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Identification of enolase as a laminin-binding protein on the surface of Staphylococcus aureus.
Carneiro, Celia R W; Postol, Edilberto; Nomizo, Regina; Reis, Luiz F L; Brentani, Ricardo R.
Afiliação
  • Carneiro CR; Discipline of Immunology, Microbiology, Immunology and Parasitology Department, Federal University of São Paulo, São Paulo, Brazil.
Microbes Infect ; 6(6): 604-8, 2004 May.
Article em En | MEDLINE | ID: mdl-15158195
We 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 alpha-enolase. Moreover, amino acid sequencing of the 52-kDa protein eluted from the 2-D gel indicated its molecular homology with alpha-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 alpha-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 alpha-enolase. Finally, the cell surface localization of S. aureus alpha-enolase was further confirmed by flow cytometry. Hence, alpha-enolase might play a critical role in the pathogenesis of S. aureus by allowing its adherence to laminin-containing extracellular matrix.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfopiruvato Hidratase / Staphylococcus aureus / Laminina / Receptores de Laminina Tipo de estudo: Diagnostic_studies Idioma: En Revista: Microbes Infect Assunto da revista: ALERGIA E IMUNOLOGIA / MICROBIOLOGIA Ano de publicação: 2004 Tipo de documento: Article País de afiliação: Brasil País de publicação: França
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfopiruvato Hidratase / Staphylococcus aureus / Laminina / Receptores de Laminina Tipo de estudo: Diagnostic_studies Idioma: En Revista: Microbes Infect Assunto da revista: ALERGIA E IMUNOLOGIA / MICROBIOLOGIA Ano de publicação: 2004 Tipo de documento: Article País de afiliação: Brasil País de publicação: França