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Varying dependency of periplasmic peptidylprolyl cis-trans isomerases in promoting Yersinia pseudotuberculosis stress tolerance and pathogenicity
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology). Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR). (Matthew Francis)
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology). Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR). (Hans Wolf-Watz)
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology). Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR). (Matthew Francis)
2011 (English)In: Biochemical Journal, ISSN 0264-6021, E-ISSN 1470-8728, Vol. 439, no 2, 321-332 p.Article in journal (Refereed) Published
Abstract [en]

Periplasmic PPIases (peptidylprolyl cis-trans isomerases) catalyse the cis-trans isomerization of peptidyl-prolyl bonds, which is a rate-limiting step during protein folding. We demonstrate that the surA, ppiA, ppiD, fkpA and fklB alleles each encode a periplasmic PPIase in the bacterial pathogen Yersinia pseudotuberculosis. Of these, four were purified to homogeneity. Purified SurA, FkpA and FklB, but not PpiD, displayed detectable PPIase activity in vitro. Significantly, only Y. pseudotuberculosis lacking surA caused drastic alterations to the outer membrane protein profile and FA (fatty acid) composition. They also exhibited aberrant cellular morphology, leaking LPS (lipopolysaccharide) into the extracellular environment. The SurA PPIase is therefore most critical for maintaining Y. pseudotuberculosis envelope integrity during routine culturing. On the other hand, bacteria lacking either surA or all of the genes ppiA, ppiD, fkpA and fklB were sensitive to hydrogen peroxide and were attenuated in mice infections. Thus Y. pseudotuberculosis exhibits both SurA-dependent and -independent requirements for periplasmic PPIase activity to ensure in vivo survival and a full virulence effect in a mammalian host.

Place, publisher, year, edition, pages
United Kingdom: Portland Press Limited , 2011. Vol. 439, no 2, 321-332 p.
Keyword [en]
chaperone, immunosuppressant, infection, membrane biogenesis, periplasmic peptidylprolyl cis–trans isomerase, protein folding, survival
National Category
Microbiology
Research subject
Microbiology; Molecular Biology; Biochemistry
Identifiers
URN: urn:nbn:se:umu:diva-48067DOI: 10.1042/BJ20110767PubMedID: 21726196OAI: oai:DiVA.org:umu-48067DiVA: diva2:446406
Funder
Swedish Research Council, 2006-3869Swedish Research Council, 2009-3660
Available from: 2011-10-10 Created: 2011-10-07 Last updated: 2017-12-08Bibliographically approved

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Varying dependency of periplasmic peptidylprolyl cis-trans isomerases in promoting Yersinia pseudotuberculosis stress tolerance and pathogenicity(2244 kB)430 downloads
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Obi, IkennaNordfelth, RolandFrancis, Matthew
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