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Titolo:
Molecular basis of allergic cross-reactivity between group 1 major allergens from birch and apple
Autore:
Holm, J; Baerentzen, G; Gajhede, M; Ipsen, H; Larsen, JN; Lowenstein, H; Wissenbach, M; Spangfort, MD;
Indirizzi:
ALK Abello AS, Biochem Allergy Res, DK-2970 Horsholm, Denmark ALK Abello AS Horsholm Denmark DK-2970 gy Res, DK-2970 Horsholm, Denmark Univ Copenhagen, Dept Chem, Prot Struct Grp, DK-2100 Copenhagen, Denmark Univ Copenhagen Copenhagen Denmark DK-2100 , DK-2100 Copenhagen, Denmark
Titolo Testata:
JOURNAL OF CHROMATOGRAPHY B
fascicolo: 1-2, volume: 756, anno: 2001,
pagine: 307 - 313
SICI:
1387-2273(20010525)756:1-2<307:MBOACB>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
BET-V-I; CAR-B-I; POLLEN ALLERGEN; IMMUNOLOGICAL RELATIONSHIP; CARPINUS-BETULUS; X-RAY; BET-V-1; HORNBEAM; PROTEIN; MAL-D-1;
Keywords:
food allergy; cross-reactivity; birch; apple;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
19
Recensione:
Indirizzi per estratti:
Indirizzo: Spangfort, MD ALK Abello AS, Biochem Allergy Res, Boge Alle 6-8, DK-2970 Horsholm, Denmark ALK Abello AS Boge Alle 6-8 Horsholm Denmark DK-2970 enmark
Citazione:
J. Holm et al., "Molecular basis of allergic cross-reactivity between group 1 major allergens from birch and apple", J CHROMAT B, 756(1-2), 2001, pp. 307-313

Abstract

Patients allergic to birch pollen often also react with fruits and vegetables, such as apple. The major cause of cross-reactivity between birch and apple is biochemical and immunological similarity between the major allergens, Bet v 1 and Mal d 1, as demonstrated by serological and cellular immunoassays. In addition, birch pollen-specific therapeutic allergy vaccination has been shown to improve allergic symptoms caused by oral ingestion of apple. Detailed analysis of molecular surface areas based on the crystal structure of Bet v 1,,and primary sequence alignment, identify potential epitopesfor cross-reactive antibodies. Two or more conserved patches are identified when comparing Bet v 1 and Mal d 1, thus providing a molecular model for serological cross-reactivity involving more than one IgE-binding epitope. Aminimum of two epitopes would be necessary for cross-linking of receptor bound IgE in functional histamine release assays and skin test. Individual amino acid substitutions, as occurring in isoallergenic variation, may, however, have a dramatic effect on epitope integrity if critical residues are affected. Thus, one area large enough to accommodate antibody-binding epitopes shared by all known Mal d 1 isoallergens and variants is identified, as well as areas shared by Bet v 1 and individual Mal d 1 isoallergens or variants. The occurrence of limited epitope coincidence between Bet v 1 and Mald 1 is in agreement with the observation that some, but not all, birch pollen allergic patients react with apple, and that the epitope repertoire recognised by the IgE of the individual patients determines the degree of cross-reactivity. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/10/20 alle ore 16:22:07