Karine Berthelot, Frédéric Peruch, Sophie Lecomte
Journal: Biochimie 2017;127():258-70
PMID: 27317253
Hevein, from Hevea brasiliensis (rubber tree), was identified in 1960. It is the most abundant soluble protein (22%) found in latex. Hevein is formed from a larger protein called prohevein. The 187 amino-acid prohevein is cleaved into two fragments: the N-terminal 43 amino-acid hevein, a lectin bearing a chitin-binding motif with antifungal properties, and a C-terminal domain (C-ter), which possesses amyloid properties. Hevein-like proteins are also widely represented in the plant kingdom and belong to a larger family related to stress and pathogenic responses. During the last 55 years, these proteins have attracted the interest of numerous specialists from the fields of plant physiology, genetics, molecular and structural biology, and physico-chemistry to allergology. This review highlights various aspects of hevein, prohevein, and C-ter from the point of view of these various fields, and examines their potential roles in latex as well as their beneficial and negative biological effects (e.g. wound sealing and resistance to pathogens which is mediated by agglutination, antimicrobial activity, and/or allergenicity). It covers results and observations from 1960 up to the most recent research.
Copyright © 2016 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.
Other Literature Sources:
Full Text Sources:
© Copyright 2026, Nutrition Evidence
We use cookies to improve your experience and analyze site traffic with Google Analytics. By continuing to use our site, you agree to our use of cookies. Learn more.