Related Experiment Video
Updated: Jul 4, 2026

Analysis of Yersinia enterocolitica Effector Translocation into Host Cells Using Beta-lactamase Effector Fusions
Published on: October 13, 2015
The Yersinia pestis autotransporter YapC mediates host cell binding, autoaggregation and biofilm formation
Suleyman Felek1, Matthew B Lawrenz2, Eric S Krukonis3,1
1Department of Biologic and Materials Sciences, University of Michigan School of Dentistry, Ann Arbor, MI 48109-1078, USA.
Abstract:
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.
Insights
The Yersinia pestis autotransporter protein YapC promotes bacterial attachment, autoaggregation, and biofilm formation. However, deleting yapC in Y. pestis did not alter these activities, suggesting functional redundancy.
Area of Science:
- Microbiology
- Molecular Biology
- Pathogen Virulence
Background:
- Yersinia pestis is a pathogenic bacterium responsible for plague.
- Autotransporter proteins are important virulence factors in Gram-negative bacteria.
- YapC shares homology with the enterotoxigenic Escherichia coli adhesin TibA.
Purpose of the Study:
- To investigate the functional activities of the Yersinia pestis autotransporter protein YapC.
- To determine YapC's role in bacterial adhesion, autoaggregation, and biofilm formation.
- To assess the in vivo relevance of YapC during Yersinia pestis infection.
Main Methods:
- Expression of YapC in a non-pathogenic E. coli strain (AAEC185).
- Assessing bacterial adhesion to macrophage (RAW264.7) and epithelial (HEp-2) cell lines.
- Evaluating autoaggregation and biofilm formation capabilities.
- Generating a yapC deletion mutant in Y. pestis strain KIM5 for phenotypic analysis.
- Quantitative reverse transcription PCR (RT-PCR) to assess yapC expression levels.
Main Results:
- YapC expression in E. coli mediated attachment to both RAW264.7 and HEp-2 cells.
- YapC facilitated autoaggregation and biofilm formation by E. coli.
- Deletion of yapC in Y. pestis did not affect adhesion or biofilm formation.
- RT-PCR indicated low in vitro expression of yapC in Y. pestis.
Conclusions:
- YapC exhibits adhesive, autoaggregative, and biofilm-forming properties in vitro.
- The lack of a clear phenotype in the Y. pestis DeltayapC mutant may be due to low yapC expression or functional redundancy.
- YapC has potential roles in Yersinia pestis pathogenesis that warrant further investigation.
Related Concept Videos
Plague
Fimbriae, Pili, and Axial Filaments
Intracellular Movement of Viruses and Bacteria
Biofilms
Yeast Signaling
Mechanism of Conjugation

