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.

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.

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