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The\n            <jats:italic>Y. pestis<\/jats:italic>\n            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\n            <jats:italic>Y. pestis<\/jats:italic>\n            . 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\u00b0C and pH 7, the order of importance for adhesins in cell binding and cytotoxicity was Ail &gt; Pla &gt; Psa.\n            <jats:italic>Y. pestis<\/jats:italic>\n            grown at 37\u00b0C and pH 7 had equal contributions from Ail and Pla but an undetectable role for Psa. At 37\u00b0C 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 \u0394\n            <jats:italic>ail<\/jats:italic>\n            mutant was the most defective in mouse virulence. The expression level of\n            <jats:italic>ail<\/jats:italic>\n            was also the highest of the three adhesins in infected mouse tissues. Compared to an\n            <jats:italic>ail<\/jats:italic>\n            mutant, additional deletion of\n            <jats:italic>psaA<\/jats:italic>\n            (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\n            <jats:italic>Y. pestis<\/jats:italic>\n            .\n          <\/jats:p>","DOI":"10.1128\/iai.00167-10","type":"journal-article","created":{"date-parts":[[2010,8,3]],"date-time":"2010-08-03T02:16:02Z","timestamp":1280801762000},"page":"4134-4150","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":78,"title":["Three\n            <i>Yersinia pestis<\/i>\n            Adhesins Facilitate Yop Delivery to Eukaryotic Cells and Contribute to Plague Virulence"],"prefix":"10.1128","volume":"78","author":[{"given":"Suleyman","family":"Felek","sequence":"first","affiliation":[{"name":"Department of Biologic and Materials Sciences, University of Michigan School of Dentistry"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tiffany M.","family":"Tsang","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, University of Michigan School of Medicine, Ann Arbor, Michigan 48109"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eric S.","family":"Krukonis","sequence":"additional","affiliation":[{"name":"Department of Biologic and Materials Sciences, University of Michigan School of Dentistry"},{"name":"Department of Microbiology and Immunology, University of Michigan School of Medicine, Ann Arbor, Michigan 48109"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1099\/jmm.0.005678-0"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.01125-07"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.65.5.1659-1668.1997"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.81.5.704-714.1961"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.86.1.101-111.1963"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.00313-08"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.89.8.3561"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1078\/0171-9335-00098"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.149.3682.422"},{"key":"e_1_3_2_11_2","unstructured":"Cantor N. 2001. 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