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Hevea brasiliensis prohevein possesses a conserved C-terminal domain with amyloid-like properties in vitro

dc.rights.licenseopen
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 1 LCPO : Polymerization Catalyses & Engineering
dc.contributor.authorBERTHELOT, Karine
dc.contributor.authorLECOMTE, Sophie
hal.structure.identifierInstitut de biochimie et génétique cellulaires [IBGC]
dc.contributor.authorCOULARY-SALIN, Bénédicte
hal.structure.identifierCentre de Recherche Paul Pascal [CRPP]
dc.contributor.authorBENTALEB, Ahmed
hal.structure.identifierLaboratoire de Chimie des Polymères Organiques [LCPO]
hal.structure.identifierTeam 1 LCPO : Polymerization Catalyses & Engineering
dc.contributor.authorPERUCH, Frédéric
IDREF: 152900748
dc.date.accessioned2020
dc.date.available2020
dc.date.issued2016
dc.identifier.issn1570-9639
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/20179
dc.description.abstractEnProhevein 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.isoen
dc.publisherElsevier
dc.subject.enHevein
dc.subject.enPlant amyloid
dc.subject.enFTIR
dc.subject.enProtein aggregation
dc.subject.enLatex allergen
dc.subject.enMAJOR LATEX ALLERGEN
dc.subject.enRUBBER PARTICLE PROTEINS
dc.subject.enTREE
dc.subject.enAGGLUTININ
dc.subject.enEXPRESSION
dc.subject.enLUTOIDS
dc.subject.enEPITOPE
dc.subject.enELECTROPHORESIS
dc.subject.enDETERMINANTS
dc.subject.enMICROFIBRILS
dc.title.enHevea brasiliensis prohevein possesses a conserved C-terminal domain with amyloid-like properties in vitro
dc.typeArticle de revue
dc.identifier.doi10.1016/j.bbapap.2016.01.006
dc.subject.halChimie/Polymères
bordeaux.journalBiochimica et Biophysica Acta Proteins and Proteomics
bordeaux.page388-399
bordeaux.volume1864
bordeaux.hal.laboratoriesLaboratoire de Chimie des Polymères Organiques (LCPO) - UMR 5629*
bordeaux.issue4
bordeaux.institutionBordeaux INP
bordeaux.institutionUniversité de Bordeaux
bordeaux.peerReviewedoui
hal.identifierhal-01383079
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-01383079v1
bordeaux.COinSctx_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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