Yersinia pestis uses the Ail outer membrane protein to recruit vitronectin
| Autor: | Vishal Jain, Gregory V. Plano, Sara Schesser Bartra, Francesca M. Marassi, L. Miya Fujimoto, Joshua G. Ring, Yi Ding, Sanjay Ram |
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| Rok vydání: | 2015 |
| Předmět: |
biology
Virulence Factors Yersinia pestis Hydrolysis Enzyme-Linked Immunosorbent Assay Plasma protein binding biology.organism_classification Microbiology Standard Complement system Fibronectin Plasminogen Activators Complement inhibitor Bacterial Proteins Laminin Host-Pathogen Interactions biology.protein Humans Vitronectin Bacterial outer membrane Bacterial Outer Membrane Proteins Protein Binding |
| Zdroj: | Microbiology. 161:2174-2183 |
| ISSN: | 1465-2080 1350-0872 |
| DOI: | 10.1099/mic.0.000179 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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