Differences in bovine parainfluenza 3 virus variants studied by sequencing of the genes of viral envelope proteins

Abstract

By determining gene nucleotide sequences we compared the primary structures of the membrane (M), fusion (F), and hemagglutinin-neuraminidase (HN) proteins of bovine parainfluenza 3 virus strains, M, SC, and MR which are substrains derived from a wild strain YN. The M and SC viruses are indistinguishable in having very weak hemagglutination (HA) and neuraminidase (NA) activities, but M virus' syncytium-inducing (Sl) activity is considerably higher than that of the SC virus. However, the results showed that the amino acid sequence of the F protein was identical in M and SC viruses, demonstrating that M virus' high Sl activity was not due to alteration of its F protein. Two differences in M and SC viruses' other proteins then seemed to be important, although their significance in the SI activity is not clear at present; the first being the 70th amino acid residue of the M protein, which was Asp in the M virus and Gly in the SC virus, and the other being the 539th residue of the HN protein, which was Tyr in the M virus and His in the SC virus. The nucleocapsid proteins of both M and SC viruses were identical. The MR virus, which is a variant derived from the M virus and has high HA and NA activities but very weak SI activity, was different from the M virus at only one site throughout the M, F, and HN proteins; the 193rd amino acid residue of the HN protein was Leu in the MR virus and Phe in the M virus. This result strongly suggested that the substitution of Leu with Phe at this particular site was closely linked to the drastic reduction in both HA and NA activities.