Binding affinity of GM3 lactone for influenza virus.
We investigated the interaction of GM3 lactone with influenza virus. The specific bindings of influenza virus and its hemagglutinin to GM3 lactone-containing mixed monolayers were studied by using a quartz-crystal microbalance. It has been known that gangliosides as receptors for influenza virus are also substrates for virus neuraminidase. GM3 lactone, however, was found to bind to influenza virus hemagglutinin, but not to be substrate for virus neuraminidase.
Sato
T
T
Department of Biomolecular Engineering, Tokyo Institute of Technology, Yokohama, Japan. tsato@bio.titech.ac.jp
Ishii
M
M
Ohtake
F
F
Nagata
K
K
Terabayashi
T
T
Kawanishi
Y
Y
Okahata
Y
Y
D000818:Animals; D002240:Carbohydrate Sequence; D002642:Chick Embryo; D005679:G(M3) Ganglioside / Q000031:analogs & derivatives* / Q000378:metabolism; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000378:metabolism; D006868:Hydrolysis; D008565:Membrane Proteins / Q000378:metabolism; D008969:Molecular Sequence Data; D009439:Neuraminidase / Q000378:metabolism; D009975:Orthomyxoviridae / Q000378:metabolism*
D005679:G(M3) Ganglioside; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D008565:Membrane Proteins; C047143:ganglioside GM3 lactone; D009439:Neuraminidase