The Type B Flagellin of Hypervirulent Clostridium difficile Is Modified with Novel Sulfonated Peptidylamido-glycans

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dc.contributor.authorBouche, Laura
dc.contributor.authorPanico, Maria
dc.contributor.authorHitchen, Paul
dc.contributor.authorBinet, Daniel
dc.contributor.authorSastre, Federico
dc.contributor.authorFaulds Pain, Alexandra
dc.contributor.authorValiente, Esmeralda
dc.contributor.authorVinogradov, Evgeny
dc.contributor.authorAubry, Annie
dc.contributor.authorFulton, Kelly
dc.contributor.authorTwine, Susan
dc.contributor.authorLogan, Susan M.
dc.contributor.authorWren, Brendan W.
dc.contributor.authorDell, Anne
dc.contributor.authorMorris, Howard R.
dc.date.accessioned2024-01-10T12:44:19Z
dc.date.available2024-01-10T12:44:19Z
dc.date.issued2016
dc.description.abstractGlycosylation of flagellins is a well recognized property of many bacterial species. In this study, we describe the structural characterization of novel flagellar glycans from a number of hypervirulent strains of C. difficile. We used mass spectrometry (nano-LC-MS and MS/MS analysis) to identify a number of putative glycopeptides that carried a variety of glycoform substitutions, each of which was linked through an initial N-acetylhexosamine residue to Ser or Thr. Detailed analysis of a LLDGSSTEIR glycopeptide released by tryptic digestion, which carried two variant structures, revealed that the glycopeptide contained, in addition to carbohydrate moieties, a novel structural entity. A variety of electrospray-MS strategies using Q-TOF technology were used to define this entity, including positive and negative ion collisionally activated decomposition MS/MS, which produced unique fragmentation patterns, and high resolution accurate mass measurement to allow derivation of atomic compositions, leading to the suggestion of a taurine-containing peptidylamido-glycan structure. Finally, NMR analysis of flagellin glycopeptides provided complementary information. The glycan portion of the modification was assigned as -Fuc3N-(13)--Rha-(12)--Rha3OMe-(13)--GlcNAc-(1)Ser, and the novel capping moiety was shown to be comprised of taurine, alanine, and glycine. This is the first report of a novel O-linked sulfonated peptidylamido-glycan moiety decorating a flagellin protein.
dc.description.funderWellcome Trust
dc.description.funderMedical Research Council
dc.description.funderBiotechnology and Biological Sciences Research Council
dc.description.funderMarie Curie Intra-European Fellowship
dc.description.funderBiotechnology and Biological Sciences Research Council
dc.description.funderMedical Research Council
dc.fechaingreso.objetodigital2024-04-25
dc.format.extent11 páginas
dc.fuente.origenWOS
dc.identifier.doi10.1074/jbc.M116.749481
dc.identifier.eissn1083-351X
dc.identifier.pubmedidMEDLINE:27758867
dc.identifier.urihttps://doi.org/10.1074/jbc.M116.749481
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/77664
dc.identifier.wosidWOS:000390095300014
dc.information.autorucIngeniería;Sastre F;S/I;219374
dc.issue.numero49
dc.language.isoen
dc.nota.accesocontenido completo
dc.pagina.final25449
dc.pagina.inicio25439
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
dc.revistaJOURNAL OF BIOLOGICAL CHEMISTRY
dc.rightsacceso abierto
dc.subjectbacteria
dc.subjectglycosylation
dc.subjectGram-positive bacteria
dc.subjectmass spectrometry (MS)
dc.subjectnuclear magnetic resonance (NMR)
dc.subjectClostridium difficile
dc.subjectflagellin
dc.subjectmodification
dc.subjectsulfonated
dc.subjectTANDEM MASS-SPECTROMETRY
dc.subjectTYROBUTYRICUM ATCC 25755
dc.subjectPROTEIN GLYCOSYLATION
dc.subjectPOSTTRANSLATIONAL MODIFICATION
dc.subjectIDENTIFICATION
dc.subjectMOTILITY
dc.subjectVIRULENCE
dc.subjectGENOME
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleThe Type B Flagellin of Hypervirulent Clostridium difficile Is Modified with Novel Sulfonated Peptidylamido-glycans
dc.typeartículo
dc.volumen291
sipa.codpersvinculados219374
sipa.indexWOS
sipa.indexScopus
sipa.trazabilidadCarga SIPA;09-01-2024
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