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dc.contributor.authorChristensen, S
dc.contributor.authorHalili, MA
dc.contributor.authorStrange, N
dc.contributor.authorPetit, GA
dc.contributor.authorHuston, WM
dc.contributor.authorMartin, JL
dc.contributor.authorMcMahon, RM
dc.date.accessioned2020-01-15T22:57:47Z
dc.date.available2020-01-15T22:57:47Z
dc.date.issued2019
dc.identifier.issn1932-6203en_US
dc.identifier.doi10.1371/journal.pone.0222595en_US
dc.identifier.urihttp://hdl.handle.net/10072/390295
dc.description.abstractChlamydia trachomatis is an obligate intracellular bacterium with a distinctive biphasic developmental cycle that alternates between two distinct cell types; the extracellular infectious elementary body (EB) and the intracellular replicating reticulate body (RB). Members of the genus Chlamydia are dependent on the formation and degradation of protein disulfide bonds. Moreover, disulfide cross-linking of EB envelope proteins is critical for the infection phase of the developmental cycle. We have identified in C. trachomatis a homologue of the Disulfide Bond forming membrane protein Escherichia coli (E. coli) DsbB (hereafter named CtDsbB) and—using recombinant purified proteins—demonstrated that it is the redox partner of the previously characterised periplasmic oxidase C. trachomatis Disulfide Bond protein A (CtDsbA). CtDsbA protein was detected in C. trachomatis inclusion vacuoles at 20 h post infection, with more detected at 32 and similar levels at 44 h post infection as the developmental cycle proceeds. As a redox pair, CtDsbA and CtDsbB largely resemble their homologous counterparts in E. coli; CtDsbA is directly oxidised by CtDsbB, in a reaction in which both periplasmic cysteine pairs of CtDsbB are required for complete activity. In our hands, this reaction is slow relative to that observed for E. coli equivalents, although this may reflect a non-native expression system and use of a surrogate quinone cofactor. CtDsbA has a second non-catalytic disulfide bond, which has a small stabilising effect on the protein’s thermal stability, but which does not appear to influence the interaction of CtDsbA with its partner protein CtDsbB. Expression of CtDsbA during the RB replicative phase and during RB to EB differentiation coincided with the oxidation of the chlamydial outer membrane complex (COMC). Together with our demonstration of an active redox pairing, our findings suggest a potential role for CtDsbA and CtDsbB in the critical disulfide bond formation step in the highly regulated development cycle.en_US
dc.description.peerreviewedYesen_US
dc.languageengen_US
dc.publisherPublic Library of Science (PLoS)en_US
dc.relation.ispartofissue9en_US
dc.relation.ispartofjournalPLoS Oneen_US
dc.relation.ispartofvolume14en_US
dc.subject.fieldofresearchBiological Sciencesen_US
dc.subject.fieldofresearchcode06en_US
dc.titleOxidoreductase disulfide bond proteins DsbA and DsbB form an active redox pair in Chlamydia trachomatis, a bacterium with disulfide dependent infection and developmenten_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Articlesen_US
dcterms.bibliographicCitationChristensen, S; Halili, MA; Strange, N; Petit, GA; Huston, WM; Martin, JL; McMahon, RM, Oxidoreductase disulfide bond proteins DsbA and DsbB form an active redox pair in Chlamydia trachomatis, a bacterium with disulfide dependent infection and development, PLoS One, 2019, 14 (9)en_US
dcterms.dateAccepted2019-09-02
dcterms.licensehttp://creativecommons.org/licenses/by/4.0/en_US
dc.date.updated2020-01-15T22:54:35Z
dc.description.versionPublisheden_US
gro.rights.copyright© 2019 Christensen et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en_US
gro.hasfulltextFull Text
gro.griffith.authorMcMahon, Roisin
gro.griffith.authorPetit, Guillaume
gro.griffith.authorMartin, Jennifer
gro.griffith.authorGreenup, Maria A.


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