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Volume 271, Number 38, Issue of September 20, 1996 pp. 23438-23444
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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A Region of the Yersinia pseudotuberculosis Invasin Protein That Contributes to High Affinity Binding to Integrin Receptors

(Received for publication, November 22, 1995, and in revised form, March 28, 1996)

Laura H. Saltman ^§ , Yin Lu ^§ , Evanthia M. Zaharias ^§ and Ralph R. Isberg ^§

From the  Howard Hughes Medical Institute, ^§ Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111

The entry of Yersinia pseudotuberculosis into cultured mammalian cells is mediated by the bacterial protein invasin. The mammalian receptors for invasin are five ₁ chain integrins. Site-directed mutagenesis of the aspartate and lysine residues in the 192-amino acid integrin binding domain of invasin was performed to identify regions, in addition to the previously characterized 903-913 region, that are important for integrin binding. One mutation, D811A, resulted in depressed ability of invasin to bind purified ₅₁ and to promote bacterial entry. Further mutational analysis of Asp-811 indicated that an oxygen-containing side chain is required at this position. A second nearby residue, Phe-808, was also shown to be important for integrin binding, as an alanine substitution at this site had properties similar to the Asp-811 mutation. This mutational analysis has therefore identified a second region that, in conjunction with residues 903-913, is required for wild type levels of integrin binding. The contribution to binding by two noncontiguous sites in the primary sequence parallels results that indicate two domains of fibronectin are involved in integrin binding.

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