title: Glycoproteomics: a powerful tool for characterizing the diverse glycoforms of bacterial pilins and flagellins.
abstract: With glycosylation now firmly established across both Archaeal and bacterial proteins, a wide array of glycan diversity has become evident from structural analysis and genomic data. These discoveries have been built in part on the development and application of mass spectrometric technologies to the bacterial glycoproteome. This review highlights recent findings using high sensitivity MS of the large variation of glycans that have been reported on flagellin and pilin proteins of bacteria, using both 'top down' and 'bottom up' approaches to the characterization of these glycoproteins. We summarize current knowledge of the sugar modifications that have been observed on flagellins and pilins, in terms of both the diverse repertoire of monosaccharides observed, and the assemblage of moieties that decorate many of these sugars.
authors.affiliation: Division of Molecular Biosciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK.
authors.forename: Paul G
authors.initials: PG
authors.lastname: Hitchen
authors.forename: Katie
authors.initials: K
authors.lastname: Twigger
authors.forename: Esmeralda
authors.initials: E
authors.lastname: Valiente
authors.forename: Rebecca H
authors.initials: RH
authors.lastname: Langdon
authors.forename: Brendan W
authors.initials: BW
authors.lastname: Wren
authors.forename: Anne
authors.initials: A
authors.lastname: Dell
mesh_terms: D036781:Fimbriae Proteins / Q000378:metabolism; D005408:Flagellin / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism*; D006031:Glycosylation; D013058:Mass Spectrometry; D040901:Proteomics
chemical_list: D006023:Glycoproteins; D005408:Flagellin; D036781:Fimbriae Proteins