title: Influenza viruses display high-affinity binding to human polyglycosylceramides represented on a solid-phase assay surface.
abstract: Polyglycosylceramides (PGCs), complex glycolipids containing up to 50 or more sugar residues, are recognized as the minor components of the cell-surface membranes, but a knowledge on their tissue distribution, structure, and function is limited. In this study, the binding of influenza viruses to preparations of PGCs was investigated using a TLC overlay assay and a microwell adsorption assay. The ability of PGCs to bind influenza virus was dependent on the source from which they were derived. Preparations of PGCs from human erythrocytes were found to support binding of A and B influenza virus strains at a much lower concentration than sialyl-6-paragloboside and to be somewhat better receptors for these viruses compared to the sialylglycoprotein fetuin. A high virus-binding activity of PGCs suggests that these species could potentially serve as biologically important cell-surface receptors for influenza viruses.
authors.affiliation: M.P. Chumakov Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow, Russia.
authors.forename: M
authors.initials: M
authors.lastname: Matrosovich
authors.forename: H
authors.initials: H
authors.lastname: Miller-Podraza
authors.forename: S
authors.initials: S
authors.lastname: Teneberg
authors.forename: J
authors.initials: J
authors.lastname: Robertson
authors.forename: K A
authors.initials: KA
authors.lastname: Karlsson
mesh_terms: D000327:Adsorption; D004912:Erythrocytes / Q000737:chemistry / Q000378:metabolism; D005915:Globosides / Q000378:metabolism; D006028:Glycosphingolipids / Q000378:metabolism* / Q000493:pharmacokinetics; D009980:Influenza A virus / Q000378:metabolism*; D009981:Influenza B virus / Q000378:metabolism*; D011485:Protein Binding; D000509:alpha-Fetoproteins / Q000378:metabolism
chemical_list: D005915:Globosides; D006028:Glycosphingolipids; D000509:alpha-Fetoproteins