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The Yersinia pestis autotransporter YapC mediates host cell binding, autoaggregation and biofilm formation

¹ Department of Biologic and Materials Sciences, University of Michigan School of Dentistry, Ann Arbor, MI 48109-1078, USA
² Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO 63110, USA
³ Department of Microbiology and Immunology, University of Michigan School of Medicine, Ann Arbor, MI 48109-0620, USA

Correspondence
Eric S. Krukonis
ekrukoni{at}umich.edu

YapC, a putative Yersinia pestis autotransporter protein, shows strong homology to the enterotoxigenic Escherichia coli adhesin TibA. As a potentially important surface protein of Y. pestis, we analysed YapC for several activities. When expressed in the non-pathogenic Fim^– E. coli strain AAEC185, YapC mediated attachment to both murine-derived macrophage-like cells (RAW264.7) and human-derived epithelial-like cells (HEp-2). In addition, expression of YapC on the surface of E. coli led to autoaggregation in DMEM tissue culture medium, a phenomenon associated with virulence in Yersinia species. YapC also mediated formation of biofilm-like deposits by E. coli AAEC185. Deletion of yapC in Y. pestis strain KIM5 resulted in no change in adhesion to either RAW264.7 or HEp-2 cells, or in biofilm formation. Lack of a phenotype for the Y. pestis yapC mutant may reflect the relatively low level of yapC expression in vitro, as assessed by RT-PCR, and/or redundant functions expressed in vitro. These data demonstrate several activities for YapC that may function during Y. pestis infection.

A supplementary table of primers is available with the online version of this paper.

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