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Characterization of the molecular chaperone ClpB from the pathogenic spirochaete Leptospira interrogans

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cris.lastimport.scopus2024-02-12T20:50:52Z
dc.abstract.enLeptospira interrogans is a spirochaete responsible for leptospirosis in mammals. The molecular mechanisms of the Leptospira virulence remain mostly unknown. Recently, it has been demonstrated that an AAA+ chaperone ClpB (a member of the Hsp100 family) from L. interrogans (ClpBLi) is not only essential for survival of Leptospira under the thermal and oxidative stresses, but also during infection of a host. The aim of this study was to provide further insight into the role of ClpB in the pathogenic spirochaetes and explore its biochemical properties. We found that a non-hydrolysable ATP analogue, ATPγS, but not AMP-PNP induces the formation of ClpBLi hexamers and stabilizes the associated form of the chaperone. ADP also induces structural changes in ClpBLi and promotes its self-assembly, but does not produce full association into the hexamers. We also demonstrated that ClpBLi exhibits a weak ATPase activity that is stimulated by κ-casein and poly-lysine, and may mediate protein disaggregation independently from the DnaK chaperone system. Unexpectedly, the presence of E. coli DnaK/DnaJ/GrpE did not significantly affect the disaggregation activity of ClpBLi and ClpBLi did not substitute for the ClpBEc function in the clpB-null E. coli strain. This result underscores the species-specificity of the ClpB cooperation with the co-chaperones and is most likely due to a loss of interactions between the ClpBLi middle domain and the E. coli DnaK. We also found that ClpBLi interacts more efficiently with the aggregated G6PDH in the presence of ATPγS rather than ATP. Our results indicate that ClpB’s importance during infection might be due to its role as a molecular chaperone involved in reactivation of protein aggregates.
dc.affiliationUniwersytet Warszawski
dc.contributor.authorZolkiewski, Michał
dc.contributor.authorWięckowski, Daniel
dc.contributor.authorKrajewska, Joanna
dc.contributor.authorArent, Zbigniew
dc.contributor.authorKędzierska-Mieszkowska, Sabina
dc.contributor.authorModrak-Wójcik, Anna
dc.contributor.authorBzowska, Maria
dc.date.accessioned2024-01-24T19:07:42Z
dc.date.available2024-01-24T19:07:42Z
dc.date.issued2017
dc.date.openaccess0
dc.description.accesstimeAFTER_PUBLICATION
dc.description.financeNie dotyczy
dc.description.numbere0181118
dc.description.versionORIGINAL_AUTHOR
dc.description.volume12 (7)
dc.identifier.doi10.1371/JOURNAL.PONE.0181118
dc.identifier.issn1932-6203
dc.identifier.urihttps://repozytorium.uw.edu.pl//handle/item/102908
dc.identifier.weblinkhttps://repo.ur.krakow.pl/info/article/UR7ad5c9e8d7d141889e1664bdf8ece55b/
dc.languageeng
dc.pbn.affiliationphysical sciences
dc.relation.ispartofPLoS ONE
dc.relation.pages1-21
dc.rightsCC-BY
dc.sciencecloudnosend
dc.titleCharacterization of the molecular chaperone ClpB from the pathogenic spirochaete Leptospira interrogans
dc.typeJournalArticle
dspace.entity.typePublication