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Reconstitution of surface lipoprotein translocation through the Slam translocon.

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cam.issuedOnline2022-04-27
dc.contributor.authorHuynh, Minh Sang
dc.contributor.authorHooda, Yogesh
dc.contributor.authorLi, Yuzi Raina
dc.contributor.authorJagielnicki, Maciej
dc.contributor.authorLai, Christine Chieh-Lin
dc.contributor.authorMoraes, Trevor F
dc.contributor.orcidHuynh, Minh Sang [0000-0002-9541-6441]
dc.contributor.orcidMoraes, Trevor F [0000-0001-9883-6145]
dc.date.accessioned2022-05-30T11:04:30Z
dc.date.available2022-05-30T11:04:30Z
dc.date.issued2022-04-27
dc.date.updated2022-05-30T11:04:30Z
dc.description.abstractSurface lipoproteins (SLPs) are peripherally attached to the outer leaflet of the outer membrane in many Gram-negative bacteria, playing significant roles in nutrient acquisition and immune evasion in the host. While the factors that are involved in the synthesis and delivery of SLPs in the inner membrane are well characterized, the molecular machinery required for the movement of SLPs to the surface are still not fully elucidated. In this study, we investigated the translocation of a SLP TbpB through a Slam1-dependent pathway. Using purified components, we developed an in vitro translocation assay where unfolded TbpB is transported through Slam1-containing proteoliposomes, confirming Slam1 as an outer membrane translocon. While looking to identify factors to increase translocation efficiency, we discovered the periplasmic chaperone Skp interacted with TbpB in the periplasm of Escherichia coli. The presence of Skp was found to increase the translocation efficiency of TbpB in the reconstituted translocation assays. A knockout of Skp in Neisseria meningitidis revealed that Skp is essential for functional translocation of TbpB to the bacterial surface. Taken together, we propose a pathway for surface destined lipoproteins, where Skp acts as a holdase for Slam-mediated TbpB translocation across the outer membrane.
dc.identifier.doi10.17863/CAM.85006
dc.identifier.eissn2050-084X
dc.identifier.issn2050-084X
dc.identifier.other35475756
dc.identifier.otherPMC9090332
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/337596
dc.languageeng
dc.language.isoeng
dc.publishereLife Sciences Publications, Ltd
dc.publisher.urlhttp://dx.doi.org/10.7554/elife.72822
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourcenlmid: 101579614
dc.sourceessn: 2050-084X
dc.subjectE. coli
dc.subjectGram negative
dc.subjectNeisseria
dc.subjectbacteria
dc.subjectinfectious disease
dc.subjectmembrane proteins
dc.subjectmicrobiology
dc.subjectprotein translocation
dc.subjectsurface lipoprotein
dc.subjectBacterial Outer Membrane Proteins
dc.subjectEscherichia coli
dc.subjectEscherichia coli Proteins
dc.subjectLipoproteins
dc.subjectPeriplasm
dc.titleReconstitution of surface lipoprotein translocation through the Slam translocon.
dc.typeArticle
dcterms.dateAccepted2022-04-26
prism.publicationNameElife
prism.volume11
pubs.funder-project-idCanadian Institutes of Health Research (PJT-148795)
pubs.funder-project-idCIHR (PJT-148795)
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0/
rioxxterms.versionVoR
rioxxterms.versionofrecord10.7554/eLife.72822

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