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Title: Identification of enolase as a laminin-binding protein on the surface of Staphylococcus aureus
Authors: Carneiro, CRW
Postol, E.
Nomizo, R.
Reis, LFL
Brentani, R. R.
Hosp Canc AC Camargo
Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Ludwig Inst Canc Res
Keywords: Staphylococcus aureus
laminin receptor
monoclonal antibodies
plasminogen activation
Issue Date: 1-May-2004
Publisher: Elsevier B.V.
Citation: Microbes and Infection. Amsterdam: Elsevier B.V., v. 6, n. 6, p. 604-608, 2004.
Abstract: 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.
ISSN: 1286-4579
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