Highlights on Hevea brasiliensis (pro)hevein proteins
dc.rights.license | open | |
hal.structure.identifier | Laboratoire de Chimie des Polymères Organiques [LCPO] | |
dc.contributor.author | BERTHELOT, Karine | |
hal.structure.identifier | Laboratoire de Chimie des Polymères Organiques [LCPO] | |
hal.structure.identifier | Team 1 LCPO : Polymerization Catalyses & Engineering | |
dc.contributor.author | PERUCH, Frédéric
IDREF: 152900748 | |
dc.contributor.author | LECOMTE, Sophie | |
dc.date.accessioned | 2020 | |
dc.date.available | 2020 | |
dc.date.issued | 2016 | |
dc.identifier.issn | 0300-9084 | |
dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/20202 | |
dc.description.abstract | 6 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. (C) 2016 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved. | |
dc.language.iso | en | |
dc.publisher | Elsevier | |
dc.subject.en | HEALTH-CARE WORKERS | |
dc.subject.en | NATURAL-RUBBER LATEX | |
dc.subject.en | Hevein | |
dc.subject.en | Prohevein | |
dc.subject.en | Hey b 6 latex allergens | |
dc.subject.en | Natural rubber | |
dc.subject.en | Antimicrobial peptides | |
dc.subject.en | Plant amyloids | |
dc.subject.en | WHEAT-GERM-AGGLUTININ | |
dc.subject.en | LUTOID-BODY FRACTION | |
dc.subject.en | LECTIN-LIKE PROTEIN | |
dc.subject.en | B-CELL EPITOPES | |
dc.subject.en | CARBOHYDRATE INTERACTIONS | |
dc.subject.en | MOLECULAR RECOGNITION | |
dc.subject.en | BINDING-PROTEIN | |
dc.subject.en | FRUIT SYNDROME | |
dc.title.en | Highlights on Hevea brasiliensis (pro)hevein proteins | |
dc.type | Article de revue | |
dc.identifier.doi | 10.1016/j.biochi.2016.06.006 | |
dc.subject.hal | Chimie/Polymères | |
bordeaux.journal | Biochimie | |
bordeaux.page | 258-270 | |
bordeaux.volume | 127 | |
bordeaux.hal.laboratories | Laboratoire de Chimie des Polymères Organiques (LCPO) - UMR 5629 | * |
bordeaux.institution | Bordeaux INP | |
bordeaux.institution | Université de Bordeaux | |
bordeaux.peerReviewed | oui | |
hal.identifier | hal-01372321 | |
hal.version | 1 | |
hal.origin.link | https://hal.archives-ouvertes.fr//hal-01372321v1 | |
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