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Updated: Mar 26, 2026

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
Published on: August 28, 2012
Hevea brasiliensis prohevein possesses a conserved C-terminal domain with amyloid-like properties in vitro
Karine Berthelot1, Sophie Lecomte2, Bénédicte Coulary-Salin3
1CNRS, CBMN, UMR 5248, Univ. Bordeaux, Bordeaux INP, F-33600 Pessac, France; CNRS, LCPO, UMR 5629, Univ. Bordeaux, Bordeaux INP, F-33600 Pessac, France.
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 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.
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