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Yersinia pestis uses the Ail outer membrane protein to recruit vitronectin

Sara Schesser Bartra1, Yi Ding2, L Miya Fujimoto2

  • 11​ Department of Microbiology and Immunology, University of Miami Miller School of Medicine, Miami, FL 33101, USA.

Microbiology (Reading, England)
|September 18, 2015
PubMed

Insights

Yersinia pestis's Ail protein binds the host protein vitronectin, aiding bacterial survival. This interaction facilitates vitronectin cleavage by the Pla protease, impacting bacterial pathogenesis.

Area of Science:

  • Microbiology
  • Pathogen-host interactions
  • Bacterial outer membrane proteins

Background:

  • Yersinia pestis causes plague and requires the Ail protein for survival in mammalian hosts.
  • Ail mediates bacterial attachment and resistance to complement-mediated lysis.
  • Ail interacts with extracellular matrix components and complement inhibitors.

Purpose of the Study:

  • To investigate the interaction between Yersinia pestis Ail protein and vitronectin.
  • To determine the functional consequences of Ail-vitronectin binding.

Main Methods:

  • ELISA using purified Ail in nanodiscs.
  • Assessing vitronectin binding by Ail-expressing Escherichia coli.
  • Evaluating vitronectin cleavage by the Pla protease.

Main Results:

  • Yersinia pestis strains expressing Ail bind host vitronectin.
  • Ail-dependent vitronectin recruitment leads to its efficient cleavage by Pla.
  • Ail directly binds vitronectin, as confirmed by ELISA.

Conclusions:

  • Ail facilitates Yersinia pestis interaction with vitronectin.
  • Vitronectin binding and subsequent cleavage by Pla are Ail-dependent mechanisms.
  • This interaction may contribute to Yersinia pestis pathogenesis by modulating host proteins.

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