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Varying dependency of periplasmic peptidylprolyl cis-trans isomerases in promoting Yersinia pseudotuberculosis stress tolerance and pathogenicity
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet). Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR). (Matthew Francis)
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet). Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR). (Hans Wolf-Watz)
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet). Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR). (Matthew Francis)
2011 (engelsk)Inngår i: Biochemical Journal, ISSN 0264-6021, E-ISSN 1470-8728, Vol. 439, nr 2, s. 321-332Artikkel i tidsskrift (Fagfellevurdert) 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.

sted, utgiver, år, opplag, sider
United Kingdom: Portland Press Limited , 2011. Vol. 439, nr 2, s. 321-332
Emneord [en]
chaperone, immunosuppressant, infection, membrane biogenesis, periplasmic peptidylprolyl cis–trans isomerase, protein folding, survival
HSV kategori
Forskningsprogram
mikrobiologi; molekylärbiologi; biokemi
Identifikatorer
URN: urn:nbn:se:umu:diva-48067DOI: 10.1042/BJ20110767PubMedID: 21726196OAI: oai:DiVA.org:umu-48067DiVA, id: diva2:446406
Forskningsfinansiär
Swedish Research Council, 2006-3869Swedish Research Council, 2009-3660Tilgjengelig fra: 2011-10-10 Laget: 2011-10-07 Sist oppdatert: 2018-06-08bibliografisk kontrollert

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Varying dependency of periplasmic peptidylprolyl cis-trans isomerases in promoting Yersinia pseudotuberculosis stress tolerance and pathogenicity(2244 kB)534 nedlastinger
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