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• W2104594786 abstract "ABSTRACT The binding of the Yersinia pseudotuberculosis and Yersinia enterocolitica invasin proteins to β 1 integrin receptors allows internalization of these organisms by cultured cells. The C-terminal 192-residue superdomain of the Y. pseudotuberculosis invasin is necessary and sufficient for integrin recognition, while a region located outside, and N-terminal to, this superdomain strongly enhances the efficiency of bacterial uptake. Within the enhancer region is a domain called D2 that allows invasin-invasin interaction. To investigate the role of the enhancer region, bacterial cell binding and entry mediated by the Y. pseudotuberculosis invasin protein (invasin pstb ) was compared to that of Y. enterocolitica invasin (invasin ent ), which lacks the D2 self-association domain. Invasin ent was shown to be unable to promote self-interaction, using the DNA binding domain of λ repressor as a reporter. Furthermore, two genetically engineered in-frame deletion mutations that removed D2 from invasin pstb were significantly less proficient than wild-type invasin pstb at promoting uptake, although the amount of surface-exposed invasin as well as the cell binding capacity of the recombinant Escherichia coli strains remained similar. Competitive uptake assays showed that E. coli cells expressing invasin pstb had a significant advantage in the internalization process versus either E. coli cells expressing invasin ent or the invasin pstb derivatives deleted for D2, further demonstrating the importance of invasin self-interaction for the efficiency of invasin-mediated uptake." @default.
• W2104594786 created "2016-06-24" @default.
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• W2104594786 date "2000-05-01" @default.
• W2104594786 modified "2023-10-02" @default.
• W2104594786 title "An Immunoglobulin Superfamily-Like Domain Unique to the <i>Yersinia pseudotuberculosis</i> Invasin Protein Is Required for Stimulation of Bacterial Uptake via Integrin Receptors" @default.
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• W2104594786 doi "https://doi.org/10.1128/iai.68.5.2930-2938.2000" @default.
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