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The post\u2010translocation chaperone PrsA2 has been adapted to assist in the folding and activity of <jats:italic>L. monocytogenes<\/jats:italic> secreted proteins required for bacterial replication within host cells. Here we present the first structure\/function investigation of the contributions of PrsA2 to protein secretion and activity as well as to bacterial virulence. Domain swap experiments with the closely related <jats:italic>L. monocytogenes<\/jats:italic> PrsA1 protein combined with targeted mutagenesis indicate distinct functional roles for the PrsA2 peptidyl\u2010prolyl isomerase (PPIase) and the N\u2010 and C\u2010terminal domains in pathogenesis. In contrast to other PrsA\u2010like proteins described thus far in the literature, an absolute <jats:italic>in vivo<\/jats:italic> requirement for PrsA2 PPIase activity is evident in mouse infection models. This work illustrates the diversity of function associated with <jats:italic>L. monocytogenes<\/jats:italic> PrsA2 that serves to promote bacterial life within the infected host.<\/jats:p>","DOI":"10.1111\/j.1365-2958.2011.07665.x","type":"journal-article","created":{"date-parts":[[2011,5,5]],"date-time":"2011-05-05T04:42:21Z","timestamp":1304570541000},"page":"1530-1548","source":"Crossref","is-referenced-by-count":48,"title":["Functional analysis of the <i>Listeria monocytogenes<\/i> secretion chaperone PrsA2 and its multiple contributions to bacterial virulence"],"prefix":"10.1111","volume":"80","author":[{"given":"Francis","family":"Alonzo III","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bobbi","family":"Xayarath","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James 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