Hevea brasiliensis prohevein possesses a conserved C-terminal domain with amyloid-like properties in vitro
BERTHELOT, Karine
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 1 LCPO : Polymerization Catalyses & Engineering
See more >
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 1 LCPO : Polymerization Catalyses & Engineering
BERTHELOT, Karine
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 1 LCPO : Polymerization Catalyses & Engineering
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 1 LCPO : Polymerization Catalyses & Engineering
PERUCH, Frédéric
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 1 LCPO : Polymerization Catalyses & Engineering
< Reduce
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 1 LCPO : Polymerization Catalyses & Engineering
Language
en
Article de revue
This item was published in
Biochimica et Biophysica Acta Proteins and Proteomics. 2016, vol. 1864, n° 4, p. 388-399
Elsevier
English Abstract
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 ...Read more >
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.Read less <
English Keywords
Hevein
Plant amyloid
FTIR
Protein aggregation
Latex allergen
MAJOR LATEX ALLERGEN
RUBBER PARTICLE PROTEINS
TREE
AGGLUTININ
EXPRESSION
LUTOIDS
EPITOPE
ELECTROPHORESIS
DETERMINANTS
MICROFIBRILS
Origin
Hal imported