title: Structural determination of gangliosides that bind to influenza A, B, and C viruses by an improved binding assay: strain-specific receptor epitopes in sialo-sugar chains.
abstract: An improved binding assay for detection of ganglioside receptors for influenza A, B, and C viruses was developed. In this system, the virions bound to gangliosides that were developed on a silica gel thin-layer plate were detected by mouse monoclonal antibody against viral hemagglutinin and peroxidase-conjugated anti-mouse immunoglobin. No hydrolysis of the gangliosides by viral receptor-destroying enzyme was detected in the present condition. The reactivity of the viruses to gangliosides depended on the amount of developed gangliosides (10 pmols-10 nmols), the molecular species of sialic acid, and their sugar sequences. Human influenza A (PR/8/34), B (Lee/40), and C (Ann Arbor/1/50) viruses bound different receptor epitopes of sialo-sugar chains of gangliosides. The A/PR/8 virus bound most effectively to Neu5Ac-containing lacto-series gangliosides carrying type I and type II sugar chains, followed by ganglio-series and hematoside-series gangliosides. The A/PR/8 virus weakly bound to Neu5Ac alpha 2,6lactotetraosylceramide [IV6(Neu5Ac)Lc4Cer] and Neu5Ac alpha 2,6paragloboside [IV6(Neu5Ac)nLc4Cer] carrying Neu5Ac alpha 2,6Gal sequence, although their Neu5Ac alpha 2,3Gal derivatives were the most potent gangliosides tested. B/Lee/40 bound restrictively to IV6(Neu5Ac)Lc4Cer and IV6(Neu5Ac)nLc4Cer, which carry Neu5Ac alpha 2,6Gal sequence, and type I and type II lacto-series sugar chain, respectively. C/Ann Arbor/1/50 reacted only with 9-O-Ac-Neu5Ac-carrying sugar chains in all the gangliosides tested. This method also allowed the microanalysis of receptor gangliosides of unknown samples. ESK cells, sensitive to the influenza A viruses infection, expressed several kinds of receptor active gangliosides, while those from ESK-R cells, resistant to the virus infection, were undetectable.
authors.affiliation: Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Science, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Suzuki
authors.forename: T
authors.initials: T
authors.lastname: Nakao
authors.forename: T
authors.initials: T
authors.lastname: Ito
authors.forename: N
authors.initials: N
authors.lastname: Watanabe
authors.forename: Y
authors.initials: Y
authors.lastname: Toda
authors.forename: G
authors.initials: G
authors.lastname: Xu
authors.forename: T
authors.initials: T
authors.lastname: Suzuki
authors.forename: T
authors.initials: T
authors.lastname: Kobayashi
authors.forename: Y
authors.initials: Y
authors.lastname: Kimura
authors.forename: A
authors.initials: A
authors.lastname: Yamada
mesh_terms: D001665:Binding Sites; D002240:Carbohydrate Sequence; D000939:Epitopes / Q000276:immunology / Q000378:metabolism*; D005732:Gangliosides / Q000737:chemistry* / Q000378:metabolism; D005915:Globosides / Q000378:metabolism; D007158:Immunologic Techniques; D009980:Influenza A virus / Q000276:immunology / Q000378:metabolism; D009981:Influenza B virus / Q000276:immunology / Q000378:metabolism; D009982:Gammainfluenzavirus / Q000276:immunology / Q000378:metabolism; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000378:metabolism; D009975:Orthomyxoviridae / Q000276:immunology / Q000378:metabolism*; D011991:Receptors, Virus / Q000737:chemistry* / Q000378:metabolism; D012680:Sensitivity and Specificity; D014773:Virology / Q000379:methods
chemical_list: D000939:Epitopes; D005732:Gangliosides; D005915:Globosides; D009844:Oligosaccharides; D011991:Receptors, Virus; C016735:sialooligosaccharides; C014812:sialosylparagloboside