Effect of amino acid substitutions on glycosylation of the haemagglutinin-neuraminidase glycoprotein of Newcastle disease virus strain Beaudette C.
The nucleotide sequences of two monoclonal antibody-resistant mutant viruses predict changes from the wild-type in the number of potential glycosylation (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.
Yusoff
K
K
Department of Biochemistry and Genetics, Medical School, University of Newcastle upon Tyne, U.K.
Nesbit
M
M
Samson
A C
AC
Emmerson
P T
PT
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000378:metabolism*; D000818:Animals; D002642:Chick Embryo; D000939:Epitopes / Q000032:analysis / Q000235:genetics / Q000276:immunology; D006031:Glycosylation; D015707:HN Protein; D006389:Hemagglutinins, Viral / Q000235:genetics* / Q000276:immunology; D009154:Mutation; D009522:Newcastle disease virus / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D014415:Tunicamycin / Q000494:pharmacology; D014759:Viral Envelope Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism*
D000596:Amino Acids; D000939:Epitopes; D015707:HN Protein; D006389:Hemagglutinins, Viral; D014759:Viral Envelope Proteins; D014415:Tunicamycin