Abstract
The sequence of the hemagglutinin (HA) gene of the LA strain of rinderpest virus (RPV) has been determined by the direct sequencing method. The amino acid sequence of the protein which it encodes displays conservation of its structural determinants with the HA proteins of the other RPV strains. The LA-HA protein was shown to have three conserved potential N-linked glycosylation sites, compared with four such sites in the HA protein of L strain. The glycosylation site at position 200 on the L-HA molecule is absent from its LA-HA counterpart, due to a lysine for an asparagine substitution. The HA proteins of L and LA strains were the same molecular weight as judged by mobility on SDS-PAGE, suggesting that the site at position 200 is not used for glycosylation.
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