Identification of enolase as a laminin-binding protein on the surface of Staphylococcus aureus

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dc.contributor.authorCarneiro, Celia Regina Whitaker [UNIFESP]
dc.contributor.authorPostol, Edilberto
dc.contributor.authorNomizo, Regina
dc.contributor.authorReis, Luiz Fernando Lima
dc.contributor.authorBrentani, Ricardo Renzo
dc.contributor.institutionHosp Canc AC Camargo
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionLudwig Inst Canc Res
dc.date.accessioned2016-01-24T12:37:08Z
dc.date.available2016-01-24T12:37:08Z
dc.date.issued2004-05-01
dc.description.abstractWe have previously demonstrated that Staphylococcus aureus, a highly invasive bacteria, presents a 52-kDa surface protein that mediates its binding to laminin. in order to better characterize this receptor, we excised this putative laminin receptor from two-dimensional (2-D) PAGE and used it as antigen for raising a mouse hyperimmune serum which was for screening an S. aureus expression library. A single clone of 0.3 kb was obtained, and its sequence revealed 100% homology with S. aureus a-enolase. Moreover, amino acid sequencing of the 52-kDa protein eluted from the 2-D gel indicated its molecular homology with a-enolase, an enzyme that presents a high evolutionary conservation among species. in parallel, monoclonal antibodies raised against the S. aureus 52-kDa band also recognized yeast a-enolase in western blot analysis. These monoclonal antibodies were also able to promote capture of iodine-labeled bacteria when adsorbed to a solid phase, and this capture was inhibited by the addition of excess rabbit muscle a-enolase. Finally, the cell surface localization of S. aureus a-enolase was further confirmed by flow cytometry. Hence, a-enolase might play a critical role in the pathogenesis of S. aureus by allowing its adherence to laminin-containing extracellular matrix. (C) 2004 Elsevier SAS. All rights reserved.en
dc.description.affiliationHosp Canc AC Camargo, São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Microbiol Immunol & Parasitol, Discipline Immunol, São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Sch Med, Inst Heart, Immunol Lab, São Paulo, Brazil
dc.description.affiliationLudwig Inst Canc Res, Sau Paulo Branch, BR-01509010 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Microbiol Immunol & Parasitol, Discipline Immunol, São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent604-608
dc.identifierhttps://dx.doi.org/10.1016/j.micinf.2004.02.003
dc.identifier.citationMicrobes and Infection. Amsterdam: Elsevier B.V., v. 6, n. 6, p. 604-608, 2004.
dc.identifier.doi10.1016/j.micinf.2004.02.003
dc.identifier.issn1286-4579
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/27732
dc.identifier.wosWOS:000221835000012
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofMicrobes and Infection
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectStaphylococcus aureusen
dc.subjectLaminin receptoren
dc.subjectLamininen
dc.subjectEnolaseen
dc.subjectMonoclonal antibodiesen
dc.subjectPlasminogen activationen
dc.titleIdentification of enolase as a laminin-binding protein on the surface of Staphylococcus aureusen
dc.typeinfo:eu-repo/semantics/article
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