Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1992-6-25
|
pubmed:abstractText |
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.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0022-1317
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
73 ( Pt 5)
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1167-76
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:1375279-Amino Acid Sequence,
pubmed-meshheading:1375279-Animals,
pubmed-meshheading:1375279-Antibodies, Monoclonal,
pubmed-meshheading:1375279-Cell Fusion,
pubmed-meshheading:1375279-Cells, Cultured,
pubmed-meshheading:1375279-Chick Embryo,
pubmed-meshheading:1375279-Epitopes,
pubmed-meshheading:1375279-Fibroblasts,
pubmed-meshheading:1375279-Glycosylation,
pubmed-meshheading:1375279-HN Protein,
pubmed-meshheading:1375279-Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase,
pubmed-meshheading:1375279-Molecular Sequence Data,
pubmed-meshheading:1375279-Mutation,
pubmed-meshheading:1375279-Newcastle disease virus,
pubmed-meshheading:1375279-Virion
|
pubmed:year |
1992
|
pubmed:articleTitle |
Inhibition of fusion by neutralizing monoclonal antibodies to the haemagglutinin-neuraminidase glycoprotein of Newcastle disease virus.
|
pubmed:affiliation |
Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester 01655.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|