Title

Inhibition of fusion by neutralizing monoclonal antibodies to the haemagglutinin-neuraminidase glycoprotein of Newcastle disease virus

UMMS Affiliation

Department of Molecular Genetics and Microbiology

Publication Date

5-1-1992

Document Type

Article

Subjects

Amino Acid Sequence; Animals; 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

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

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.

Rights and Permissions

Citation: J Gen Virol. 1992 May;73 ( Pt 5):1167-76.

Related Resources

Link to Article in PubMed

Journal/Book/Conference Title

The Journal of general virology

PubMed ID

1375279