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

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

Autor Carneiro, CRW Google Scholar
Postol, E. Google Scholar
Nomizo, R. Google Scholar
Reis, LFL Google Scholar
Brentani, R. R. Google Scholar
Instituição Hosp Canc AC Camargo
Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Ludwig Inst Canc Res
Resumo 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 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.
Assunto Staphylococcus aureus
laminin receptor
monoclonal antibodies
plasminogen activation
Idioma Inglês
Data 2004-05-01
Publicado em Microbes and Infection. Amsterdam: Elsevier B.V., v. 6, n. 6, p. 604-608, 2004.
ISSN 1286-4579 (Sherpa/Romeo, fator de impacto)
Editor Elsevier B.V.
Extensão 604-608
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000221835000012

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