Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Pathogenesis-related proteins of plants as allergens
Autore:
Midoro-Horiuti, T; Brooks, EG; Goldblum, RM;
Indirizzi:
Univ Texas, Med Branch, Child Hlth Res Ctr, Dept Pediat, Galveston, TX 77555 USA Univ Texas Galveston TX USA 77555 r, Dept Pediat, Galveston, TX 77555 USA
Titolo Testata:
ANNALS OF ALLERGY ASTHMA & IMMUNOLOGY
fascicolo: 4, volume: 87, anno: 2001,
pagine: 261 - 271
SICI:
1081-1206(200110)87:4<261:PPOPAA>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
JUNIPERUS-ASHEI POLLEN; AMINO-ACID-SEQUENCE; LIPID-TRANSFER PROTEINS; JUDAICA MAJOR ALLERGEN; THAUMATIN-LIKE PROTEIN; NATURAL-RUBBER LATEX; SALICYLIC-ACID; CROSS-REACTIVITY; JASMONIC ACID; MOLECULAR CHARACTERIZATION;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Citazioni:
84
Recensione:
Indirizzi per estratti:
Indirizzo: Midoro-Horiuti, T Univ Texas, Med Branch, Child Hlth Res Ctr, Dept Pediat,Route 0366, Galveston, TX 77555 USA Univ Texas Route 0366 Galveston TX USA77555 X 77555 USA
Citazione:
T. Midoro-Horiuti et al., "Pathogenesis-related proteins of plants as allergens", ANN ALLER A, 87(4), 2001, pp. 261-271

Abstract

Objective: Many pathogenesis-related (PR) proteins from plants are allergenic. We review the evidence that PR proteins represent an increasingly important group of plant-derived allergens. Data Sources: A detailed literature search was conducted through PubMed and GenBank databases. Study Selection: All reports in PubMed and GenBank related to PR protein allergens for which at least partial amino acid sequence is known were included. Results: Production of PR proteins by plants is induced in plants by stress. Members of PR-protein groups 2, 3, 4, 5, 8, 10, and 14 have demonstratedallergenicity. PR2-, 3-, 4-, and 8-homologous allergens are represented bythe latex allergens. Cross-reactivity of PR3 latex allergen, Hev b 6.02, with some fruit allergens may be a reflection of the representation of homologous PR proteins among varied plants. The expression of one of the representative PR5-homologous cedar pollen allergens, Jun a 3, is highly variable across years and geographic areas, possibly because of variable induction of this PR protein by environmental factors. PR10-homologous birch pollen allergen, Bet v 1, is structurally similar to and cross-reacts with PR10 proteins from fruits (eg, Mal d 1) which cause oral allergy syndrome. PR14 allergens (eg, Zea m 14) consist of lipid transfer proteins found in grains andfruits and are inducers of anaphylaxis. Conclusions: PR-homologous allergens are pervasive in nature. Similarity in the amino acid sequences among members of PR proteins may be responsible for cross-reactivity among allergens from diverse plants. Induced expression of PR-homologous allergens by environmental factors may explain varying degrees of allergenicity. Man-made environmental pollutants may also alter the expression of some PR protein allergens.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 02:49:02