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Bap, a biofilm matrix protein of Staphylococcus aureus prevents cellular internalization through binding to GP96 host receptor

dc.contributor.authorValle Turrillas, Jaione
dc.contributor.authorLatasa Osta, Cristina
dc.contributor.authorGil Puig, Carmen
dc.contributor.authorToledo Arana, Alejandro
dc.contributor.authorSolano Goñi, Cristina
dc.contributor.authorPenadés, José R.
dc.contributor.authorLasa Uzcudun, Íñigo
dc.contributor.departmentIdAB. Instituto de Agrobiotecnología / Agrobioteknologiako Institutuaes_ES
dc.date.accessioned2016-11-04T15:34:18Z
dc.date.available2016-11-04T15:34:18Z
dc.date.issued2012
dc.description.abstractThe biofilm matrix, composed of exopolysaccharides, proteins, nucleic acids and lipids, plays a well-known role as a defence structure, protecting bacteria from the host immune system and antimicrobial therapy. However, little is known about its responsibility in the interaction of biofilm cells with host tissues. Staphylococcus aureus, a leading cause of biofilmassociated chronic infections, is able to develop a biofilm built on a proteinaceous Bap-mediated matrix. Here, we used the Bap protein as a model to investigate the role that components of the biofilm matrix play in the interaction of S. aureus with host cells. The results show that Bap promotes the adhesion but prevents the entry of S. aureus into epithelial cells. A broad analysis of potential interaction partners for Bap using ligand overlayer immunoblotting, immunoprecipitation with purified Bap and pull down with intact bacteria, identified a direct binding between Bap and Gp96/GRP94/Hsp90 protein. The interaction of Bap with Gp96 provokes a significant reduction in the capacity of S. aureus to invade epithelial cells by interfering with the fibronectin binding protein invasion pathway. Consistent with these results, Bap deficient bacteria displayed an enhanced capacity to invade mammary gland epithelial cells in a lactating mice mastitis model. Our observations begin to elucidate the mechanisms by which components of the biofilm matrix can facilitate the colonization of host tissues and the establishment of persistent infections.en
dc.description.sponsorshipJ.V. and A.T-A were supported by Spanish Ministry of Science and Innovation ‘‘Ramón y Cajal’’ contract. This work was supported by Spanish Ministry of Science and Innovation Grants BIO2008-05284-C02-01, AGL2011-23954 and the grant of Dpto. de Innovación from Gobierno de Navarra IIQ14066.RI1.en
dc.format.mimetypeapplication/pdfen
dc.identifier.doi10.1371/journal.ppat.1002843
dc.identifier.issn1553-7366 (Electronic)
dc.identifier.issn1553-7374 (Electronic)
dc.identifier.urihttps://academica-e.unavarra.es/handle/2454/22613
dc.language.isoengen
dc.publisherPublic Library of Scienceen
dc.relation.ispartofPLoS Pathogens 8(8): e1002843en
dc.relation.projectIDinfo:eu-repo/grantAgreement/MICINN//BIO2008-05284-C02-01/ES/en
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/6PN/AGL2011-23954en
dc.relation.publisherversionhttps://dx.doi.org/10.1371/journal.ppat.1002843
dc.rights© 2012 Valle et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en
dc.rights.accessRightsAcceso abierto / Sarbide irekiaes
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessen
dc.rights.urihttps://creativecommons.org/licenses/by/3.0/
dc.subjectStaphylococcus aureusen
dc.subjectBacterial biofilmsen
dc.subjectEpithelial cellsen
dc.subjectRecombinant proteinsen
dc.subjectMammary glandsen
dc.subjectMembrane proteinsen
dc.subjectProtein interactionsen
dc.subjectHost cellsen
dc.titleBap, a biofilm matrix protein of Staphylococcus aureus prevents cellular internalization through binding to GP96 host receptoren
dc.typeArtículo / Artikuluaes
dc.typeinfo:eu-repo/semantics/articleen
dc.type.versionVersión publicada / Argitaratu den bertsioaes
dc.type.versioninfo:eu-repo/semantics/publishedVersionen
dspace.entity.typePublication
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relation.isAuthorOfPublication.latestForDiscovery022e51f1-528f-49d1-901a-5a76313639df

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