| Three Yersinia pestis adhesins facilitate Yop delivery to eukaryotic cells and contribute to plague virulence. | |
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MedLine Citation:
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PMID: 20679446 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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To establish a successful infection, Yersinia pestis requires the delivery of cytotoxic Yops to host cells. Yops inhibit phagocytosis, block cytokine responses, and induce apoptosis of macrophages. The Y. pestis adhesin Ail facilitates Yop translocation and is required for full virulence in mice. To determine the contributions of other adhesins to Yop delivery, we deleted five known adhesins of Y. pestis. In addition to Ail, plasminogen activator (Pla) and pH 6 antigen (Psa) could mediate Yop translocation to host cells. The contribution of each adhesin to binding and Yop delivery was dependent upon the growth conditions. When cells were pregrown at 28°C and pH 7, the order of importance for adhesins in cell binding and cytotoxicity was Ail > Pla > Psa. Y. pestis grown at 37°C and pH 7 had equal contributions from Ail and Pla but an undetectable role for Psa. At 37°C and pH 6, both Ail and Psa contributed to binding and Yop delivery, while Pla contributed minimally. Pla-mediated Yop translocation was independent of protease activity. Of the three single mutants, the Δail mutant was the most defective in mouse virulence. The expression level of ail was also the highest of the three adhesins in infected mouse tissues. Compared to an ail mutant, additional deletion of psaA (encoding Psa) led to a 130,000-fold increase in the 50% lethal dose for mice relative to that of the KIM5 parental strain. Our results indicate that in addition to Ail, Pla and Psa can serve as environmentally specific adhesins to facilitate Yop secretion, a critical virulence function of Y. pestis. |
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Authors:
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Suleyman Felek; Tiffany M Tsang; Eric S Krukonis |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-08-02 |
Journal Detail:
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Title: Infection and immunity Volume: 78 ISSN: 1098-5522 ISO Abbreviation: Infect. Immun. Publication Date: 2010 Oct |
Date Detail:
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Created Date: 2010-09-22 Completed Date: 2010-11-12 Revised Date: 2011-07-27 |
Medline Journal Info:
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Nlm Unique ID: 0246127 Medline TA: Infect Immun Country: United States |
Other Details:
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Languages: eng Pagination: 4134-50 Citation Subset: IM |
Affiliation:
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Department of Biologic and Materials Sciences, University of Michigan School of Dentistry, Ann Arbor, MI 48109-1078, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adhesins, Bacterial
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metabolism* Animals Bacterial Adhesion / physiology Cell Line Female Gene Expression Regulation, Bacterial / physiology Humans Membrane Proteins / metabolism* Mice Mutation Plague / microbiology* Virulence Yersinia pestis / metabolism*, pathogenicity* |
| Chemical | |
Reg. No./Substance:
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0/Adhesins, Bacterial; 0/Membrane Proteins |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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