Biochemical characterization of a glycoprotein required for rhinovirus attachment.

摘要: Human rhinoviruses attach to specific receptors located on the surfaces of host cells as a first step in viral infection. A 90-kDa cell surface protein was previously shown be involved attachment human susceptible (Tomassini, J. E., and Colonno, R.J. (1986) Virol. 58, 290-295). Digestion purified receptor with various glycosidases revealed that 30% its molecular mass comprised complex-type oligosaccharides, one-third being contributed by sialic acid. The presence acid confirmed demonstrating wheat germ lectin can inhibit membranes, while lectins other sugar specificities had no effect. oligosaccharides were N-linked tunicamycin treatment N-glycanase digestion. Seven glycosylation sites detected partial digestion N-glycanase. Native an isoelectric focusing point 4.2, compared 5.3 for deglycosylated protein. Studies virus antibody binding neuraminidase-treated membranes suggested although carbohydrates may host-virus interaction, carbohydrate is not predominant component cellular site.