Yersinia pestis uses the Ail outer membrane protein to recruit vitronectin

Sara Schesser Bartra, Yi Ding, L. Miya Fujimoto, Joshua G. Ring, Vishal Jain, Sanjay Ram, Francesca M. Marassi, Gregory V. Plano

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


Yersinia pestis, the agent of plague, requires the Ail (attachment invasion locus) outer membrane protein to survive in the blood and tissues of its mammalian hosts. Ail is important for both attachment to host cells and for resistance to complement-dependent bacteriolysis. Previous studies have shown that Ail interacts with components of the extracellular matrix, including fibronectin, laminin and heparan sulfate proteoglycans, and with the complement inhibitor C4b-binding protein. Here, we demonstrate that Ail-expressing Y. pestis strains bind vitronectin – a host protein with functions in cell attachment, fibrinolysis and inhibition of the complement system. The Ail-dependent recruitment of vitronectin resulted in efficient cleavage of vitronectin by the outer membrane Pla (plasminogen activator protease). Escherichia coli DH5α expressing Y. pestis Ail bound vitronectin, but not heat-treated vitronectin. The ability of Ail to directly bind vitronectin was demonstrated by ELISA using purified refolded Ail in nanodiscs.

Original languageEnglish (US)
Pages (from-to)2174-2183
Number of pages10
JournalMicrobiology (United Kingdom)
Issue number11
StatePublished - Nov 2015

ASJC Scopus subject areas

  • Microbiology


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