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dc.contributor.authorJanesch, Bettina
dc.contributor.authorSchirmeister, Falko
dc.contributor.authorMaresch, Daniel
dc.contributor.authorAltmann, Friedrich
dc.contributor.authorMessner, Paul
dc.contributor.authorKolarich, Daniel
dc.contributor.authorSchaeffer, Christina
dc.date.accessioned2017-05-29T12:34:59Z
dc.date.available2017-05-29T12:34:59Z
dc.date.issued2016
dc.identifier.issn0959-6658
dc.identifier.doi10.1093/glycob/cwv087
dc.identifier.urihttp://hdl.handle.net/10072/337595
dc.description.abstractFlagellin glycosylation impacts, in several documented cases, the functionality of bacterial flagella. The basis of flagellin glycosylation has been studied for various Gram-negative bacteria, but less is known about flagellin glycans of Gram-positive bacteria including Paenibacillus alvei, a secondary invader of honeybee colonies diseased with European foulbrood. Paenibacillus alvei CCM 2051T swarms vigorously on solidified culture medium, with swarming relying on functional flagella as evidenced by abolished biofilm formation of a non-motile P. alvei mutant defective in the flagellin protein Hag. Here, the glycobiology of the polar P. alvei flagella was investigated. Analysis on purified flagellin demonstrated that the 30-kDa Hag protein (PAV_2c01710) is modified with an O-linked trisaccharide comprised of one hexose and two N-acetyl-hexosamine residues, at three sites of glycosylation. Downstream of the hag gene on the bacterial chromosome, two open reading frames (PAV_2c01630, PAV_2c01640) encoding putative glycosyltransferases were shown to constitute a flagellin glycosylation island. Mutants defective in these genes exhibited altered migration in sodium dodecyl sulfate polyacrylamide gel electrophoresis as well as loss of extracellular flagella production and bacterial motility. This study reveals that flagellin glycosylation in P. alvei is pivotal to flagella formation and bacterial motility in vivo, and simultaneously identifies flagella glycosylation as a second protein O-glycosylation system in this bacterium, in addition to the well-investigated S-layer tyrosine O-glycosylation pathway.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherOxford University Press
dc.relation.ispartofpagefrom74
dc.relation.ispartofpageto87
dc.relation.ispartofissue1
dc.relation.ispartofjournalGlycobiology
dc.relation.ispartofvolume26
dc.subject.fieldofresearchBiological sciences
dc.subject.fieldofresearchBiochemistry and cell biology not elsewhere classified
dc.subject.fieldofresearchBiomedical and clinical sciences
dc.subject.fieldofresearchcode31
dc.subject.fieldofresearchcode310199
dc.subject.fieldofresearchcode32
dc.titleFlagellin glycosylation in Paenibacillus alvei CCM 2051T
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorKolarich, Daniel


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