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Monoclonal antibodies specific for the influenza virus A/PR/8/34 hemagglutinin (HA) were used to examine the structure of the HA glycoprotein by immunofluorescence techniques during infection of MDCK cells. One antibody (Y8-10C2), shown previously to detect conformational alterations in the HA coinciding with the acid induction of viral fusion activity, bound to internalized virus but not to virus adsorbed to the cell surface. The binding of Y8-10C2 was completely inhibited by ammonium chloride treatment of the cells. These findings are consistent with the idea that Y8-10C2 detects conformational changes in the HA which accompany the acid-induced fusion of viral and endosomal membranes. The same antibody also bound to newly synthesized HA but not to later forms of cytoplasmic HA or to HA incorporated into the cell membrane during virus maturation. A possible common denominator of the antigenic changes detected by antibody Y8-10C2 during virus entry and replication may be alterations in the structural relationship among the three HA monomers which form the mature HA molecule.

Monoclonal antibodies detect different forms of influenza virus hemagglutinin during viral penetration and biosynthesis