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dc.contributor.authorPower, Peter M
dc.contributor.authorSeib, Kate L
dc.contributor.authorJennings, Michael P
dc.date.accessioned2012-11-02
dc.date.accessioned2014-08-15T01:50:52Z
dc.date.accessioned2017-03-02T00:24:30Z
dc.date.available2017-03-02T00:24:30Z
dc.date.issued2006
dc.date.modified2014-08-15T01:50:52Z
dc.identifier.issn0006-291X
dc.identifier.doi10.1016/j.bbrc.2006.06.182
dc.identifier.urihttp://hdl.handle.net/10072/62261
dc.description.abstractPili (type IV fimbriae) of Neisseria meningitidis are glycosylated by the addition of O-linked sugars. Recent work has shown that PglF, a protein with homology to O-antigen 'flippases', is required for the biosynthesis of the pilin-linked glycan and suggests pilin glycosylation occurs in a manner analogous to the wzy-dependent addition of O-antigen to the core-LPS. O-Antigen ligases are crucial in this pathway for the transfer of undecraprenol-linked sugars to the LPS-core in Gram-negative bacteria. An O-antigen ligase homologue, pglL, was identified in N. meningitidis. PglL mutants showed no change in LPS phenotypes but did show loss of pilin glycosylation, confirming PglL is essential for pilin O-linked glycosylation in N. meningitidis.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherElsevier
dc.publisher.placeUnited Kingdom
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom904
dc.relation.ispartofpageto908
dc.relation.ispartofissue4
dc.relation.ispartofjournalBiochemical and Biophysical Research Communications
dc.relation.ispartofvolume347
dc.rights.retentionY
dc.subject.fieldofresearchMedicinal and biomolecular chemistry
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchBacteriology
dc.subject.fieldofresearchMedical biochemistry and metabolomics
dc.subject.fieldofresearchcode3404
dc.subject.fieldofresearchcode3101
dc.subject.fieldofresearchcode310701
dc.subject.fieldofresearchcode3205
dc.titlePilin glycosylation in Neisseria meningitidis occurs by a similar pathway to wzy-dependent O-antigen biosynthesis in Escherichia coli.
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codec1x
gro.facultyFaculty of Science, Environment, Engineering and Technology
gro.hasfulltextNo Full Text
gro.griffith.authorSeib, Kate
gro.griffith.authorJennings, Michael P.


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