The immunological relationship of epitopes on major tree pollen allergens

Rohac, Madeleine; Birkner, Thomas; Reimitzer, Ingrid; Bohle, Barbara; Steiner, Robert F.; Breitenbach, Michael; Kraft, Dietrich; Scheiner, Otto; Gabl, F; Rumpold, Helmut

doi:10.1016/0161-5890(91)90054-n

Cited by 69 publications

(43 citation statements)

References 15 publications

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“…Birch pollen allergen, Bet v 1 (9,12), was chosen as a model because it represents the major allergen for Ͼ 95% of tree pollen and plant food allergic patients and Ͼ 60% of these patients are sensitized exclusively to Bet v 1 (12,13). In addition, Bet v 1 binds a high percentage of specific serum IgE antibodies and shares B cell as well as T cell epitopes with homologous allergens present in tree pollen and plant-derived food (15,16,(31)(32)(33)(34).…”

Section: Discussionmentioning

confidence: 99%

Conversion of the major birch pollen allergen, Bet v 1, into two nonanaphylactic T cell epitope-containing fragments: candidates for a novel form of specific immunotherapy.

Vrtala¹,

Hirtenlehner²,

Vangelista³

et al. 1997

J. Clin. Invest.

199

230

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Section: Discussionmentioning

confidence: 99%

Conversion of the major birch pollen allergen, Bet v 1, into two nonanaphylactic T cell epitope-containing fragments: candidates for a novel form of specific immunotherapy.

Vrtala¹,

Hirtenlehner²,

Vangelista³

et al. 1997

J. Clin. Invest.

199

230

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“…This is expected to be more pronounced for pollens from trees belonging to the same botanical order or family. In fact, there is evidence for cross-reactivity among pollen extracts of the order Fagales (alder, birch, hazel and hornbeam) [25], as well as among common cypress and Japanese cedar pollens (Pinales) [26]. These cross-reactivities have been associated with the presence of common epitopes in their major allergens, and are correlated with either similar amino acid sequences of polypeptide segments or common carbohydrate determinants [9,27,281.…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of an olive allergen‐like protein from lilac pollen

Batanero

Villalba

López-Otı́n

et al. 1994

European Journal of Biochemistry

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An olive allergen‐like protein has been isolated from lilac (Syringa vulgaris) pollen extract. The protein can be considered as an allergen since is recognized by IgE from olive hypersensitive human sera, and has been called Syr v I (IUIS nomenclature). This protein consists of a glycosylated polypeptide of 20 kDa, which has an amino acid composition, spectroscopic properties, and an N‐terminal sequence similar to the major allergen from olive pollen, Ole e I. The lilac allergen is recognized by rabbit polyclonal antisera raised against olive allergen as well as by an Ole e I‐specific monoclonal antibody. Using a polymerase chain reaction strategy, based on the similarities observed between these olive and lilac proteins, three cDNA clones encoding Syr v I have been isolated and sequenced. These clones code for a polymorphic protein of 145 residues with a derived molecular mass of about 16400Da, which contains a potential N‐glycosylation site. Comparison of the deduced amino acid sequences of these Syr v I isoforms to each other revealed identities of 90–97%. Moreover, these sequences showed a high degree of similarity (85.5–89.6% identity) with Ole e I. The structural and immunological characterization of Syr v I justify the cross‐reactions observed between olive and lilac pollen extracts. The molecular cloning of Syr v I is relevant for the epitope mapping in Oleacease allergens, and may contribute to an improvement in the design of reagents for diagnosis and therapy of IgE‐dependent allergic reactions.

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“…Because of the high homology in the major allergens of the family Betulaceae, either polyclonal antibodies against birch pollen (Eriksson et al 1987, Valenta et al 1991a or monoclonal Bet B Z (Rohac et al 1991) have been recommended for diagnostic and therapeutic measurement. Our results show that for aerobiological monitoring at least alder pollen antigens are adequately detected by the IgG-ELISA analysis now in use.…”

Section: E Peliboiieii ( I I I D a Raritio-lelitiiiiiikimentioning

confidence: 99%