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Receptor-binding protein of lactococcus lactis phages : identification and characterization of the saccharide receptor-binding site

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bul.description.provenanceec spbfr
bul.rights.dateAccepPubl2006-03-17fr
bul.rights.periodeEmbargoforeverfr
bul.rights.raisonEmbargoInfiniPour que le document soit diffusé en libre accès, en accord avec le délai prescrit par l’éditeur de Journal of bacteriology, il faudrait déposer la version acceptée pour publication, incluant toutes les modifications demandées, mais sans la mise en page de la revue. Pour ce faire, effectuez une demande de modification à l’aide de la liste des dépôts diffusés à partir du tableau de suivi.fr
bul.rights.typeDatedatePublicationfr
dc.contributor.authorTremblay, Denise
dc.contributor.authorTegoni, Mariella
dc.contributor.authorLabrie, Steve
dc.contributor.authorSpinelli, Silvia
dc.contributor.authorMoineau, Sylvain
dc.contributor.authorCampanacci, Valérie
dc.contributor.authorBlangy, Stéphanie
dc.contributor.authorHuyghe, Céline
dc.contributor.authorDesmyter, Aline
dc.contributor.authorCambillau, Christian
dc.date.accessioned2020-04-14T12:20:41Z
dc.date.available9999-12-31
dc.date.issued2006-03-17
dc.description.abstractPhage p2, a member of the lactococcal 936 phage species, infects Lactococcus lactis strains by binding initially to specific carbohydrate receptors using its receptor-binding protein (RBP). The structures of p2 RBP, a homotrimeric protein composed of three domains, and of its complex with a neutralizing llama VH domain (VHH5) have been determined (S. Spinelli, A. Desmyter, C. T. Verrips, H. J. de Haard, S. Moineau, and C. Cambillau, Nat. Struct. Mol. Biol. 13:85–89, 2006). Here, we show that VHH5 was able to neutralize 12 of 50 lactococcal phages belonging to the 936 species. Moreover, escape phage mutants no longer neutralized by VHH5 were isolated from 11 of these phages. All of the mutations (but one) cluster in the RBP/VHH5 interaction surface that delineates the receptor-binding area. A glycerol molecule, observed in the 1.7-Å resolution structure of RBP, was found to bind tightly (Kd = 0.26 M) in a crevice located in this area. Other saccharides bind RBP with comparable high affinity. These data prove the saccharidic nature of the bacterial receptor recognized by phage p2 and identify the position of its binding site in the RBP head domain.fr
dc.identifier.doi10.1128/JB.188.7.2400-2410.2006fr
dc.identifier.issn0021-9193fr
dc.identifier.pubmed16547026fr
dc.identifier.urihttp://hdl.handle.net/20.500.11794/38729
dc.languageengfr
dc.publisherAmerican Society for Microbiologyfr
dc.rightshttp://purl.org/coar/access_right/c_16ec
dc.subject.rvmBactériophage P2fr
dc.subject.rvmLactococcus lactisfr
dc.subject.rvmProtéines de liaisonfr
dc.subject.rvmSaccharidesfr
dc.subject.rvmSites actifs (Biochimie)fr
dc.titleReceptor-binding protein of lactococcus lactis phages : identification and characterization of the saccharide receptor-binding sitefr
dc.typearticle de recherche
dc.type.legacyCOAR1_1::Texte::Périodique::Revue::Contribution à un journal::Article::Article de recherchefr
dcterms.bibliographicCitationJournal of bacteriology, Vol. 188 (7), 2400-2410 (2006)fr
dspace.accessstatus.time2023-05-24 18:04:57
dspace.entity.typePublication
relation.isAuthorOfPublication17224655-a23d-48b9-b40d-a5a58328ffde
relation.isAuthorOfPublication577a8fb6-1b11-4b5f-8f36-fe5a4d4ec9a9
relation.isAuthorOfPublication599b62d2-4b51-4b07-9539-3cef15723b3f
relation.isAuthorOfPublication.latestForDiscovery17224655-a23d-48b9-b40d-a5a58328ffde
relation.isResourceTypeOfPublication4c433ef5-3937-4530-8252-cca17d715747
relation.isResourceTypeOfPublication.latestForDiscovery4c433ef5-3937-4530-8252-cca17d715747
rioxxterms.project.funder-nameMarseille-Nice Génopolefr
rioxxterms.project.funder-nameUnileverfr
rioxxterms.project.funder-nameNatural Sciences and Engineering Research Council of Canadafr
rioxxterms.versionVersion of Record (VoR)fr
rioxxterms.version-of-recordhttps://doi.org/10.1128/JB.188.7.2400-2410.2006fr
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