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• W2117795272 abstract "Bacterial attachment to host tissue is considered to be a crucial primary step in pathogen infection. Previous studies have shown that Streptococcus defectivus adheres specifically to cell-secreted extracellular matrix (ECM). Though generally not exposed in vivo, this host tissue is exposed at endothelial cell junctions and sites of tissue injury. In this report, we identify a ca. 200-kDa surface protein of S. defectivus involved in ECM adherence. Nitrous acid-derived mutant strains that were unable to bind ECM and which failed to adsorb adhesin-specific antibody from polyclonal inhibitory sera were isolated. A surface protein (ca. 200 kDa) was absent from ECM-nonadherent mutants, indicating its involvement in ECM attachment. Additionally, affinity-purified antibody to the ca. 200-kDa protein inhibited whole-cell S. defectivus ECM attachment, whereas antibody to the same region of the nonadherent mutant cell wall-associated protein profile did not. Furthermore, solubilized cell wall-associated protein extracts of parent but not mutant strains bound ECM, confirming the significance of this protein in ECM adherence. Therefore, we propose that the ca. 200-kDa protein is the major S. defectivus surface component that mediates the ECM attachment of these organisms." @default.
• W2117795272 created "2016-06-24" @default.
• W2117795272 creator A5004568151 @default.
• W2117795272 creator A5047751063 @default.
• W2117795272 date "1993-12-01" @default.
• W2117795272 modified "2023-10-16" @default.
• W2117795272 title "Identification of the surface component of Streptococcus defectivus that mediates extracellular matrix adherence" @default.
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• W2117795272 doi "https://doi.org/10.1128/iai.61.12.4994-5000.1993" @default.
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