BERTHELOT, K.; LECOMTE, S.; COULARY-SALIN, B.; BENTALEB, A.; PERUCH, F.

doi:10.1016/j.bbapap.2016.01.006

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Biochim Biophys Acta. 2016, vol. 1864, n° 4, p. 388-399

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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.< Réduire

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

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