Membrane particles possessing receptor activity for influenza virions have been reconstituted following solubihzation of human erythrocyte membranes with octyl glucoside (OG) and fractionation on a DEAE-cellulose column. Fractions that eluted with 1.5 MNaCl yielded, after removal of OG, reconstituted membrane particles (RMP) which could bind virus and inhibit hemagglutination. RMP contained essentially two membrane proteins (glycophorin and a nonglycosylated protein of molecular weight 29,000), two phospholipids (sphingomyelin and phosphatidylcholine), cholesterol, and gangliosides. Incubation of influenza virus with RMP at 4° resulted in the formation of a virus-RMP complex (liposomes). The specificity of the receptor was demonstrated by inhibition of viral attachment when RMP were treated with neuraminidase or preincubated with rabbit anti-M or anti-N antiserum, suggesting that both the carbohydrates and peptide moiety may play a role in attachment. Calculations suggest that there are 6 × 103 JV-acetyl neuraminic acid residues per attached virion. This system provides a simple and gentle means of reconstituting membrane components to study receptor activity.

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