Literature DB >> 27317253

Highlights on Hevea brasiliensis (pro)hevein proteins.

Karine Berthelot1, Frédéric Peruch2, Sophie Lecomte3.   

Abstract

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.

Entities:  

Keywords:  Antimicrobial peptides; Hev b 6 latex allergens; Hevein; Natural rubber; Plant amyloids; Prohevein

Mesh:

Substances:

Year:  2016        PMID: 27317253     DOI: 10.1016/j.biochi.2016.06.006

Source DB:  PubMed          Journal:  Biochimie        ISSN: 0300-9084            Impact factor:   4.079


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