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Titolo:
Gastrodianin-like mannose-binding proteins: a novel class of plant proteins with antifungal properties
Autore:
Wang, XC; Bauw, G; Van Damme, EJM; Peumans, WJ; Chen, ZL; Van Montagu, M; Angenon, G; Dillen, W;
Indirizzi:
State Univ Ghent, Vlaams Interuniv Inst Biotechnol, Vakgrp Mol Genet, B-9000 Ghent, Belgium State Univ Ghent Ghent Belgium B-9000 p Mol Genet, B-9000 Ghent, Belgium State Univ Ghent, Vlaams Interuniv Inst Biotechnol, Dept Plantengenet, B-9000 Ghent, Belgium State Univ Ghent Ghent Belgium B-9000 lantengenet, B-9000 Ghent, Belgium Katholieke Univ Leuven, Lab Fytopathol & Plantenbescherming, B-3001 Heverlee, Belgium Katholieke Univ Leuven Heverlee Belgium B-3001 B-3001 Heverlee, Belgium Peking Univ, Coll Life Sci, Natl Lab Prot Engn & Plant Engn, Beijing 100871, Peoples R China Peking Univ Beijing Peoples R China 100871 ijing 100871, Peoples R China
Titolo Testata:
PLANT JOURNAL
fascicolo: 6, volume: 25, anno: 2001,
pagine: 651 - 661
SICI:
0960-7412(200103)25:6<651:GMPANC>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSGENIC TOBACCO PLANTS; SPECIES LISTERA-OVATA; MOLECULAR-CLONING; ANTIMICROBIAL PEPTIDES; EPIPACTIS-HELLEBORINE; ENHANCED RESISTANCE; MIRABILIS-JALAPA; ESCHERICHIA-COLI; ACTIN-BINDING; FUNGAL GROWTH;
Keywords:
antifungal protein; Epipactis helleborine; Gastrodia elata; lectin; mannose-binding protein; Orchidaceae;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
66
Recensione:
Indirizzi per estratti:
Indirizzo: Van Montagu, M State Univ Ghent, Vlaams Interuniv Inst Biotechnol, Vakgrp Mol Genet, KL Ledeganckstr 35, B-9000 Ghent, Belgium State Univ Ghent KL Ledeganckstr 35 Ghent Belgium B-9000 m
Citazione:
X.C. Wang et al., "Gastrodianin-like mannose-binding proteins: a novel class of plant proteins with antifungal properties", PLANT J, 25(6), 2001, pp. 651-661

Abstract

The orchid Gastrodia elata depends on the fungus Armillaria mellea to complete its life cycle. In the interaction, fungal hyphae penetrate older, nutritive corms but not newly formed corms. From these corms, a protein fraction with in vitro activity against plant-pathogenic fungi has previously been purified. Here, the sequence of gastrodianin, the main constituent of theantifungal fraction, is reported. Four isoforms that encoded two differentmature proteins were identified at the cDNA level. Another isoform was detected in sequenced peptides. Because the antifungal activity of gastrodianins produced in and purified from Escherichia coil and Nicotiana tabacum wascomparable to that of gastrodianin purified from the orchid, gastrodianinsare the active component of the antifungal fractions. Gastrodianin accumulation is probably an important part of the mechanism by which the orchid controls Armillaria penetration. Gastrodianin was found to be homologous to monomeric mannose-binding proteins of other orchids, of which at least one (Epipactis helleborine mannose-binding protein) also displayed in vitro antifungal activity. This establishes the gastrodianin-like proteins (GLIPs) asa novel class of antifungal proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/12/17 alle ore 23:37:31