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dc.contributor.authorKu, S.en_US
dc.contributor.authorShulz, B.en_US
dc.contributor.authorPower, P.en_US
dc.contributor.authorJennings, M.en_US
dc.date.accessioned2017-04-24T13:16:03Z
dc.date.available2017-04-24T13:16:03Z
dc.date.issued2009en_US
dc.date.modified2010-10-04T06:54:05Z
dc.identifier.issn0006291Xen_US
dc.identifier.doi10.1016/j.bbrc.2008.11.025en_AU
dc.identifier.urihttp://hdl.handle.net/10072/34377
dc.description.abstractO-Glycosylation is emerging as a common posttranslational modification of surface exposed proteins in bacterial mucosal pathogens. In pathogenic Neisseria an O-glycosylation pathway modifies a single abundant protein, pilin, the subunit protein that forms pili. Here, we identify an additional outer membrane glycoprotein in pathogenic Neisseria, the nitrite reductase AniA, that is glycosylated in its C-terminal repeat region by the pilin glycosylation pathway. To our knowledge, this is the first report of a general O-glycosylation pathway in a prokaryote. We also show that AniA displays polymorphisms in residues that map to the surface of the protein. A frame-shift mutation abolishes AniA expression in 34% of Neisseria meningitidis strains surveyed, however, all Neisseria gonorrhoeae strains examined are predicted to express AniA, implying a crucial role for AniA in gonococcal biology.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherElsevieren_US
dc.publisher.placeUnited Statesen_US
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom84en_US
dc.relation.ispartofpageto89en_US
dc.relation.ispartofissue1en_US
dc.relation.ispartofjournalBiochemical and Biophysical Research Communicationsen_US
dc.relation.ispartofvolume378en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchInfectious Agentsen_US
dc.subject.fieldofresearchcode060502en_US
dc.titleThe pilin O-glycosylation pathway of pathogenic Neisseria is a general system that glycosylates AniA, an outer membrane nitrite reductaseen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2009
gro.hasfulltextNo Full Text


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