Nature of the Sendai virus receptor: glycoprotein versus ganglioside

Abstract

Gangliosides were compared with glycoproteins as potential receptors for Sendai virus by incorporating measured amounts of the glycoconjugates into lecithin-cholesterol liposomes and measuring binding by a hemagglutination assay with sheep erythrocytes. HeLa cell gangliosides showed no binding activity toward the virus up to 15 jig of sialic acid per 5 ,umol of lecithin-cholesterol, whereas HeLa cell glycoproteins incorporated into similar liposomes caused avid virus binding below 1 ,ug of sialic acid. These sialoglycoproteins could be separated from the bulk of cell proteins by multiple chloroform-methanol extractions. Purified rat brain gangliosides at a level of 120 ,ug of sialic acid in liposomes did not bind virus, whereas chloroform-methanol-extracted rat brain proteins caused only marginal binding. Bovine brain gangliosides differed slightly from the rat brain mixture in showing weak binding properties. Our results thus indicate that glycoproteins, rather than gangliosides, are the natural receptors for Sendai virus and that tissues differ as to the quantity of such protein receptors.

Ganglioside‐Induced Neuritogenesis: Verification That Gangliosides Are the Active Agents, and Comparison of Molecular Species

“…These findings have been difficult to interpret because most ganglioside preparations contain at least residual, and often considerable, amounts of lipophilic peptides that solubilize in chloroform-methanol (C-M) and copurify with the gangliosides (Brunngraber et al, 1976;Wu et al, 1980;Ledeen et al, 1983). Therefore it is possible that the reported effects may have resulted from such contaminants, a prospect lent some credence by the fact that the neurotropic agents characterized to date have for the most part been peptides Adler, 1980, 1981;Harper and Thoenen, 1980).…”

Sendai virus-erythrocyte membrane interaction: quantitative and kinetic analysis of viral binding, dissociation, and fusion

“…The fusion process is a two-step reaction, involving a binding step and the actual fusion event, and is mediated by the viral spike glycoproteins HN and F (4). Cell attachment is accomplished by an interaction between HN and sialic acid-containing glycoproteins (32,39) or glycolipids (14,34), and the F protein, which consists of two disulfide-bonded polypeptides, F1 and F2 (4), has been identified as the fusion factor. It has been proposed that a hydrophobic segment contained in the F1 polypeptide of this protein (7,15) interacts directly with the target membrane (15,30,36), causing a (local) perturbation of the bilayer structure which subsequently leads to bilayer merging.…”

Treatment of human peripheral blood leukocytes with proteases does not affect Sendai virus-induced interferon production

“…A certain specific terminal sequence of polysaccharide has recently been reported to be an effective viral receptor (8,9,11) and is present in such subtypes of gangliosides as GTia, Gqlb, and Gplc (5,9). However, glycoproteins possessing the same terminal polysaccharide sequence, e.g., glycophorin, were also reported to act as the virus receptor (10,12). Sendai virus is widely used as a potent inducer of interferon (IFN) in leukocytes and other cells, but little is known about the detailed mechanisms of IFN induction.…”