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Research Article |
1 Department of Microbiology, Umeå University, 901 87 Umeå,
Sweden
2 Department of Medical Biochemistry and Microbiology, Uppsala University, BMC,
Box 582, 751 23 Uppsala, Sweden
3 Max Planck Institute for Biochemistry, Department of Molecular Medicine, Am
Klopferspitz 18A, 82152 Martinsried, Germany
* Author for correspondence (e-mail: maria.fallman{at}molbiol.umu.se )
Accepted 18 April 2002
Invasin of Yersinia pseudotuberculosis binds to ß1-integrins on host cells and triggers internalization of the bacterium. To elucidate the mechanism behind the ß1-integrin-mediated internalization of Yersinia, a ß1-integrin-deficient cell line, GD25, transfected with wild-type ß1A, ß1B or different mutants of the ß1A subunit was used. Both ß1A and ß1B bound to invasin-expressing bacteria, but only ß1A was able to mediate internalization of the bacteria. The cytoplasmic region of ß1A, differing from ß1B, contains two NPXY motifs surrounding a double threonine site. Exchanging the tyrosines of the two NPXYs to phenylalanines did not inhibit the uptake, whereas a marked reduction was seen when the first tyrosine (Y783) was exchanged to alanine. A similar reduction was seen when the two nearby threonines (TT788-9) were exchanged with alanines. It was also noted that cells affected in bacterial internalization exhibited reduced spreading capability when seeded onto invasin, suggesting a correlation between the internalization of invasin-expressing bacteria and invasin-induced spreading. Likewise, integrins defective in forming peripheral focal complex structures was unable to mediate uptake of invasin-expressing bacteria.
Key words: Invasin, ß1-integrin, Yersinia pseudotuberculosis, Focal complexes, Bacterial internalization
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