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• W2076202013 abstract "Invasin allows efficient entry into mammalian cells by Yersinia pseudotuberculosis. It has been shown that the C-terminal 192 amino acids of invasin are essential for binding of beta1 integrin receptors and subsequent uptake. By analyzing the internalization of latex beads coated with invasin derivatives, an additional domain of invasin was shown to be required for efficient bacterial internalization. A monomeric derivative encompassing the C-terminal 197 amino acids was inefficient at promoting entry of latex beads, whereas dimerization of this derivative by antibody significantly increased uptake. By using the DNA-binding domain of lambda repressor as a reporter for invasin self-interaction, we have demonstrated that a region of the invasin protein located N-terminal to the cell adhesion domain of invasin is able to self-associate. Chemical cross-linking studies of purified and surface-exposed invasin proteins, and the dominant-interfering effect of a non-functional invasin derivative are consistent with the presence of a self-association domain that is located within the region of invasin that enhances bacterial uptake. We conclude that interaction of homomultimeric invasin with multiple integrins establishes tight adherence and receptor clustering, thus providing a signal for internalization." @default.
• W2076202013 created "2016-06-24" @default.
• W2076202013 creator A5076382250 @default.
• W2076202013 creator A5078759067 @default.
• W2076202013 date "1999-03-01" @default.
• W2076202013 modified "2023-10-16" @default.
• W2076202013 title "A region of the Yersinia pseudotuberculosis invasin protein enhances integrin-mediated uptake into mammalian cells and promotes self-association" @default.
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• W2076202013 doi "https://doi.org/10.1093/emboj/18.5.1199" @default.
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