Felek Suleyman, Lawrenz Matthew B, Krukonis Eric S
Department of Biologic and Materials Sciences, University of Michigan School of Dentistry, Ann Arbor, MI 48109-1078, USA.
Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO 63110, USA.
Microbiology (Reading). 2008 Jun;154(Pt 6):1802-1812. doi: 10.1099/mic.0.2007/010918-0.
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 DeltayapC 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.
YapC是一种推测的鼠疫耶尔森菌自转运蛋白，与产肠毒素大肠杆菌粘附素TibA具有高度同源性。作为鼠疫耶尔森菌一种潜在的重要表面蛋白，我们分析了YapC的多种活性。当在非致病性Fim(-)大肠杆菌菌株AAEC185中表达时，YapC介导了对鼠源巨噬细胞样细胞（RAW264.7）和人源上皮样细胞（HEp-2）的粘附。此外，YapC在大肠杆菌表面的表达导致在DMEM组织培养基中自动聚集，这一现象与耶尔森菌属的毒力有关。YapC还介导了大肠杆菌AAEC185形成生物膜样沉积物。鼠疫耶尔森菌菌株KIM5中yapC的缺失导致对RAW264.7或HEp-2细胞的粘附以及生物膜形成均无变化。鼠疫耶尔森菌DeltayapC突变体缺乏表型可能反映了通过RT-PCR评估的yapC在体外相对较低的表达水平，和/或在体外表达的冗余功能。这些数据证明了YapC的几种活性，其可能在鼠疫耶尔森菌感染过程中发挥作用。
