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The hemagglutinating properties of influenza virus envelope protein, prepared by reassociation of polypeptide subunits, have been defined and compared with those of virus and ether-split hemagglutinin. In general, the characteristics of the intact and ether-split virus were found to be similar, whereas those of the envelope protein were distinctly different. The use of chicken, pigeon, and guinea pig erythrocytes both at 23 and 4 C disclosed that the hemagglutinating titers of envelope protein preparations were particularly dependent on the system employed. Under optimal conditions, with guinea pig cells at 4 C, the titers of envelope protein preparations were equivalent to those of the original virus concentrates. The hemagglutinating activity of envelope protein was particularly sensitive to elevated temperature, concentrated urea, sulfhydryl-reducing reagents, and tryptic digestion at high salt concentrations. In all these respects, the intact virus was more resistant than the envelope protein. Interpretation of the data indicates that the hemagglutinin is stabilized when associated with the lipid micelle at the surface of the virus.

Envelope Protein of Influenza Virus I. Hemagglutinating Activity of Reassociated Subunits