Lipid Transfer Protein-Associated Clinical Syndrome. Int Arch Allergy Immunol 2007;143:92-102

BACKGROUND: Grape allergy is considered rare; grape lipid transfer protein (LTP; Vit v 1), an endochitinase and a thaumatin-like protein (TLP) have been reported as grape allergens. A considerable number of patients have referred to our department for severe reactions to grapes, and several IgE binding proteins were detected . OBJECTIVES: The aim of this study was to identify and characterise the allergens involved in severe allergic reactions to grapes and describe the population in which they occur . METHODS: Patients with reported severe allergic reactions to grapes (n = 37) are described. Grape allergens were purified/fractionated by a combination of chromatographic techniques, identified by proteomic analysis and biochemically characterised. Immunoreactivity was assessed by blot (inhibitions) and RAST (inhibitions), and skin prick tests were performed with the isolated allergens . RESULTS: All subjects were polyallergic, sensitised and reactive to several additional foods and pollen. All patients were sensitised to grape LTP. A 28-kDa expansin, a 37.5-kDa polygalacturonase-inhibiting protein, a 39-kDa beta-1,3-glucanase and a 60-kDa protein were identified as minor grape allergens. Endochitinase and TLP did not play a role. Inhibition experiments revealed the possible cross-reactive role of LTP for clinical sensitivities to other LTP-containing plant foods, but also the involvement of cross-reactive carbohydrate determinants of minor allergens in IgE cross-reactivity . CONCLUSIONS: LTP is the major grape allergen, while additional minor allergens may contribute to clinical reactivity. Severe grape allergy presents in atopic patients who frequently react to other LTP-containing, plant-derived foods. The 'LTP syndrome' is the appropriate term to describe this condition.

↩

[10] - Gupta N, Martin BM, Metcalfe DD, Rao PV. Identification of a novel hydroxyproline-rich glycoprotein as the major allergen in Parthenium pollen. J Allergy Clin Immunol 1996;98:903-912

The airborne pollen of the Compositae weed, Parthenium hysterophorus, is a major cause of allergic rhinitis in the Indian subcontinent and in certain parts of the southern United States and western Australia. Earlier studies have identified a 31 kd protein as the major allergen in Parthenium pollen. OBJECTIVE: This study was undertaken to carry out the purification, immunochemical characterization, sequencing, and epitope analysis of this major allergen, designated as Par h I. METHODS: The IgE-binding activity of the allergen was evaluated by immunoblot and inhibition ELISAs. Pronase digestion, periodate oxidation, and chemical deglycosylation were performed to determine the role of peptide and carbohydrate components of the allergen in IgE binding. RESULTS: The data provide evidence for the involvement of carbohydrate moieties on Par h 1 in its IgE-binding ability. The N-terminal 91 amino acid sequence of Par h 1 shows 81% identity with a protein from sunflower anther, and the hydroxyproline-rich region of Par h 1 is 30% to 40% identical to similar stretches in extensins, a class of hydroxyproline-rich cell wall glycoproteins from different plant species. IgE antibodies in the sera of individuals allergic to Parthenium cross-reacted with a 50 kd hydroxyproline-arabinose-rich extensin precursor from potato tuber, and this binding was periodate-sensitive. CONCLUSIONS: It appears that a group of soluble plant glycoproteins, which are related to the ubiquitous extensins, have certain carbohydrate-containing IgE-binding epitopes that may contribute to allergenic cross-reactivity among specific pollens and foods.

↩

[11] - Reider N, Sepp N, Fritsch P, Weinlich G, Jensen-Jarolim E. Anaphylaxis to camomile: clinical features and allergen cross-reactivity. Clin Exp Allergy 2000;30:1436-1443

BACKGROUND: Medicinal remedies of plant origin became very popular in recent years, and allergic reactions to these are on the rise, accordingly. Camomile has been reported as a potential trigger of severe anaphylaxis. The allergens responsible for camomile allergy have not been characterized as yet. OBJECTIVE: The present study aims at reviewing the clinical symptomatology of immediate-type reactions in a series of patients sensitized to camomile and at characterizing the responsible allergens. METHODS: Fourteen patients with a history of allergy either to camomile or to spices or weeds, and a positive skin prick test/RAST to camomile were investigated for related allergic reactions to food, pollen and others. IgE-binding patterns were determined by immunoblotting, inhibition tests and deglycosylation experiments. RESULTS: Ten of 14 patients had a clinical history of immediate-type reactions to camomile, in some cases life threatening. Eleven subjects were also sensitized to mugwort in prick or RAST, eight to birch tree pollen. Using a polyclonal rabbit anti-Bet v 1 antibody, a homologue of the major birch pollen allergen Bet v 1 was detected in two camomile blots. In four cases a group of higher molecular weight allergens (23-50 kDa) showed IgE-binding to camomile. All allergens proved heat stable. Binding was inhibited in variable degrees by extracts from celery roots, anize seeds and pollen from mugwort, birch and timothy grass. Deglycosylation experiments proved the presence of carbohydrate determinants in camomile which were not responsible for IgE-binding, though. Profilins (Bet v 2) were not detected in our camomile extracts. CONCLUSION: Incidence and risk of type I allergy to camomile may be underestimated. Concurrent sensitization to mugwort and birch pollen is not infrequent. Bet v 1 and noncarbohydrate higher molecular weight proteins were found to be eliciting allergens and are responsible for cross-reactivity with other foods and pollen.

↩

[12] - Luengo O, Mollá R, Gámez C, Cardona V, López E, Sastre B, et al. Allergenicity and cross-reactivity of Senecio pollen: identification of novel allergens using the immunoproteomics approach. Clin Exp Allergy 2008;38:1048-1060

BACKGROUND: The genus Senecio is the largest genus of the family Asteraceae (Compositae). The allergenicity of Senecio has not been assessed previously . OBJECTIVE: The aim of this study was to investigate the allergens of Senecio jacobea pollen and to determine their immunological characteristics and clinical relevance . METHODS: Fifty patients with rhinoconjunctivitis and a positive skin prick test (SPT) to Senecio were recruited. The clinical relevance of this pollen was assessed by means of a nasal provocation test (NPT). Allergens were characterized by one-dimensional electrophoresis (SDS-PAGE) and two-dimensional gel electrophoresis and immunoblotting. Furthermore, characterization and identification of the allergens were performed by mass spectrometry (MS). In vitro inhibition tests were performed to evaluate cross-reactivity with other pollen . RESULTS: Three predominant allergens, both in the intensity of reaction and the frequency of recognition by human-allergic sera, were 59 (60%), 42 (50%) and 31 kDa (50%). The two-dimensional analysis allowed the identification of several allergens. One spot around 42 kDa was identified as a protein homologous to pectate lyase and three other spots were homologous to malate dehydrogenase by MS. S. jacobea proteins showed cross-reactivity with other proteins of the Asteraceae family and also with Parietaria judaica. This was demonstrated by immunoblotting and ELISA inhibition studies . CONCLUSION: S. jacobea constitute a newly discovered allergenic source. It shows cross-reactivity with other members of the Asteraceae plant family as well as with P. judaica.

↩

[13] - Jiménez A, Moreno C, Martinez J, Martinez A, Bartolome B, Guerra F, et al. Sensitization to sunflower pollen: only an occupational allergy? Int Arch Allergy Immunol 1994;105:297-307

Sunflower (Helianthus annuus) pollen sensitization has been reported as an occupational allergy. In this report, the sensitization of the general population living in sunflower-growing areas to Helianthus pollen was studied. Both RAST results in 32 adults with summer symptoms previously diagnosed as allergic to Artemisia pollen, and cross-reactivity studies between H. annuus and other Compositae suggested that H. annuus pollen was the main allergen involved in the hypersensitivity reaction of those patients. Good correlation was found between RAST and SPT to Helianthus and between RAST and conjunctival provocation test to Helianthus. Bronchial challenge tests performed on 8 of the 32 patients confirmed the clinical implication of Helianthus pollen in suspected subjects. Five workers, handling sunflower pollen, who suffered from related symptoms were subjected to the same study, showing lesser wheal areas and lesser specific IgE levels than a non-worker group. Thirteen patients with RAST values > or = class 2 showed 2 IgE-binding fractions at 34.0 and 42.8 kD in 65% of sera and 3 IgE-binding fractions at pI 4.9, 9.6 and 10.2 in 54% of sera. By means of micropreparative high-resolution chromatography, it was possible to purify a 34-kD major allergen. Analysis performed by RAST inhibition with sera from atopic patients and ELISA inhibition with experimental anti-Helianthus rabbit sera demonstrated a cross-reactivity between Helianthus and other Compositae, but low affinity of specific anti-Helianthus antibodies for heterologous antigens. Taking into account the above-mentioned data, and the high prevalence of Helianthus pollen in the atmosphere during harvesting (in spite of its entomophilous character), Helianthus pollen should be considered as an allergenic source to be investigated in the general population living in sunflower-growing regions suffering from seasonal summer allergy.

↩

[14] - Bousquet J, Dhivert H, Clauzel AM, Hewitt B, Michel FB. Occupational allergy to sunflower pollen. J Allergy Clin Immunol 1985;75:70-74

Although the sunflower belongs to the Compositeae family, allergy to sunflower pollen is not common. The occurrence of occupational allergy to this pollen species made it possible to characterize cross-reactive patterns of Compositeae pollens in a human experimental model. A 24-yr-old man developed rhinitis and conjunctivitis over 5 yr of exposure to sunflower pollens, and asthma developed during the fifth year. All respiratory and occular symptoms disappeared after he was removed from exposure, but he had a food allergic reaction while he was eating honey containing 30% sunflower pollens. The diagnosis of occupational allergy was based on history, skin prick tests and RAST to the pollen. Bronchial provocation tests performed after removal from exposure confirmed the sensitivity to sunflower pollens but there was no nonspecific hyperreactivity. It was found by RAST inhibition that sunflower pollen does not cross-react with other Compositeae pollens tested or with sunflower seed. The honey that elicited food intolerance was demonstrated to inhibit significantly sunflower pollen RAST

↩

[15] - Fernandez C, Martin-Esteban M, Fiandor A, Pascual CY, Lopez Serrano C, Martinez Alzamora F, et al. Analysis of cross-reactivity between sunflower pollen and other pollens of the Compositae family. J Allergy Clin Immunol 1993;92:660-667

The sera of 20 patients with Compositae pollen allergy were investigated for the presence of IgE antibodies reacting against sunflower pollen by means of RAST and immunoblotting studies. Thirteen IgE-binding bands were detected with molecular weights ranging from 14.4 to 94 kd. Two of these bands, with molecular weights of 24 and 25 kd, contained major allergens that reacted strongly with 100% (24 kd) and 95% (25 kd) of the sera, respectively. Cross-reactivity between sunflower and other Compositae pollens (mugwort, marguerite, dandelion, golden rod, and short ragweed) was revealed by RAST and immunoblotting inhibition experiments. Mugwort pollen exhibited the greatest degree of allergenic homology (cross-reactivity) with sunflower pollen, whereas at the other end of the spectrum, short ragweed showed less cross-reactive epitopes.

↩

[16] - Kanny G, Frémont S, Nicolas JP, Moneret-Vautrin DA. Food allergy to sunflower oil in a patient sensitized to mugwort pollen. Allergy 1994;49:561-564

↩

[17] - Fernandez C, Martin-Esteban M, Fiandor A, Pascual CY, Lopez Serrano C, Martinez Alzamora F, et al. Analysis of cross-reactivity between sunflower pollen and other pollens of the Compositae family. J Allergy Clin Immunol 1993;92:660-667

The sera of 20 patients with Compositae pollen allergy were investigated for the presence of IgE antibodies reacting against sunflower pollen by means of RAST and immunoblotting studies. Thirteen IgE-binding bands were detected with molecular weights ranging from 14.4 to 94 kd. Two of these bands, with molecular weights of 24 and 25 kd, contained major allergens that reacted strongly with 100% (24 kd) and 95% (25 kd) of the sera, respectively. Cross-reactivity between sunflower and other Compositae pollens (mugwort, marguerite, dandelion, golden rod, and short ragweed) was revealed by RAST and immunoblotting inhibition experiments. Mugwort pollen exhibited the greatest degree of allergenic homology (cross-reactivity) with sunflower pollen, whereas at the other end of the spectrum, short ragweed showed less cross-reactive epitopes.

↩

[18] - Egger M, Wopfner N, Himly M, Dedic A, Bauer R, Mari A, et al. Art v 1, the Major Mugwort Allergen, Cross-Reacts With Proteins Originating From Compositae and Grass Pollen. AAAAI 60th Annual Meeting, San Francisco, 19-23 March 2004, Poster n°1098 (113(2 suppl):S300)

Rationale Art v 1 is the major mugwort (Artemisia vulgaris) pollen allergen and therefore represents one of the main causes of late summer pollinosis in Europe. Cross-reacting specific IgE antibodies can lead to clinically significant reactions with other members of the Compositae plant family (e.g. ragweed) in other geographic areas, such as Northern America. Furthermore, previous studies revealed cross-reactivity between mugwort pollen and certain food, known as the „celery-mugwort-spice-syndrome‰. Method s : In vitro cross-reactivity between Art v 1 and proteins from other Compositae-, grass- and tree pollen and common food allergen sources was investigated by immunoblot and IgE-inhibition experiments using the following antibodies: polyclonal rabbit anti-natural Art v 1, rabbit anti-recombinant Art v 1, moAb anti-Art v 1, produced by genetic immunization, and sera from mugwort and ragweed sensitized patients. Result s : The glycoallergen Art v 1 shares epitopes with proteins originating mainly from the botanically related plants of the Compositae family (Artemisia absinthium, Ambrosia artemisifolia, Ambrosia psilostachya, Ambrosia trifida and Helianthus annuus) and with the timothy grass (Phleum pratense) major allergen Phl p 1. We could not observe cross-reactivity between Art v 1 and proteins in extracts from tree pollen (Betula verrucosa) and food (apple and celery). Conclusions : The Art v 1 cross-reactive epitopes seem to encompass both the Art v 1 polypeptide and O-glycans attached to its C-terminal domain. Cross-reactivity with the glycoprotein Phl p 1 seems to be due to structural similarities in the Art v 1 defensin like domain or to sugar chains linked to its proline rich domain.

↩

[19] - Fernandez C, Martin-Esteban M, Fiandor A, Pascual CY, Lopez Serrano C, Martinez Alzamora F, et al. Analysis of cross-reactivity between sunflower pollen and other pollens of the Compositae family. J Allergy Clin Immunol 1993;92:660-667

The sera of 20 patients with Compositae pollen allergy were investigated for the presence of IgE antibodies reacting against sunflower pollen by means of RAST and immunoblotting studies. Thirteen IgE-binding bands were detected with molecular weights ranging from 14.4 to 94 kd. Two of these bands, with molecular weights of 24 and 25 kd, contained major allergens that reacted strongly with 100% (24 kd) and 95% (25 kd) of the sera, respectively. Cross-reactivity between sunflower and other Compositae pollens (mugwort, marguerite, dandelion, golden rod, and short ragweed) was revealed by RAST and immunoblotting inhibition experiments. Mugwort pollen exhibited the greatest degree of allergenic homology (cross-reactivity) with sunflower pollen, whereas at the other end of the spectrum, short ragweed showed less cross-reactive epitopes.

↩

[20] - de Lacoste de Laval A, Guérin L, Leduc V. Allergie aux pollen et graine de tournesol, réactions croisées ou cosensibilisation. Rev Fr Allergol Immunol Clin 2004;44:348

↩

[21] - Jiménez A, Moreno C, Martinez J, Martinez A, Bartolome B, Guerra F, et al. Sensitization to sunflower pollen: only an occupational allergy? Int Arch Allergy Immunol 1994;105:297-307

Sunflower (Helianthus annuus) pollen sensitization has been reported as an occupational allergy. In this report, the sensitization of the general population living in sunflower-growing areas to Helianthus pollen was studied. Both RAST results in 32 adults with summer symptoms previously diagnosed as allergic to Artemisia pollen, and cross-reactivity studies between H. annuus and other Compositae suggested that H. annuus pollen was the main allergen involved in the hypersensitivity reaction of those patients. Good correlation was found between RAST and SPT to Helianthus and between RAST and conjunctival provocation test to Helianthus. Bronchial challenge tests performed on 8 of the 32 patients confirmed the clinical implication of Helianthus pollen in suspected subjects. Five workers, handling sunflower pollen, who suffered from related symptoms were subjected to the same study, showing lesser wheal areas and lesser specific IgE levels than a non-worker group. Thirteen patients with RAST values > or = class 2 showed 2 IgE-binding fractions at 34.0 and 42.8 kD in 65% of sera and 3 IgE-binding fractions at pI 4.9, 9.6 and 10.2 in 54% of sera. By means of micropreparative high-resolution chromatography, it was possible to purify a 34-kD major allergen. Analysis performed by RAST inhibition with sera from atopic patients and ELISA inhibition with experimental anti-Helianthus rabbit sera demonstrated a cross-reactivity between Helianthus and other Compositae, but low affinity of specific anti-Helianthus antibodies for heterologous antigens. Taking into account the above-mentioned data, and the high prevalence of Helianthus pollen in the atmosphere during harvesting (in spite of its entomophilous character), Helianthus pollen should be considered as an allergenic source to be investigated in the general population living in sunflower-growing regions suffering from seasonal summer allergy.

↩

[22] - Bousquet J, Dhivert H, Clauzel AM, Hewitt B, Michel FB. Occupational allergy to sunflower pollen. J Allergy Clin Immunol 1985;75:70-74

Although the sunflower belongs to the Compositeae family, allergy to sunflower pollen is not common. The occurrence of occupational allergy to this pollen species made it possible to characterize cross-reactive patterns of Compositeae pollens in a human experimental model. A 24-yr-old man developed rhinitis and conjunctivitis over 5 yr of exposure to sunflower pollens, and asthma developed during the fifth year. All respiratory and occular symptoms disappeared after he was removed from exposure, but he had a food allergic reaction while he was eating honey containing 30% sunflower pollens. The diagnosis of occupational allergy was based on history, skin prick tests and RAST to the pollen. Bronchial provocation tests performed after removal from exposure confirmed the sensitivity to sunflower pollens but there was no nonspecific hyperreactivity. It was found by RAST inhibition that sunflower pollen does not cross-react with other Compositeae pollens tested or with sunflower seed. The honey that elicited food intolerance was demonstrated to inhibit significantly sunflower pollen RAST

↩

[23] - Perrick D, Stafford CT, Armstrong E, DuRant RH. Modification of the fluorescent allergosorbent test as an inhibition assay for determination of cross-reactivity among aeroallergens. J Allergy Clin Immunol 1991;87:98-103

The fluorescent allergosorbent test was adapted as an inhibition assay to determine cross-reactivity between aeroallergens. With this method, similar antigenic determinants were found between short ragweed and giant ragweed, cocklebur, lamb's-quarter, rough pigweed, marsh elder, and goldenrod. Cocklebur and giant ragweed were highly potent in their ability to competitively bind to short ragweed IgE. The other pollens demonstrated lower potency of cross-reacting antigens. The fluorescent allergosorbent test-inhibition assay appears to be a useful method to determine cross-reactivity among aeroallergens.

↩

[24] - Lee YW, Choi SY, Lee EK, Sohn JH, Park JW, Hong CS. The Cross-allergenecity of Pollens from Compositae Family: Dendranthema grandiflorum, Artemisia vulgaris and Taraxacum officinale. J Allergy Clin Immunol 2007;119(1 suppl):S107

RATIONALE: Chrysanthemum, dandelion and mugwort belong to Compositae (Asteraceae) family. But their cross-allergenecity was evaluated incompletely. So we investigated the clinical aspects and the cross-allergenecity of these 3 plants. METHODS: We reviewed 6,497 allergic patients who have ever had skin prick test (SPT) during last 10 years. And then, the sensitization rates of the pollens were estimated. The binding patterns of specific IgE (sIgE) were analyzed by immunoblotting. Cross-allergenecity between these pollens was evaluated by inhibition ELISA. RESULTS: Among 6,497 patients, 17% had positive responses to one of above-mentioned 3 plants. And 5.2% demonstrated positive reactions to all three. Some patients responded exclusively to one allergen (1.5% to chrysanthemum, 1.4% to dandelion and 4.5% to mugwort). By mugwort, sIgE to chrysanthemum, dandelion and mugwort were inhibited upto 95%, 86% and 96% in inhibition ELISA using the pooled sera atopic to all three (n=6). 50% inhibitory allergen concentrations (IC50) for chrysanthemum-, dandelion- and mugwort-sIgE were not different between solid phase antigens and mugwort. However, mugwort-sIgE level was only suppressed upto 74% and 27% by chrysanthemum, dandelion, respectively. IC50 of chrysanthemum and dandelion for mugwort-sIgE were 0.3 and 57.0 mcg/mL each, while that of mugwort was 0.05 mcg/mL. Mugwort also inhibited the dandelion-sIgE of one serum exclusively atopic to dandelion. CONCLUSIONS: Chrysanthemum and dandelion pollens had extensive cross-allergenecity with mugwort.

↩

[25] - Jiménez A, Moreno C, Martinez J, Martinez A, Bartolome B, Guerra F, et al. Sensitization to sunflower pollen: only an occupational allergy? Int Arch Allergy Immunol 1994;105:297-307

Sunflower (Helianthus annuus) pollen sensitization has been reported as an occupational allergy. In this report, the sensitization of the general population living in sunflower-growing areas to Helianthus pollen was studied. Both RAST results in 32 adults with summer symptoms previously diagnosed as allergic to Artemisia pollen, and cross-reactivity studies between H. annuus and other Compositae suggested that H. annuus pollen was the main allergen involved in the hypersensitivity reaction of those patients. Good correlation was found between RAST and SPT to Helianthus and between RAST and conjunctival provocation test to Helianthus. Bronchial challenge tests performed on 8 of the 32 patients confirmed the clinical implication of Helianthus pollen in suspected subjects. Five workers, handling sunflower pollen, who suffered from related symptoms were subjected to the same study, showing lesser wheal areas and lesser specific IgE levels than a non-worker group. Thirteen patients with RAST values > or = class 2 showed 2 IgE-binding fractions at 34.0 and 42.8 kD in 65% of sera and 3 IgE-binding fractions at pI 4.9, 9.6 and 10.2 in 54% of sera. By means of micropreparative high-resolution chromatography, it was possible to purify a 34-kD major allergen. Analysis performed by RAST inhibition with sera from atopic patients and ELISA inhibition with experimental anti-Helianthus rabbit sera demonstrated a cross-reactivity between Helianthus and other Compositae, but low affinity of specific anti-Helianthus antibodies for heterologous antigens. Taking into account the above-mentioned data, and the high prevalence of Helianthus pollen in the atmosphere during harvesting (in spite of its entomophilous character), Helianthus pollen should be considered as an allergenic source to be investigated in the general population living in sunflower-growing regions suffering from seasonal summer allergy.

↩

[26] - Fernandez C, Martin-Esteban M, Fiandor A, Pascual CY, Lopez Serrano C, Martinez Alzamora F, et al. Analysis of cross-reactivity between sunflower pollen and other pollens of the Compositae family. J Allergy Clin Immunol 1993;92:660-667

The sera of 20 patients with Compositae pollen allergy were investigated for the presence of IgE antibodies reacting against sunflower pollen by means of RAST and immunoblotting studies. Thirteen IgE-binding bands were detected with molecular weights ranging from 14.4 to 94 kd. Two of these bands, with molecular weights of 24 and 25 kd, contained major allergens that reacted strongly with 100% (24 kd) and 95% (25 kd) of the sera, respectively. Cross-reactivity between sunflower and other Compositae pollens (mugwort, marguerite, dandelion, golden rod, and short ragweed) was revealed by RAST and immunoblotting inhibition experiments. Mugwort pollen exhibited the greatest degree of allergenic homology (cross-reactivity) with sunflower pollen, whereas at the other end of the spectrum, short ragweed showed less cross-reactive epitopes.

↩

[27] - Egger M, Wopfner N, Himly M, Dedic A, Bauer R, Mari A, et al. Art v 1, the Major Mugwort Allergen, Cross-Reacts With Proteins Originating From Compositae and Grass Pollen. AAAAI 60th Annual Meeting, San Francisco, 19-23 March 2004, Poster n°1098 (113(2 suppl):S300)

Rationale Art v 1 is the major mugwort (Artemisia vulgaris) pollen allergen and therefore represents one of the main causes of late summer pollinosis in Europe. Cross-reacting specific IgE antibodies can lead to clinically significant reactions with other members of the Compositae plant family (e.g. ragweed) in other geographic areas, such as Northern America. Furthermore, previous studies revealed cross-reactivity between mugwort pollen and certain food, known as the „celery-mugwort-spice-syndrome‰. Method s : In vitro cross-reactivity between Art v 1 and proteins from other Compositae-, grass- and tree pollen and common food allergen sources was investigated by immunoblot and IgE-inhibition experiments using the following antibodies: polyclonal rabbit anti-natural Art v 1, rabbit anti-recombinant Art v 1, moAb anti-Art v 1, produced by genetic immunization, and sera from mugwort and ragweed sensitized patients. Result s : The glycoallergen Art v 1 shares epitopes with proteins originating mainly from the botanically related plants of the Compositae family (Artemisia absinthium, Ambrosia artemisifolia, Ambrosia psilostachya, Ambrosia trifida and Helianthus annuus) and with the timothy grass (Phleum pratense) major allergen Phl p 1. We could not observe cross-reactivity between Art v 1 and proteins in extracts from tree pollen (Betula verrucosa) and food (apple and celery). Conclusions : The Art v 1 cross-reactive epitopes seem to encompass both the Art v 1 polypeptide and O-glycans attached to its C-terminal domain. Cross-reactivity with the glycoprotein Phl p 1 seems to be due to structural similarities in the Art v 1 defensin like domain or to sugar chains linked to its proline rich domain.

↩

[28] - de Lacoste de Laval A, Guérin L, Leduc V. Allergie aux pollen et graine de tournesol, réactions croisées ou cosensibilisation. Rev Fr Allergol Immunol Clin 2004;44:348

↩

[29] - Gupta N, Martin BM, Metcalfe DD, Rao PV. Identification of a novel hydroxyproline-rich glycoprotein as the major allergen in Parthenium pollen. J Allergy Clin Immunol 1996;98:903-912

The airborne pollen of the Compositae weed, Parthenium hysterophorus, is a major cause of allergic rhinitis in the Indian subcontinent and in certain parts of the southern United States and western Australia. Earlier studies have identified a 31 kd protein as the major allergen in Parthenium pollen. OBJECTIVE: This study was undertaken to carry out the purification, immunochemical characterization, sequencing, and epitope analysis of this major allergen, designated as Par h I. METHODS: The IgE-binding activity of the allergen was evaluated by immunoblot and inhibition ELISAs. Pronase digestion, periodate oxidation, and chemical deglycosylation were performed to determine the role of peptide and carbohydrate components of the allergen in IgE binding. RESULTS: The data provide evidence for the involvement of carbohydrate moieties on Par h 1 in its IgE-binding ability. The N-terminal 91 amino acid sequence of Par h 1 shows 81% identity with a protein from sunflower anther, and the hydroxyproline-rich region of Par h 1 is 30% to 40% identical to similar stretches in extensins, a class of hydroxyproline-rich cell wall glycoproteins from different plant species. IgE antibodies in the sera of individuals allergic to Parthenium cross-reacted with a 50 kd hydroxyproline-arabinose-rich extensin precursor from potato tuber, and this binding was periodate-sensitive. CONCLUSIONS: It appears that a group of soluble plant glycoproteins, which are related to the ubiquitous extensins, have certain carbohydrate-containing IgE-binding epitopes that may contribute to allergenic cross-reactivity among specific pollens and foods.

↩

[30] - Sriramarao P, Rao PV. Allergenic cross-reactivity between Parthenium and ragweed pollen allergens. Int Arch Allergy Immunol 1993;100:79-85

Cross-reactivity of allergens from the pollen of the Compositae weeds, Parthenium hysterophorus (American feverfew) and Ambrosia (ragweed), in 2 groups of patients with different geographic distributions was studied Parthenium-sensitive Indian patients, who were never exposed to ragweed, elicited positive skin reactions with ragweed pollen extracts. A significant correlation in the RAST scores of Parthenium and ragweed-specific IgE was observed with the sera of Parthenium and ragweed-sensitive Indian and US patients, respectively. RAST inhibition experiments demonstrated that the binding of IgE antibodies in the sera of ragweed-sensitive patients to short (W1) and giant (W3) ragweed allergen discs could be inhibited by up to 94% by Parthenium pollen extracts Similar inhibition (up to 82%) was obtained when the sera of Parthenium rhinitis patients were incubated with ragweed allergen extracts. A dose-dependent proliferation of lymphocytes from a Parthenium-sensitive rhinitis patient with elevated levels of both Parthenium and ragweed-specific IgE was observed when incubated with Parthenium and ragweed pollen extracts. A 1.6-fold higher proliferation, however, was observed with Parthenium pollen extract at a concentration of 100 micrograms/ml. These results suggest that shared epitopes present on Parthenium and ragweed pollen allergens are recognized by both Indian and US patients sensitized by exposure to Parthenium and ragweed pollen, respectively. The high degree of cross-reactivity between Parthenium and ragweed pollen allergens suggests that individuals sensitized to Parthenium may develop type-I hypersensitivity reactions to ragweed and vice versa when they travel to regions infested with the weed to which they had not been previously exposed.

↩

[31] - Luengo O, Mollá R, Gámez C, Cardona V, López E, Sastre B, et al. Allergenicity and cross-reactivity of Senecio pollen: identification of novel allergens using the immunoproteomics approach. Clin Exp Allergy 2008;38:1048-1060

BACKGROUND: The genus Senecio is the largest genus of the family Asteraceae (Compositae). The allergenicity of Senecio has not been assessed previously . OBJECTIVE: The aim of this study was to investigate the allergens of Senecio jacobea pollen and to determine their immunological characteristics and clinical relevance . METHODS: Fifty patients with rhinoconjunctivitis and a positive skin prick test (SPT) to Senecio were recruited. The clinical relevance of this pollen was assessed by means of a nasal provocation test (NPT). Allergens were characterized by one-dimensional electrophoresis (SDS-PAGE) and two-dimensional gel electrophoresis and immunoblotting. Furthermore, characterization and identification of the allergens were performed by mass spectrometry (MS). In vitro inhibition tests were performed to evaluate cross-reactivity with other pollen . RESULTS: Three predominant allergens, both in the intensity of reaction and the frequency of recognition by human-allergic sera, were 59 (60%), 42 (50%) and 31 kDa (50%). The two-dimensional analysis allowed the identification of several allergens. One spot around 42 kDa was identified as a protein homologous to pectate lyase and three other spots were homologous to malate dehydrogenase by MS. S. jacobea proteins showed cross-reactivity with other proteins of the Asteraceae family and also with Parietaria judaica. This was demonstrated by immunoblotting and ELISA inhibition studies . CONCLUSION: S. jacobea constitute a newly discovered allergenic source. It shows cross-reactivity with other members of the Asteraceae plant family as well as with P. judaica.

↩

[32] - Vallier P, Dechamp C, Vial O, Deviller P. A study of allergens in celery with cross-sensitivity to mugwort and birch pollens. Clin Allergy 1988;18:491-500

Sixty-one sera with positive RAST to mugwort pollen (Artemisiae vulgaris) were submitted to RASTs for birch pollen (Betula verrucosa) and celery (Apium graveolens). In 36 cases RAST results were positive for celery. In addition, 23 sera presented specific IgE to birch pollen. The binding of specific IgE to individual allergens in celery, mugwort pollen and birch pollen was studied by the immunoblotting technique. This involved electrophoretic separation of allergenic extracts, electrotransfer of proteins onto nitrocellulose sheets and sensitive immunoenzymatic detection. Eighteen sera had specific IgE binding to two celery components of molecular weight around 15 kD. All these sera also detected a 15 kD allergen in mugwort and two allergens in birch of 14 kD and 16 kD molecular weight. The sera that did not detect the 15 kD bands in celery failed to react with both the 15 kD mugwort component and the 14 and 16 kD birch components. Specific cross-inhibitions of the detection of these allergens on immunoblots were obtained by pre-incubation of the sera with crude extract of the three species. These results strongly suggest that such allergens display some structural identity and that they could be at the origin of some cases of crossed hypersensitivity to celery, mugwort pollen and birch pollen

↩

[33] - van Ree R, Voitenko V, van Leeuwen WA, Aalberse RC. Profilin is a cross-reactive allergen in pollen and vegetable foods. Int Arch Allergy Immunol 1992;98:97-104

Sera with IgE antibodies against grass pollen often contain IgE against vegetable foods. We investigated the role of the ubiquitous protein profilin in this cross-reactivity. Profilin was purified from Lolium perenne grass pollen by means of affinity purification with Sepharose-coupled poly(L-proline). This solid phase was also used as capturing agent for profilin from pollen and food extracts for application in a radioallergosorbent test. It was shown that profilin is an allergen in grass pollen and in a wide range of vegetable foods, like potato and celery. Within a grass-pollen-sensitive population, patients with IgE to vegetable foods have a high incidence of antibodies against profilin. IgE antibodies against grass pollen profilin were shown to be cross-reactive with respect to vegetable foods

↩

[34] - Gonzalez EM, Villalba M, Rodriguez R. Allergenic cross-reactivity of olive pollen. Allergy 2000;55:658-663

BACKGROUND: Sera of patients allergic to olive (Olea europaea) pollen were used to analyze the IgE cross-reactivity between olive-pollen extract and other pollens obtained from phylogenetically unrelated species. METHODS: We used IgE immunostaining of pollen extracts blotted to nitrocellulose membranes after SDS-PAGE and inhibition analysis of this binding. RESULTS: A high inhibition of the IgE binding on olive-pollen extract was exhibited by birch, mugwort, pine, and cypress pollens, suggesting that these extracts contain proteins which share common epitopes and thus can be recognized by olive-allergic sera. IgE binding to Gramineae pollen extracts was not inhibited by olive-pollen extract, indicating a primary sensitization of the patients to these species. From the inhibition assays, the presence of an allergen of 45 kDa in the olive pollen, which has no homologous counterparts in other allergenic species, has been inferred. CONCLUSIONS: Olive pollen contains allergens which cross-react with pollens from unrelated species, a fact that could simplify the diagnosis and treatment of pollinosis.

↩

[35] - Miralles JC, Caravaca F, Guillén F, Lombardero M, Negro JM. Cross-reactivity between Platanus pollen and vegetables. Allergy 2002;57:146-149

Background: Several associations have been described between tree and plant pollens and certain foods. The objective of this study is to verify whether there is cross-reactivity between Platanus pollen and vegetable origin foods. Methods: We selected 56 patients allergic to vegetable foods and subjected them to cutaneous tests with aeroallergens and vegetable foods. A statistical analysis was performed to evaluate the association of Platanus pollen with foods and with other aeroallergens. Later, a specific IgE determination was performed as well as a RAST (radioallergosorbent) inhibition experiment, to verify the existence of cross-reactivity in vitro. Results: In the cutaneous tests we found a positive correlation between Platanus pollen and hazelnut, peanut, banana and celery. The results of the RAST inhibition experiment indicate an important cross-reactivity between the pollen of Platanus acerifolia and hazelnut and banana fruit, and an intermediate cross-reactivity with celery and peanut. Conclusion: We have described an association between the pollen of the Platanus tree and some vegetable foods such as hazelnut, banana, peanut and celery. This association could be explained by the in vitro IgE cross-reactivity detected.

↩

[36] - Niederberger V, Purohit A, Oster JP, Spitzauer S, Valenta R, Pauli G. The allergen profile of ash (Fraxinus excelsior) pollen: cross-reactivity with allergens from various plant species. Clin Exp Allergy 2002;32:933-941

BackgroundAsh, a wind-pollinated tree belonging to the family Oleaceae, is distributed world-wide and has been suggested as a potent allergen source in spring time. ObjectiveThe aim of this study was to determine the profile of allergen components in ash pollen in order to refine diagnosis and therapy for patients with sensitivity to ash pollen MethodsThe IgE reactivity profile of 40 ash pollen-allergic patients was determined by immunoblotting. Antibodies raised to purified pollen allergens from tree and grass pollens were used to identify cross-reactive structures in ash pollen extract. IgE immunoblot inhibition studies were performed with recombinant and natural pollen allergens to characterize ash pollen allergens and to determine the degree of cross-reactivity between pollen allergens from ash, olive, birch, grasses and weeds. ResultsThe allergen profile of ash pollen comprises Fra e 1, a major allergen related to the major olive allergen, Ole e 1, and to group 11 grass pollen allergens, the panallergen profilin, a two EF-hand calcium-binding protein, a pectinesterase-like molecule and an allergen sharing epitopes with group 4 grass pollen allergens. Thus, the relevant allergens of ash are primarily allergens that share epitopes with pollen allergens from other tree, grass and weed species. ConclusionsAllergic symptoms to ash pollen can be the consequence of sensitization to cross-reactive allergens from other sources. The fact that ash pollen-allergic patients can be discriminated on the basis of their specific IgE reactivity profile to highly or moderately cross-reactive allergens has implications for the selection of appropriate forms of treatment.

↩

[37] - Stumvoll S, Westritschnig K, Lidholm J, Spitzauer S, Colombo P, Duro G, et al. Identification of cross-reactive and genuine Parietaria judaica pollen allergens. J Allergy Clin Immunol 2003;111:974-979

BACKGROUND: The weed Parietaria judaica is one of the most important pollen allergen sources in the Mediterranean area. OBJECTIVE: We sought to identify P judaica pollen allergen, which might be used to serologically distinguish genuine Parietaria sensitization and cross-reactivity to allergens from other weed species (eg, mugwort and ragweed). METHODS: The allergen profile of P judaica IgE-reactive sera from weed pollen-sensitized allergic individuals from the Mediterranean region (n = 36) with high Parietaria pollen exposure and from weed pollen-allergic patients with little or no Parietaria exposure (Austria, n = 42; Scandinavia, n = 8; United States, n = 19) was established by CAP FEIA measurements and by IgE immunoblot inhibition experiments with recombinant allergens. RESULTS: The majority (83%) of the Mediterranean weed pollen-allergic patients mounted high IgE antibody levels (mean specific IgE, 20.89 kUA/L) against recombinant (r) Par j 2, whereas only 7% of the non-Mediterranean weed-allergic patients showed low IgE reactivity to rPar j 2 (mean specific IgE, 1.03 kUA/L). The cytoskeletal protein profilin and a 2-EF-hand calcium-binding allergen were identified as cross-reactive Parietaria allergens, which were recognized preferentially by Parietaria -positive, non-Mediterranean weed pollen-allergic patients. CONCLUSION: rPar j 2 might be used as a diagnostic marker allergen to identify weed pollen-allergic patients who are genuinely sensitized against Parietaria pollen and thus would be particularly suited for specific immunotherapy with Parietaria pollen extract.

↩

[38] - Perrick D, Stafford CT, Armstrong E, DuRant RH. Modification of the fluorescent allergosorbent test as an inhibition assay for determination of cross-reactivity among aeroallergens. J Allergy Clin Immunol 1991;87:98-103

The fluorescent allergosorbent test was adapted as an inhibition assay to determine cross-reactivity between aeroallergens. With this method, similar antigenic determinants were found between short ragweed and giant ragweed, cocklebur, lamb's-quarter, rough pigweed, marsh elder, and goldenrod. Cocklebur and giant ragweed were highly potent in their ability to competitively bind to short ragweed IgE. The other pollens demonstrated lower potency of cross-reacting antigens. The fluorescent allergosorbent test-inhibition assay appears to be a useful method to determine cross-reactivity among aeroallergens.

↩

[39] - Mur P, Brito Feo F, Lombardero M, Barber D, Galindo PA, Gomez E, et al. Allergy to linden (Tilia cordata). Allergy 2001;56:457-458

↩

[40] - Garcia-Gonzalez JJ, Bartolome-Zavala B, Del Mar Trigo-Perez M, Barcelo-Munoz JM, Fernandez-Melendez S, Negro-Carrasco MA, et al. Pollinosis to Ricinus communis (castor bean): an aerobiological, clinical and immunochemical study. Clin Exp Allergy 1999;29:1265-1275

Ricinus communis (castor bean) is a species included into the Euphorbiaceae family, common to all the warm regions of the world. Although the allergenicity of its seed is well known, references are scarce regarding the role played by its pollen as a pneumo-allergen. OBJECTIVES: To carry out an aerobiological study of this pollen in the Malaga area (southern Spain); describe the physicochemical characteristics of its most relevant allergens; and to demonstrate the existence of patients with respiratory allergy due to this pollen. METHODS: A Burkard spore trap was used for the aerobiological study from 1992 to 1996. Skin prick tests with castor bean pollen extract were performed to 1946 patients with rhinitis and/or asthma. Specific IgE levels were measured in castor bean-positive SPT patient sera. Immunochemical characterization of the most relevant allergens was performed using electrophoretic techniques. In vitro cross-reactivity studies using positive patient sera were carried out. Nasal challenge tests were done in 32 subjects randomly selected from the sensitized patient group. RESULTS: Castor bean is a perennial pollen with total annual pollen levels never exceeding 1%. One hundred and eighteen (7.7%) patients showed positive prick test (74 rhinitis, 36 rhinitis and asthma, eight asthma). Nine were monosensitized. Specific IgE levels were > or =0.35 PRU/mL in 39 (33%) of patient sera. Nasal challenge test: 10 subjects presented non-specific nasal hyperactivity, 15 were positive and seven negative. The molecular masses and isoelectric points of the main IgE-binding proteins, ranged from approximately 67-15.5/14.5 kDa and approximately 4.5-5.5, respectively. Profilin of the extract was purified by poli-L-proline-Sepharose chromatography and it appeared as one of the most frequent allergens. CONCLUSION: Castor bean pollen is an allergen which causes respiratory (mainly nasal) symptoms.

↩

[41] - Hirschwehr R, Heppner C, Spitzauer S, Sperr WR, Valent P, Berger U, et al. Identification of common allergenic structures in mugwort and ragweed pollen. J Allergy Clin Immunol 1998;101:196-206

Identification of common allergenic structures in mugwort and ragweed pollen. BACKGROUND: Despite the rare occurrence of ragweed in Middle Europe, a surprisingly high number of patients allergic to mugwort, a frequently encountered weed, display IgE reactivity against ragweed pollen allergens. OBJECTIVE: The aim of this study was to investigate whether the high prevalence of IgE reactivity against ragweed in patients allergic to mugwort is caused by the presence of common allergenic determinants. We also sought to characterize any cross-reactive allergens. METHODS: Common allergenic structures in mugwort and ragweed pollen were characterized by qualitative IgE immunoblot inhibition experiments performed with natural allergen extracts and recombinant allergens. The degree of cross-reactivity was estimated by quantitative CAP-FEIA competitions. The clinical significance of cross-reactive IgE antibodies was studied with histamine release experiments and nasal provocation tests. RESULTS: Mugwort and ragweed RAST values were significantly correlated in a population of 82 Austrian patients allergic to mugwort. IgE antibodies cross-reacted with allergens of comparable molecular weight that were present in both extracts. By using recombinant birch profilin and specific antisera for IgE inhibition experiments, profilin was identified as one of the cross-reactive components in mugwort and ragweed pollen. Preincubation of sera from patients allergic to mugwort with mugwort extract inhibited IgE binding to ragweed pollen extract greater than 80%. Mugwort and ragweed pollen extract induced comparable histamine release and reduction of nasal air flow in a patient with IgE reactivity against the major mugwort allergen Art v 1. CONCLUSION: In addition to profilin, mugwort and ragweed pollen contain a number of cross-reactive allergens, among them the major mugwort allergen Art v 1. Cross-reactive IgE antibodies can lead to clinically significant allergic reactions.

↩

[42] - Valenta R, Duchêne M, Ebner C, Valent P, Sillaber C, Deviller P, et al. Profilins constitute a novel family of functional plant pan-allergens. J Exp Med 1992;175:377-385

Type I allergy is a major health problem in industrialized countries where up to 15% of the population suffer from allergic symptoms (rhinitis, conjunctivitis, and asthma). Previously, we identified a cDNA clone that encoded a birch pollen allergen as profilin. Profilins constitute a ubiquitous family of proteins that control actin polymerization in eukaryotic cells; in particular, profilin participates in the acrosomal reaction of animal sperm cells. Although profilins had been unknown in plants so far, our finding led to the assumption that profilins might have similar functions in pollens during plant fertilization and therefore represent allergenic components in almost all pollens. We show that profilins are prominent allergens that can be isolated from tree pollens (Betula verrucosa, birch), from pollens of grasses (Phleum pratense, timothy grass), and weeds (Artemisia vulgaris, mugwort). About 20% of all pollen allergic patients tested (n = 65) displayed immunoglobulin E (IgE) reactivity to recombinant birch profilin that was expressed in pKK223-3 An IgE inhibition experiment performed with recombinant birch profilin and purified natural profilins from timothy grass and mugwort indicates common IgE epitopes. Moreover, all pollen profilins purified from these far distantly related plant species, and likewise the purified recombinant birch profilin, are able to elicit dose-dependent histamine release via high affinity Fc epsilon receptor of blood basophils from profilin allergic patients. The presence of profilin and possibly related proteins as crossreacting allergenic components in various plants therefore provides an explanation as to why certain allergic patients display type I allergic reactions with pollens and even food from distantly related plants. A functional pan-allergen, like profilin, available as purified recombinant protein, may be a useful diagnostic and probably therapeutic reagent.

↩

[43] - Barderas R, Villalba M, Rodriguez R. Recombinant expression, purification and cross-reactivity of chenopod profilin: rChe a 2 as a good marker for profilin sensitization. Biol Chem 2004;385:731-737

Chenopod pollen is one of the major sources of allergens in some locations in the US, southern Europe and desert countries, and pollen profilin (Che a 2) is a major allergen. Recombinant Che a 2 (rChe a 2) has been produced in Escherichia coil cells with a final yield of 25 mg/l of cell culture. The expressed protein was isolated and structurally characterized by means of mass spectrometry, Edman degradation and circular dichroism. rChe a 2 displayed a molecular mass of 13 959 Da, which agrees with that of the amino acid sequence. The N-terminal amino acid sequence indicated the correct processing of the recombinant product. The immunological analysis of rChe a 2 showed IgG- and IgE-binding capabilities equivalent to those of its natural counterpart, Che a 2, isolated from the pollen. Inhibition experiments showed high cross-reactivity degrees with different allergenic sources. Inhibition degrees of >95% and >80% were obtained for chenopod profilin and, respectively, latex and pollen extracts, whereas 10-95% of inhibition was observed for different plant-derived foods. Due to its close relation to other allergenic profilins from pollens, plant-derived foods and latex, rChe a 2 could be a useful tool in clinical trials to detect profilin-allergic patients and perhaps, depending on its clinical relevance, in specific immunotherapy of these hypersensitive individuals.

↩

[44] - Luengo O, Mollá R, Gámez C, Cardona V, López E, Sastre B, et al. Allergenicity and cross-reactivity of Senecio pollen: identification of novel allergens using the immunoproteomics approach. Clin Exp Allergy 2008;38:1048-1060

BACKGROUND: The genus Senecio is the largest genus of the family Asteraceae (Compositae). The allergenicity of Senecio has not been assessed previously . OBJECTIVE: The aim of this study was to investigate the allergens of Senecio jacobea pollen and to determine their immunological characteristics and clinical relevance . METHODS: Fifty patients with rhinoconjunctivitis and a positive skin prick test (SPT) to Senecio were recruited. The clinical relevance of this pollen was assessed by means of a nasal provocation test (NPT). Allergens were characterized by one-dimensional electrophoresis (SDS-PAGE) and two-dimensional gel electrophoresis and immunoblotting. Furthermore, characterization and identification of the allergens were performed by mass spectrometry (MS). In vitro inhibition tests were performed to evaluate cross-reactivity with other pollen . RESULTS: Three predominant allergens, both in the intensity of reaction and the frequency of recognition by human-allergic sera, were 59 (60%), 42 (50%) and 31 kDa (50%). The two-dimensional analysis allowed the identification of several allergens. One spot around 42 kDa was identified as a protein homologous to pectate lyase and three other spots were homologous to malate dehydrogenase by MS. S. jacobea proteins showed cross-reactivity with other proteins of the Asteraceae family and also with Parietaria judaica. This was demonstrated by immunoblotting and ELISA inhibition studies . CONCLUSION: S. jacobea constitute a newly discovered allergenic source. It shows cross-reactivity with other members of the Asteraceae plant family as well as with P. judaica.

↩

[45] - Egger M, Mutschlechner S, Wopfner N, Gadermaier G, Briza P, Ferreira F. Pollen-food syndromes associated with weed pollinosis: an update from the molecular point of view. Allergy 2006;61:461-476

Pollinosis patients often display adverse reactions upon the ingestion of plant-derived foods as a result of immunoglobulin E (IgE) cross-reactive structures shared by pollen and food allergen sources. The symptoms of such pollen-food syndromes (PFS) or class 2 food allergies range from local oral allergy syndrome to severe systemic anaphylaxis. Two clinical syndromes, the celery-mugwort-spice syndrome and the mugwort-mustard-allergy syndrome have been described in association with weed pollinosis. However, other associations between weed pollinosis and hypersensitivity to certain kinds of food have also been observed, like the mugwort-peach, the ragweed-melon-banana, the plantain-melon, the pellitory-pistachio, the goosefoot-fruit, the Russian thistle-saffron, and the hop-celery association. The number of allergen sources involved, the allergens, and influencing factors including geography, diet, and food preparation contribute to the high clinical complexity of PFS. So far, known causative cross-reactive allergens include profilins, lipid transfer proteins, and high-molecular weight allergens and/or glycoallergens. The current usage of nonstandardized allergen extracts poses additional problems for both diagnosis and therapy of PFS patients. Further identification and characterization of involved allergens is inescapable for better understanding of PFS and vaccine development. Panels of recombinant allergens and/or hypo-allergens are promising tools to improve both PFS diagnostics and therapy.

↩

[46] - de la Torre Morin F, Sanchez Machin I, Garcia Robaina JC, Fernandez-Caldas E, Sanchez Trivino M. Clinical cross-reactivity between Artemisia vulgaris and Matricaria chamomilla (Chamomile). J Investig Allergol Clin Immunol 2001;11:118-122

Artemisia vulgaris is a common weed and an important source of allergens on the subtropical island of Tenerife, Canary Islands, Spain. It pollinates mainly from July to September, although, due to some local climatic conditions, it may flower throughout the year. Cross-reactivity with hazelnut, kiwi, birch, several Compositae (Ambrosia, Chrysanthemum, Matricaria, Solidago) and grass allergens has been suggested. Few studies have addressed the issue of in vivo cross-reactivity between A. vulgaris and Matricaria chamomilla. The objective of this study was to perform conjunctival and bronchial challenges with A. vulgaris and M. chamomilla and oral challenge with chamomile in 24 patients with asthma and/or rhinitis sensitized primarily to A. vulgaris. Skin prick tests with M. chamomilla were positive in 21 patients. Eighteen patients had a positive conjunctival provocation test with a A. vulgaris pollen extract and 13 patients had a positive conjunctival provocation test with a M. chamomilla pollen extract. Bronchial provocation tests with A. vulgaris were positive in 15 patients and with M. chamomilla pollen in another 16 individuals. Oral provocation tests, conducted with a commercial chamomile infusion were positive in 13 patients. Nine of these individuals were skin test positive to food allergens and 17 to others pollens of the Compositae family. This study confirms a high degree of in vivo cross-reactivity between A. vulgaris and M. chamomilla. Sensitization to A. vulgaris seems to be a primary risk factor for experiencing symptoms after the ingestion of chamomile infusions. Based on the results of bronchial provocation tests, M. chamomilla pollen could be a relevant inhalant allergen.

↩

Les allergènes des pollens d’Astéracées

Réactivité croisée entre différents pollens d’Astéracées

Réactions croisées entre pollens d’Astéracées et d’autres pollens

Réactions croisées entre pollens d’Astéracées et aliments

Rubriques

Dans la même rubrique

Les Amaranthacées

Les ambroisies

L’armoise

Les plantains

Les Euphorbiacées

Les Pariétaires