The glycosylation sites on the haemagglutinin-neuraminidase glycoprotein of Newcastle disease virus


Citation

Khatijah Yusoff, . (1990) The glycosylation sites on the haemagglutinin-neuraminidase glycoprotein of Newcastle disease virus. [Proceedings Paper]

Abstract

Several Newcastle disease virus strain Beaudette C mutants which are resistant to monoclonal antibodies MAbs directed against the haemagglutinin-neuraminidase HN glycoproteins have been analysed. The nucleotide sequences of two of these mutants predict changes from the wild type in the number of potential glycosylation sites Asn-X-Thr/Ser in the mutant HN glycoproteins. 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 synthesised in chick embryo fibroblasts following infection by either mutant or wild type virus in the presence of tunicamycin an inhibitor of glycosylation co-migrate on SDS-PAGE. These results confirm that the HN protein of F5 has gained a glycosylation site at Asn 323-Ser-Ser and that a glycosylation site at Asn 481-His-Thr is indeed glycosylated in the wild type HN protein but is lost in that of Z18.


Download File

Full text available from:

Abstract

Several Newcastle disease virus strain Beaudette C mutants which are resistant to monoclonal antibodies MAbs directed against the haemagglutinin-neuraminidase HN glycoproteins have been analysed. The nucleotide sequences of two of these mutants predict changes from the wild type in the number of potential glycosylation sites Asn-X-Thr/Ser in the mutant HN glycoproteins. 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 synthesised in chick embryo fibroblasts following infection by either mutant or wild type virus in the presence of tunicamycin an inhibitor of glycosylation co-migrate on SDS-PAGE. These results confirm that the HN protein of F5 has gained a glycosylation site at Asn 323-Ser-Ser and that a glycosylation site at Asn 481-His-Thr is indeed glycosylated in the wild type HN protein but is lost in that of Z18.

Additional Metadata

[error in script]
Item Type: Proceedings Paper
Additional Information: 6 ref. Summary En
AGROVOC Term: VIRUS DE LA ENFERMEDAD DE NEWCASTLE
AGROVOC Term: MUTANTES
AGROVOC Term: GLICOPROTEINAS/ MUTACION
Geographical Term: MALAYSIA
Depositing User: Ms. Norfaezah Khomsan
Last Modified: 24 Apr 2025 05:26
URI: http://webagris.upm.edu.my/id/eprint/14697

Actions (login required)

View Item View Item