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dc.contributor.authorSchulz, Benjamin L
dc.contributor.authorJen, Freda EC
dc.contributor.authorPower, Peter M
dc.contributor.authorJones, Christopher E
dc.contributor.authorFox, Kate L
dc.contributor.authorKu, Shan C
dc.contributor.authorBlanchfield, Joanne T
dc.contributor.authorJennings, Michael P
dc.date.accessioned2018-01-12T01:12:52Z
dc.date.available2018-01-12T01:12:52Z
dc.date.issued2013
dc.date.modified2014-01-13T00:45:44Z
dc.identifier.issn1932-6203
dc.identifier.doi10.1371/journal.pone.0062768
dc.identifier.urihttp://hdl.handle.net/10072/55578
dc.description.abstractO-glycosylation of proteins in Neisseria meningitidis is catalyzed by PglL, which belongs to a protein family including WaaL O-antigen ligases. We developed two hidden Markov models that identify 31 novel candidate PglL homologs in diverse bacterial species, and describe several conserved sequence and structural features. Most of these genes are adjacent to possible novel target proteins for glycosylation. We show that in the general glycosylation system of N. meningitidis, efficient glycosylation of additional protein substrates requires local structural similarity to the pilin acceptor site. For some Neisserial PglL substrates identified by sensitive analytical approaches, only a small fraction of the total protein pool is modified in the native organism, whereas others are completely glycosylated. Our results show that bacterial protein O-glycosylation is common, and that substrate selection in the general Neisserial system is dominated by recognition of structural homology.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherPublic Library of Science
dc.publisher.placeUnited States
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrome62768-1
dc.relation.ispartofpagetoe62768-11
dc.relation.ispartofissue5
dc.relation.ispartofjournalPloS One
dc.relation.ispartofvolume8
dc.rights.retentionY
dc.subject.fieldofresearchHistory, heritage and archaeology
dc.subject.fieldofresearchcode43
dc.titleIdentification of Bacterial Protein O-Oligosaccharyltransferases and Their Glycoprotein Substrates
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dcterms.licensehttps://creativecommons.org/licenses/by/4.0/
dc.description.versionVersion of Record (VoR)
gro.rights.copyright© 2013 Schulz 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.
gro.date.issued2013
gro.hasfulltextFull Text
gro.griffith.authorJennings, Michael P.
gro.griffith.authorJen, Freda E.


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