Binding of influenza A virus to monosialoganglioside (GM3) reconstituted in glucosylceramide and sphingomyelin membranes.
The binding of influenza A virus to GM3-containing monolayers at an air/water interface was quantitatively investigated by use of a quartz crystal microbalance (QCM). A QCM was horizontally attached to the monolayer from the air phase and the binding behavior of influenza virus was followed by the frequency changes of the QCM. GM3 was reconstituted in the momolayer of sphingomyelin (SM) or glucosylceramide (GlcCer). When the mole fraction of GM3 was below 30 mol%, the binding rate of the influenza A virus to the GM3/GlcCer membrane was significantly faster than that to GM3/SM membranes. When the mole fraction of GM3 in SM was below 20 mol%, specific binding of influenza virus was not observed at all. Binding of the virus to the GM3/GlcCer mixed membrane was inhibited by the addition of sialyllactose (Neu5Ac alpha 2-3Gal beta 1-4Glc). The virus binding was also visually observed by scanning electron microscopy. Viruses selectively bound to GM3/GlcCer (20:80, by mol%) membrane, but not to GM3/SM (20:80, by mol%) membrane. Furthermore, it was suggested that specific binding of influenza virus to the GM3/GlcCer membrane induced the changes in morphology of virus. It was clearly demonstrated that binding of influenza virus to GM3 was influenced by matrix lipids surrounding GM3.
Sato
T
T
Department of Biomolecular Engineering, Tokyo Institute of Technology, Yokohama, Japan.
Serizawa
T
T
Okahata
Y
Y
D002462:Cell Membrane / Q000737:chemistry; D005679:G(M3) Ganglioside / Q000737:chemistry*; D005963:Glucosylceramides / Q000737:chemistry; D009980:Influenza A virus / Q000737:chemistry*; D008567:Membranes, Artificial; D008855:Microscopy, Electron, Scanning; D011991:Receptors, Virus / Q000737:chemistry*; D013109:Sphingomyelins / Q000737:chemistry
D005679:G(M3) Ganglioside; D005963:Glucosylceramides; D008567:Membranes, Artificial; D011991:Receptors, Virus; D013109:Sphingomyelins