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Open AccessJournal ArticleDOI

Antigenic sites on the CVS rabies virus glycoprotein: analysis with monoclonal antibodies.

Monique Lafon, +2 more
- 01 Apr 1983 - 
- Vol. 64, Iss: 4, pp 843-851
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TLDR
Antigenic variation in the glycoprotein of rabies (CVS-11) virus was studied and competition radioimmunoassay suggested that one of these three antigenic sites was topologically distinct, with the other two in close proximity.
Abstract
Antigenic variation in the glycoprotein of rabies (CVS-11) virus was studied. Neutralization-resistant variant viruses were isolated in vitro at high frequency (10(-4) to 10(-5)) in the presence of anti-glycoprotein monoclonal antibody. Analysis of these variants identified at least three functionally independent antigenic sites, based on the grouping of variants that were no longer neutralized by one or more of a panel of 24 monoclonal antibodies. Competition radioimmunoassay suggested that one of these three antigenic sites was topologically distinct, with the other two in close proximity. In addition, it was shown that most (but not all) neutralization-resistant variants failed to bind the relevant monoclonal antibody. Viruses with altered antigenicity were shown to accumulate in virus stocks following several passages in vitro in the absence of antibody. In addition, variants were isolated in vivo following treatment of mice with monoclonal antibody.

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Citations
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Laboratory techniques in rabies

TL;DR: In this article, laboratory techniques in rabies were used to detect the presence of rabies in mice. But they did not identify the source of the virus, and the authors did not report any cases.
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A priori delineation of a peptide which mimics a discontinuous antigenic determinant

TL;DR: A technique was developed for identifying peptides with high affinity for a given antibody by testing a monoclonal antibody directed against a discontinuous antigenic determinant on foot-and-mouth disease virus, and peptides mimicking the determinant were identified even though the tertiary structure of the proteins comprising the virus capsid is unknown.
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Protection from rabies by a vaccinia virus recombinant containing the rabies virus glycoprotein gene

TL;DR: V-RGpro8 virus was highly effective in priming mice to generate a secondary rabies virus-specific cytotoxic T-lymphocyte response following culture of lymphocytes with either ERA or PM strains of rabiesirus.
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Rabies virulence: effect on pathogenicity and sequence characterization of rabies virus mutations affecting antigenic site III of the glycoprotein.

TL;DR: Although all substitutions affected neutralization and were located close to each other in the glycoprotein sequence, only substitutions at position 333 affected pathogenicity, and mutants from the other groups were pathogenic, causing paralysis and death as does CVS.
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Unexplained rabies in three immigrants in the United States. A virologic investigation.

TL;DR: Rabies infection in these three patients did not originate in the United States but resulted from exposures in Laos, the Philippines, and Mexico, suggesting that the onset of the clinical manifestations of rabies occurred after long incubation periods.
References
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Journal ArticleDOI

Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoluril.

TL;DR: The stability and sparing solubility of this chloroglycoluril in water can account for the minimal damage to proteins and living cells observed in these iodinations and allow for elimination of the reduction step employed at the close of iodinations with soluble chloroamides such as chloramine-T.
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Isolation of pure IgG1, IgG2a and IgG2b immunoglobulins from mouse serum using protein A-sepharose.

TL;DR: A simple and rapid method for isolating pure mouse IgG1, IgG 2a and IgG2b immunoglobulins in nearly 100% yield is described and all IgG was retained at pH 8.0 and this could not be eluted by washing.
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Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation

TL;DR: Four ‘antigenic sites’ on the three-dimensional structure of the influenza haemagglutinin are identified and at least one amino acid substitution in each site seems to be required for the production of new epidemic strains between 1968 and 1975.
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Antigenic structure of influenza virus haemagglutinin defined by hybridoma antibodies

TL;DR: Analysis of 34 mutant viruses selected has enabled us to define four antigenic sites on the haemagglutinin molecule that have undergone antigenic drift to a different extent in nature, which implies that the mechanisms responsible for antigenic Drift act selectively on distinct structures of the HA molecule.
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