Pathogenesis-related proteins of plants as allergens

Citation
T. Midoro-horiuti et al., Pathogenesis-related proteins of plants as allergens, ANN ALLER A, 87(4), 2001, pp. 261-271
Citations number
84
Categorie Soggetti
Clinical Immunolgy & Infectious Disease
Journal title
ANNALS OF ALLERGY ASTHMA & IMMUNOLOGY
ISSN journal
10811206 → ACNP
Volume
87
Issue
4
Year of publication
2001
Pages
261 - 271
Database
ISI
SICI code
1081-1206(200110)87:4<261:PPOPAA>2.0.ZU;2-0
Abstract
Objective: Many pathogenesis-related (PR) proteins from plants are allergen ic. We review the evidence that PR proteins represent an increasingly impor tant 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 al lergens for which at least partial amino acid sequence is known were includ ed. 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 demonstrated allergenicity. PR2-, 3-, 4-, and 8-homologous allergens are represented by the latex allergens. Cross-reactivity of PR3 latex allergen, Hev b 6.02, wi th some fruit allergens may be a reflection of the representation of homolo gous PR proteins among varied plants. The expression of one of the represen tative PR5-homologous cedar pollen allergens, Jun a 3, is highly variable a cross years and geographic areas, possibly because of variable induction of this PR protein by environmental factors. PR10-homologous birch pollen all ergen, Bet v 1, is structurally similar to and cross-reacts with PR10 prote ins from fruits (eg, Mal d 1) which cause oral allergy syndrome. PR14 aller gens (eg, Zea m 14) consist of lipid transfer proteins found in grains and fruits 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 f or cross-reactivity among allergens from diverse plants. Induced expression of PR-homologous allergens by environmental factors may explain varying de grees of allergenicity. Man-made environmental pollutants may also alter th e expression of some PR protein allergens.