title: A general strategy for the chemoenzymatic synthesis of asymmetrically branched N-glycans.
abstract: A systematic, efficient means of producing diverse libraries of asymmetrically branched N-glycans is needed to investigate the specificities and biology of glycan-binding proteins. To that end, we describe a core pentasaccharide that at potential branching positions is modified by orthogonal protecting groups to allow selective attachment of specific saccharide moieties by chemical glycosylation. The appendages were selected so that the antenna of the resulting deprotected compounds could be selectively extended by glycosyltransferases to give libraries of asymmetrical multi-antennary glycans. The power of the methodology was demonstrated by the preparation of a series of complex oligosaccharides that were printed as microarrays and screened for binding to lectins and influenza-virus hemagglutinins, which showed that recognition is modulated by presentation of minimal epitopes in the context of complex N-glycans.
authors.affiliation: Complex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, GA 30602, USA.
authors.forename: Zhen
authors.initials: Z
authors.lastname: Wang
authors.forename: Zoeisha S
authors.initials: ZS
authors.lastname: Chinoy
authors.forename: Shailesh G
authors.initials: SG
authors.lastname: Ambre
authors.forename: Wenjie
authors.initials: W
authors.lastname: Peng
authors.forename: Ryan
authors.initials: R
authors.lastname: McBride
authors.forename: Robert P
authors.initials: RP
authors.lastname: de Vries
authors.forename: John
authors.initials: J
authors.lastname: Glushka
authors.forename: James C
authors.initials: JC
authors.lastname: Paulson
authors.forename: Geert-Jan
authors.initials: GJ
authors.lastname: Boons
mesh_terms: D001665:Binding Sites; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D000939:Epitopes; D006031:Glycosylation; D016695:Glycosyltransferases / Q000378:metabolism*; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry / Q000378:metabolism*; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D013058:Mass Spectrometry; D046228:Microarray Analysis; D019906:Nuclear Magnetic Resonance, Biomolecular; D009844:Oligosaccharides / Q000096:biosynthesis / Q000138:chemical synthesis* / Q000737:chemistry* / Q000378:metabolism; D037121:Plant Lectins / Q000737:chemistry / Q000378:metabolism; D054788:Ribosome Inactivating Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D000939:Epitopes; C543345:H1N1 virus hemagglutinin; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D037102:Lectins; D009844:Oligosaccharides; D037121:Plant Lectins; C050600:Sambucus nigra lectins; C045629:erythrina lectin; C109963:hemagglutinin, avian influenza A virus; C064549:lectin, Aleuria aurantia; D016695:Glycosyltransferases; D054788:Ribosome Inactivating Proteins