title: Glycosylation and oligomerization of the spike protein of Marburg virus.
abstract: The oligosaccharide side chains of the glycoprotein of Marburg virus (MW 170,000) have been analyzed by determining their sensitivity to enzymatic degradation and their reactivity with lectins. It was found that they consist of N- and O-glycans. Studies employing chemical cross-linking showed that the glycoprotein is present as a homotrimer in the viral envelope.
authors.affiliation: Institut für Virologie, Philipps-Universität, Germany.
authors.forename: H
authors.initials: H
authors.lastname: Feldmann
authors.forename: C
authors.initials: C
authors.lastname: Will
authors.forename: M
authors.initials: M
authors.lastname: Schikore
authors.forename: W
authors.initials: W
authors.lastname: Slenczka
authors.forename: H D
authors.initials: HD
authors.lastname: Klenk
mesh_terms: D003432:Cross-Linking Reagents; D006031:Glycosylation; D046911:Macromolecular Substances; D029024:Marburgvirus / Q000378:metabolism* / Q000648:ultrastructure; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000378:metabolism; D008970:Molecular Weight; D011485:Protein Binding; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D003432:Cross-Linking Reagents; D046911:Macromolecular Substances; D008562:Membrane Glycoproteins; D014759:Viral Envelope Proteins