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

doi:10.1016/j.bbapap.2016.01.006

Metadatos

Licencia de uso del documento

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]

Idioma

Article de revue

Este ítem está publicado en

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

Elsevier

Resumen en inglés

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.< Leer menos

Palabras clave en inglés

Hevein

Plant amyloid

FTIR

Protein aggregation

Latex allergen

MAJOR LATEX ALLERGEN

RUBBER PARTICLE PROTEINS

TREE

AGGLUTININ

EXPRESSION

LUTOIDS

EPITOPE

ELECTROPHORESIS

DETERMINANTS

MICROFIBRILS

Metadatos

Compartir este ítem

Licencia de uso del documento

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

Idioma

Este ítem está publicado en

Resumen en inglés

Palabras clave en inglés

URI

DOI

Orígen

Centros de investigación