BERTHELOT, Karine; LECOMTE, Sophie; COULARY-SALIN, Bénédicte; BENTALEB, Ahmed; PERUCH, Frédéric

doi:10.1016/j.bbapap.2016.01.006

Métadonnées

Licence d’utilisation du document

BERTHELOT, Karine
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 1 LCPO : Polymerization Catalyses & Engineering

LECOMTE, Sophie

COULARY-SALIN, Bénédicte
Institut de biochimie et génétique cellulaires [IBGC]

Langue

Article de revue

Ce document a été publié dans

Biochimica et Biophysica Acta Proteins and Proteomics. 2016, vol. 1864, n° 4, p. 388-399

Elsevier

Résumé en anglais

Prohevein is a wound-induced protein and a main allergen from latex of Hevea brasiliensis (rubber tree). This 187 amino-acid protein is cleaved in two fragments: a N-terminal 43 amino-acids called hevein, a lectin bearing a chitin-binding motif with antifungal properties and a C-terminal domain (C-ter) far less characterized. We provide here new insights on the characteristics of prohevein, hevein and C-terminal domain. Using complementary biochemical (ThT/CR/chitin binding, agglutination) and structural (modeling, ATR-FTIR, TEM, WAXS) approaches, we show that this domain clearly displays all the characteristics of an amyloid-like proteins in vitro, that could confer agglutination activity in synergy with its chitin-binding activity. Additionally, this C-ter domain is highly conserved and present in numerous plant prohevein-like proteins or pathogenesis-related (PR and WIN) proteins. This could be the hallmark of the eventual presence of proteins with amyloid properties in plants, that could potentially play a role in defense through aggregation properties. (C) 2016 Elsevier B.V. All rights reserved.< Réduire

Mots clés en anglais

Hevein

Plant amyloid

FTIR

Protein aggregation

Latex allergen

MAJOR LATEX ALLERGEN

RUBBER PARTICLE PROTEINS

TREE

AGGLUTININ

EXPRESSION

LUTOIDS

EPITOPE

ELECTROPHORESIS

DETERMINANTS

MICROFIBRILS

Métadonnées

Partager cette publication !

Licence d’utilisation du document

Hevea brasiliensis prohevein possesses a conserved C-terminal domain with amyloid-like properties in vitro

Langue

Ce document a été publié dans

Résumé en anglais

Mots clés en anglais

URI

DOI

Origine

Unités de recherche