[The concept of transmembrane asymmetry of lateral domains in biomemranes and influenza virus envelope fine structure].

The molecular architectures of enveloped viruses are one demonstrative example of perfectly arranged macromolecular complex that is achieved through the structural specificity of virus assembly. Virus morphogenesis is a multi-step process that depends on the concerted actions of many viral and cellular components as well as fitted organization of main viral constituents. Viral envelope was shown to be composed of the mixture of lipid raft and non-raft domains. The domains are recruited from the host-cell membrane as discrete well-ordered lipid-protein units in the process of virus assembly. Raft-like nature of influenza virus A envelope was visualized using a novel approach of cold solubilization of the detergent-resistant membranes from intact influenza virus A virions with the mixture of two non-ionic detergents drastically differing in their raft-solubilizing activities, NP40 and octyl-glucopyranoside. In the view of this methodological approach, the virus envelope is apparently an ensemble of platforms which are flexibly joint in the viral envelope, and composed of surface glycoproteins (hemagglutinin and neuraminidase), matrix M1 protein and lipids. The modern concept of transmembrane asymmetry of lateral domains in biological membranes was involved to explain the solubilization mechanism revealed. Using principles of this concept we suggest matrix M1 protein shell as a structure-forming base to support asymmetrical rafts in the virus envelope.