Afficher la notice abrégée

hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorDURET, Sybille
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorBATAILLER, Brigitte
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorDUBRANA, Marie-Pierre
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorSAILLARD, Colette
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorRENAUDIN, Joël
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorBEVEN, Laure
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorARRICAU-BOUVERY, Nathalie
dc.date.issued2014
dc.identifier.issn1462-5814
dc.description.abstractEnSpiroplamas are helical, cell wall-less bacteria belonging to the Class Mollicutes, a group of microorganisms phylogenetically related to low G+C, Gram-positive bacteria. Spiroplasma species are all found associated with arthropods and a few, including Spiroplasma citri are pathogenic to plant. Thus S. citri has the ability to colonize cells of two very distinct hosts, the plant and the insect vector. While spiroplasmal factors involved in transmission by the leafhopper Circulifer haematoceps have been identified, their specific contribution to invasion of insect cells is poorly understood. In this study we provide evidence that the lipoprotein spiralin plays a major role in the very early step of cell invasion. Confocal laser scanning immunomicroscopy revealed a relocalization of spiralin at the contact zone of adhering spiroplasmas. The implication of a role for spiralin in adhesion to insect cells was further supported by adhesion assays showing that a spiralin-less mutant was impaired in adhesion and that recombinant spiralin triggered adhesion of latex beads. We also showed that cytochalasin D induced changes in the surface-exposed glycoconjugates, as inferred from the lectin binding patterns, and specifically improved adhesion of S. citri wild-type but not of the spiralin-less mutant. These results indicate that cytochalasin D exposes insect cell receptors of spiralin that are masked in untreated cells. In addition, competitive adhesion assays with lectins strongly suggest spiralin to exhibit glycoconjugate binding properties similar to that of the Vicia villosa agglutinin (VVA) lectin.
dc.language.isoen
dc.publisherWiley
dc.title.enInvasion of insect cells by Spiroplasma citri involves spiralin relocalization and lectin/glycoconjugate-type interactions
dc.typeArticle de revue
dc.identifier.doi10.1111/cmi.12265
dc.subject.halSciences du Vivant [q-bio]/Autre [q-bio.OT]
bordeaux.journalCellular Microbiology
bordeaux.page1119-1132
bordeaux.volume16
bordeaux.issue7
bordeaux.peerReviewedoui
hal.identifierhal-02637387
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02637387v1
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Cellular%20Microbiology&rft.date=2014&rft.volume=16&rft.issue=7&rft.spage=1119-1132&rft.epage=1119-1132&rft.eissn=1462-5814&rft.issn=1462-5814&rft.au=DURET,%20Sybille&BATAILLER,%20Brigitte&DUBRANA,%20Marie-Pierre&SAILLARD,%20Colette&RENAUDIN,%20Jo%C3%ABl&rft.genre=article


Fichier(s) constituant ce document

FichiersTailleFormatVue

Il n'y a pas de fichiers associés à ce document.

Ce document figure dans la(les) collection(s) suivante(s)

Afficher la notice abrégée