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J Gen Virol 70 (1989), 1549-1552; DOI 10.1099/0022-1317-70-6-1549
© 1989 Society for General Microbiology
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Effect of Amino Acid Substitutions on Glycosylation of the Haemagglutinin-Neuraminidase Glycoprotein of Newcastle Disease Virus Strain Beaudette C

Khatijah Yusoff, Mark Nesbit, Anthony C. R. Samson and Peter T. Emmerson

Department of Biochemistry and Genetics, Medical School, University of Newcastle upon Tyne, Newcastle upon Tyne NE2 4HH, U.K.

The nucleotide sequences of two monoclonal antibody-resistant mutant viruses predict changes from the wild-type in the number of potential glycosylation sites (Asn-X-Thr/Ser) in the mutant haemagglutinin-neuraminidase (HN) glycoproteins of the Beaudette C strain of Newcastle disease virus. The HN glycoproteins of these mutants, F5 and Z18, migrate either slower (F5) or faster (Z18) than that of the wild-type in SDS-PAGE. HN proteins synthesized in chick embryo fibroblasts following infection by either mutant or wild-type virus in the presence of tunicamycin (an inhibitor of glycosylation), comigrate on SDS-PAGE. These results confirm that the HN protein of the mutant virus, F5, has gained a glycosylation site at Asn(323)-Ser-Ser and that the conserved potential glycosylation site at Asn(481)-His-Thr is indeed glycosylated in the HN protein of the wild-type Beaudette C strain of Newcastle disease virus but is lost in that of the mutant virus, Z18.

Keywords: NDV mutants, HN glycoprotein, amino acid substitution

Received 8 December 1988; accepted 1 February 1989.




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