Inhibition of fusion by neutralizing monoclonal antibodies to the haemagglutinin-neuraminidase glycoprotein of Newcastle disease virus
UMass Chan Affiliations
Department of Molecular Genetics and MicrobiologyDocument Type
Journal ArticlePublication Date
1992-05-01Keywords
Amino Acid SequenceAnimals
Antibodies, Monoclonal
Cell Fusion
Cells, Cultured
Chick Embryo
Epitopes
Fibroblasts
Glycosylation
HN Protein
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
Molecular Sequence Data
Mutation
Newcastle disease virus
Virion
Life Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
The majority of neutralizing monoclonal antibodies (MAbs) to the haemagglutinin-neuraminidase (HN) glycoprotein of Newcastle disease virus prevent attachment of the virus to cellular receptors and inhibits virion-induced fusion from without (FFWO) and fusion from within (FFWI) mediated by the virus glycoprotein-laden infected cell surface. For these antibodies, the inhibition of fusion is presumed to be the result of the prevention of HN-mediated bridging of potential fusion partners. MAbs against antigenic sites 3 and 4 neutralize virus infectivity, but by a mechanism other than the prevention of attachment, the exact nature of which remains to be established. Antibodies to both of these sites effectively inhibit virion-induced FFWO, even when the inducing virus is not infectious. This is consistent with the mechanism of neutralization of these MAbs involving the inhibition of an early, post-attachment step in infection. MAbs to site 3 also inhibit FFWI, but those to site 4 do not, even when added at high concentrations. This suggests that the requirement for HN may be different in the two modes of fusion. The epitopes recognized by MAbs to sites 3 and 4 have been delineated by the identification of individual nucleotide substitutions in the HN genes of neutralization escape variants. Some of the deduced amino acid substitutions result in additional N-linked glycosylation sites in HN, which are utilized and presumably account for the escape from neutralization.Source
J Gen Virol. 1992 May;73 ( Pt 5):1167-76.
DOI
10.1099/0022-1317-73-5-1167Permanent Link to this Item
http://hdl.handle.net/20.500.14038/38197PubMed ID
1375279Related Resources
ae974a485f413a2113503eed53cd6c53
10.1099/0022-1317-73-5-1167