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