Src homology domain 2 adaptors affect adherence of Salmonella enterica serovar Typhimurium to non-phagocytic cells
Author(s) -
Erin C. Boyle,
Nat F. Brown,
John H. Brumell,
B. Brett Finlay
Publication year - 2007
Publication title -
microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.019
H-Index - 179
eISSN - 1465-2080
pISSN - 1350-0872
DOI - 10.1099/mic.0.2007/008581-0
Subject(s) - internalization , salmonella enterica , microbiology and biotechnology , biology , salmonella , proto oncogene tyrosine protein kinase src , actin , actin cytoskeleton , cytoskeleton , receptor , signal transducing adaptor protein , serotype , cell , signal transduction , bacteria , biochemistry , genetics
The ability of Salmonella enterica serovar Typhimurium (S. Typhimurium) to penetrate the intestinal epithelium is key to its pathogenesis. Bacterial invasion can be seen as a two-step process initially requiring adherence to the host cell surface followed by internalization into the host cell. Evidence suggests that adherence of S. Typhimurium to host cells is receptor-mediated; however, the host cell receptor(s) has/have not been identified. Internalization of S. Typhimurium absolutely requires the actin cytoskeleton yet only a few of the cytoskeletal components involved in this process have been identified. In order to identify host proteins that may play a role in S. Typhimurium invasion, the recruitment of actin-associated proteins was investigated. The contribution of recruited Src homology 2 adaptor proteins to invasion was further investigated and it was found that, while not involved in bacterial internalization itself, the adaptors Nck and ShcA influenced adherence of S. Typhimurium to non-phagocytic cells.
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