Hevea brasiliensis prohevein possesses a conserved C-terminal domain with amyloid-like properties in vitro
| dc.rights.license | open | |
| hal.structure.identifier | Laboratoire de Chimie des Polymères Organiques [LCPO] | |
| hal.structure.identifier | Team 1 LCPO : Polymerization Catalyses & Engineering | |
| dc.contributor.author | BERTHELOT, Karine | |
| dc.contributor.author | LECOMTE, Sophie | |
| hal.structure.identifier | Institut de biochimie et génétique cellulaires [IBGC] | |
| dc.contributor.author | COULARY-SALIN, Bénédicte | |
| hal.structure.identifier | Centre de Recherche Paul Pascal [CRPP] | |
| dc.contributor.author | BENTALEB, Ahmed | |
| 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.date.accessioned | 2020 | |
| dc.date.available | 2020 | |
| dc.date.issued | 2016 | |
| dc.identifier.issn | 1570-9639 | |
| dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/20179 | |
| dc.description.abstractEn | 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. (C) 2016 Elsevier B.V. All rights reserved. | |
| dc.language.iso | en | |
| dc.publisher | Elsevier | |
| dc.subject.en | Hevein | |
| dc.subject.en | Plant amyloid | |
| dc.subject.en | FTIR | |
| dc.subject.en | Protein aggregation | |
| dc.subject.en | Latex allergen | |
| dc.subject.en | MAJOR LATEX ALLERGEN | |
| dc.subject.en | RUBBER PARTICLE PROTEINS | |
| dc.subject.en | TREE | |
| dc.subject.en | AGGLUTININ | |
| dc.subject.en | EXPRESSION | |
| dc.subject.en | LUTOIDS | |
| dc.subject.en | EPITOPE | |
| dc.subject.en | ELECTROPHORESIS | |
| dc.subject.en | DETERMINANTS | |
| dc.subject.en | MICROFIBRILS | |
| dc.title.en | Hevea brasiliensis prohevein possesses a conserved C-terminal domain with amyloid-like properties in vitro | |
| dc.type | Article de revue | |
| dc.identifier.doi | 10.1016/j.bbapap.2016.01.006 | |
| dc.subject.hal | Chimie/Polymères | |
| bordeaux.journal | Biochimica et Biophysica Acta Proteins and Proteomics | |
| bordeaux.page | 388-399 | |
| bordeaux.volume | 1864 | |
| bordeaux.hal.laboratories | Laboratoire de Chimie des Polymères Organiques (LCPO) - UMR 5629 | * |
| bordeaux.issue | 4 | |
| bordeaux.institution | Bordeaux INP | |
| bordeaux.institution | Université de Bordeaux | |
| bordeaux.peerReviewed | oui | |
| hal.identifier | hal-01383079 | |
| hal.version | 1 | |
| hal.origin.link | https://hal.archives-ouvertes.fr//hal-01383079v1 | |
| bordeaux.COinS | ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Biochimica%20et%20Biophysica%20Acta%20%20Proteins%20and%20Proteomics&rft.date=2016&rft.volume=1864&rft.issue=4&rft.spage=388-399&rft.epage=388-399&rft.eissn=1570-9639&rft.issn=1570-9639&rft.au=BERTHELOT,%20Karine&LECOMTE,%20Sophie&COULARY-SALIN,%20B%C3%A9n%C3%A9dicte&BENTALEB,%20Ahmed&PERUCH,%20Fr%C3%A9d%C3%A9ric&rft.genre=article |
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