Characterization of Newcastle disease virus envelope glycoproteins expressed in insect cells.

Recombinant baculoviruses carrying cDNAs of hemagglutinin-neuraminidase (HN) and fusion (F) glycoprotein genes of virulent and avirulent strains of Newcastle disease virus (NDV) were constructed to examine the contribution of the individual proteins in cell fusion. F proteins of both virulent and avirulent strains expressed by the recombinant viruses were glycosylated and translocated onto the cell surfaces and only the F protein of the virulent origin was proteolytically cleaved into F1 and F2 subunits and bound intermolecularly by disulfide bonds. HN proteins of virulent and avirulent strains expressed by the recombinant viruses showed both hemadsorption and neuraminidase activities. Single infection of the recombinant baculoviruses could not induce cell fusion; however, co-infection with the recombinant viruses of the F protein of virulent strain and HN protein of both strains gave clear syncytia in insect cells. The syncytium formation was much clearer in the cells co-infected with the recombinants of F protein of virulent strain and the HN protein of avirulent strain in comparison with those co-infected with F and HN recombinant viruses of virulent origin. The cell fusion was completely blocked by monoclonal antibodies against the F protein but not by those to the HN protein.