Identification of enolase as a laminin-binding protein on the surface of Staphylococcus aureus |
| |
Authors: | Carneiro Celia R W Postol Edilberto Nomizo Regina Reis Luiz F L Brentani Ricardo R |
| |
Institution: | 1. Discipline of Immunology, Microbiology, Immunology and Parasitology Department, Federal University of São Paulo, São Paulo, Brazil;2. Laboratory of Immunology—Heart Institute, University of São Paulo School of Medicine, São Paulo, Brazil;3. Hospital do Câncer A.C. Camargo, São Paulo, Brazil;4. Ludwig Institute for Cancer Research, Ruo Prof. Antonio Prudente 109/4A, São Paulo branch, 01509-010 São Paulo, SP, Brazil |
| |
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 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. |
| |
Keywords: | |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|