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• W1910764452 startingPage "1530" @default.
• W1910764452 abstract "As an organism that has evolved to live in environments ranging from soil to the cytosol of mammalian cells, Listeria monocytogenes must regulate the secretion and activity of protein products that promote survival within these habitats. The post-translocation chaperone PrsA2 has been adapted to assist in the folding and activity of L. monocytogenes 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 L. monocytogenes PrsA1 protein combined with targeted mutagenesis indicate distinct functional roles for the PrsA2 peptidyl-prolyl isomerase (PPIase) and the N- and C-terminal domains in pathogenesis. In contrast to other PrsA-like proteins described thus far in the literature, an absolute in vivo requirement for PrsA2 PPIase activity is evident in mouse infection models. This work illustrates the diversity of function associated with L. monocytogenes PrsA2 that serves to promote bacterial life within the infected host." @default.
• W1910764452 created "2016-06-24" @default.
• W1910764452 creator A5019729277 @default.
• W1910764452 creator A5050620343 @default.
• W1910764452 creator A5058791363 @default.
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• W1910764452 date "2011-05-05" @default.
• W1910764452 modified "2023-10-15" @default.
• W1910764452 title "Functional analysis of the Listeria monocytogenes secretion chaperone PrsA2 and its multiple contributions to bacterial virulence" @default.
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• W1910764452 doi "https://doi.org/10.1111/j.1365-2958.2011.07665.x" @default.
• W1910764452 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3115453" @default.
• W1910764452 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21545417" @default.
• W1910764452 hasPublicationYear "2011" @default.
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