{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T06:02:07Z","timestamp":1791266527532,"version":"4.1.0"},"reference-count":83,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2009,7,1]],"date-time":"2009-07-01T00:00:00Z","timestamp":1246406400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2009,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p><jats:italic>Listeria monocytogenes<\/jats:italic>is an intracellular bacterial pathogen whose virulence depends on the regulated expression of numerous secreted bacterial factors. As for other gram-positive bacteria, many proteins secreted by<jats:italic>L. monocytogenes<\/jats:italic>are translocated across the bacterial membrane in an unfolded state to the compartment existing between the membrane and the cell wall. This compartment presents a challenging environment for protein folding due to its high density of negative charge, high concentrations of cations, and low pH. We recently identified PrsA2 as a gene product required for<jats:italic>L. monocytogenes<\/jats:italic>virulence. PrsA2 was identified based on its increased secretion by strains containing a mutationally activated form of<jats:italic>prfA<\/jats:italic>, the key regulator of<jats:italic>L. monocytogenes<\/jats:italic>virulence gene expression. The<jats:italic>prsA2<\/jats:italic>gene product is one of at least two predicted peptidyl-prolyl<jats:italic>cis<\/jats:italic>\/<jats:italic>trans<\/jats:italic>-isomerases encoded by<jats:italic>L. monocytogenes<\/jats:italic>; these proteins function as posttranslocation protein chaperones and\/or foldases. In this study, we demonstrate that PrsA2 plays a unique and important role in<jats:italic>L. monocytogenes<\/jats:italic>pathogenesis by promoting the activity and stability of at least two critical secreted virulence factors: listeriolysin O (LLO) and a broad-specificity phospholipase. Loss of PrsA2 activity severely attenuated virulence in mice and impaired bacterial cell-to-cell spread in host cells. In contrast, mutants lacking<jats:italic>prsA1<\/jats:italic>resembled wild-type bacteria with respect to intracellular growth and cell-to-cell spread as well as virulence in mice. PrsA2 is thus distinct from PrsA1 in its unique requirement for the stability and full activity of<jats:italic>L. monocytogenes<\/jats:italic>-secreted factors that contribute to host infection.<\/jats:p>","DOI":"10.1128\/iai.00280-09","type":"journal-article","created":{"date-parts":[[2009,5,19]],"date-time":"2009-05-19T01:09:49Z","timestamp":1242695389000},"page":"2612-2623","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":69,"title":["The Posttranslocation Chaperone PrsA2 Contributes to Multiple Facets of<i>Listeria monocytogenes<\/i>Pathogenesis"],"prefix":"10.1128","volume":"77","author":[{"suffix":"III","given":"Francis","family":"Alonzo","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, Illinois"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gary C.","family":"Port","sequence":"additional","affiliation":[{"name":"Seattle Biomedical Research Institute, Seattle, Washington"},{"name":"Molecular and Cellular Biology Program, University of Washington, Seattle, Washington"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Min","family":"Cao","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Clemson University, Clemson, South Carolina"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nancy E.","family":"Freitag","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, Illinois"},{"name":"Seattle Biomedical Research Institute, Seattle, Washington"},{"name":"Molecular and Cellular Biology Program, University of Washington, Seattle, Washington"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.00976-06"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"2005","DOI":"10.4049\/jimmunol.139.6.2005","volume":"139","year":"1987","unstructured":"Bishop, D. 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