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Pla is a transmembrane \u03b2-barrel protein and member of the omptin family of outer membrane proteases which require bound lipopolysaccharide (LPS) to be proteolytically active. Plasminogen activation and autoprocessing of Pla were dramatically higher in<jats:italic>Y. pestis<\/jats:italic>cells grown at 37\u00b0C than in cells grown at 20\u00b0C; the difference in enzymatic activity by far exceeded the increase in the cellular content of the Pla protein.<jats:italic>Y. pestis<\/jats:italic>modifies its LPS structure in response to growth temperature. We purified His<jats:sub>6<\/jats:sub>-Pla under denaturing conditions and compared various LPS types for their capacity to enhance plasmin formation by His<jats:sub>6<\/jats:sub>-Pla solubilized in detergent. Reactivation of His<jats:sub>6<\/jats:sub>-Pla was higher with<jats:italic>Y. pestis<\/jats:italic>LPSs isolated from bacteria grown at 37\u00b0C than with LPSs from cells grown at 25\u00b0C. Lack of O antigens and the presence of the outer core region as well as a lowered level of acylation in LPS were found to enhance the Pla-LPS interaction. Genetic substitution of arginine 138, which is part of a three-dimensional protein motif for binding to lipid A phosphates, decreased both the enzymatic activity of His<jats:sub>6<\/jats:sub>-Pla and the amount of Pla in<jats:italic>Y. pestis<\/jats:italic>cells, suggesting the importance of the Pla-lipid A phosphate interaction. The temperature-induced changes in LPS are known to help<jats:italic>Y. pestis<\/jats:italic>to avoid innate immune responses, and our results strongly suggest that they also potentiate Pla-mediated proteolysis.<\/jats:p>","DOI":"10.1128\/iai.01329-09","type":"journal-article","created":{"date-parts":[[2010,4,6]],"date-time":"2010-04-06T00:26:28Z","timestamp":1270513588000},"page":"2644-2652","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":35,"title":["Temperature-Induced Changes in the Lipopolysaccharide of<i>Yersinia pestis<\/i>Affect Plasminogen Activation by the Pla Surface Protease"],"prefix":"10.1128","volume":"78","author":[{"given":"Marjo","family":"Suomalainen","sequence":"first","affiliation":[{"name":"General Microbiology, Department of Biosciences, FIN-00014 University of Helsinki, Helsinki, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leandro Araujo","family":"Lobo","sequence":"additional","affiliation":[{"name":"General Microbiology, Department of Biosciences, FIN-00014 University of Helsinki, Helsinki, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Klaus","family":"Brandenburg","sequence":"additional","affiliation":[{"name":"Divisions of Biophysics"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Buko","family":"Lindner","sequence":"additional","affiliation":[{"name":"Immunochemistry"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ritva","family":"Virkola","sequence":"additional","affiliation":[{"name":"General Microbiology, Department of Biosciences, FIN-00014 University of Helsinki, Helsinki, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuriy A.","family":"Knirel","sequence":"additional","affiliation":[{"name":"N. 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