The molecular organization of the influenza virus surface. Studies using photoreactive and fluorescent labeled phospholipid probes.
The membrane structures of remantadin-sensitive and remantadin-resistant influenza virus strains were studied using a photoreactive fatty acid as well as analogues of phosphatidylcholine, phosphatidylethanolamine and sphingomyelin, carrying a fluorescent or photoreactive reporter group at the end of one of the aliphatic chains. The results obtained demonstrated for the first time that the phospholipids of the viral membrane form lateral domains differing by the fluidity of their hydrocarbon chains and, probably, by the head-group composition of the lipids. The hemagglutinin small subunit (HA2) was shown to protrude into the apolar region of the phospholipid bilayer, whereas the M1 protein makes contact only with the inner surface. In the remantadin-sensitive virions the heavy hemagglutinin chain (HA1) appears not to be in contact with the lipid bilayer, whereas in the remantadin-resistant strain HA1 has a hydrophobic segment that proved to be inserted into the bilayer.
D000818:Animals; D002645:Chickens; D004352:Drug Resistance, Microbial; D005456:Fluorescent Dyes; D009980:Influenza A virus / Q000648:ultrastructure*; D008563:Membrane Lipids / Q000032:analysis; D008566:Membranes / Q000648:ultrastructure; D010743:Phospholipids; D010777:Photochemistry; D012299:Rimantadine / Q000494:pharmacology; D014763:Viral Matrix Proteins; D014764:Viral Proteins / Q000032:analysis
D005456:Fluorescent Dyes; D008563:Membrane Lipids; D010743:Phospholipids; D014763:Viral Matrix Proteins; D014764:Viral Proteins; D012299:Rimantadine