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dc.contributor.authorBushell, Simon
dc.contributor.authorMainprize, Iain L.
dc.contributor.authorWear, Martin A.
dc.contributor.authorLou, Hubing
dc.contributor.authorWhitfield, Chris
dc.contributor.authorNaismith, Jim
dc.identifier.citationBushell , S , Mainprize , I L , Wear , M A , Lou , H , Whitfield , C & Naismith , J 2013 , ' Wzi Is an Outer Membrane Lectin that Underpins Group 1 Capsule Assembly in Escherichia coli ' , Structure , vol. 21 , no. 5 , pp. 844-853 .
dc.identifier.otherPURE: 62947753
dc.identifier.otherPURE UUID: 9e4a2421-c849-4e2d-adc0-438585d96f90
dc.identifier.otherWOS: 000318829400017
dc.identifier.otherScopus: 84877251817
dc.description.abstractMany pathogenic bacteria encase themselves in a polysaccharide capsule that provides a barrier to the physical and immunological challenges of the host. The mechanism by which the capsule assembles around the bacterial cell is unknown. Wzi, an integral outer-membrane protein from Escherichia coli, has been implicated in the formation of group 1 capsules. The 2.6 angstrom resolution structure of Wzi reveals an 18-stranded beta-barrel fold with a novel arrangement of long extracellular loops that blocks the extracellular entrance and a helical bundle that plugs the periplasmic end. Mutagenesis shows that specific extracellular loops are required for in vivo capsule assembly. The data show that Wzi binds the K30 carbohydrate polymer and, crucially, that mutants functionally deficient in vivo show no binding to K30 polymer in vitro. We conclude that Wzi is a novel outer-membrane lectin that assists in the formation of the bacterial capsule via direct interaction with capsular polysaccharides.
dc.rights© The Authors. This is an open access article, available from http://www.sciencedirect.comen
dc.subjectSurface-plasmon resonanceen
dc.subjectColanic acid biosynthesisen
dc.subjectGram-negative bacteriaen
dc.subjectK antigensen
dc.subjectStructural basisen
dc.subjectQH301 Biologyen
dc.titleWzi Is an Outer Membrane Lectin that Underpins Group 1 Capsule Assembly in Escherichia colien
dc.typeJournal articleen
dc.contributor.sponsorThe Wellcome Trusten
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.description.statusPeer revieweden

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