Literature DB >> 6169797

Neutralization of foot-and-mouth disease virus. I. Sensitization of the 140S virion by antibody also reactive with the 12S protein subunit.

M M Hardy, D M Moore.   

Abstract

The in vitro interaction of foot-and-mouth disease virus (FMDV) with an immune serum resulted in a fraction of virus which failed to be neutralized. This inability of antibody to neutralize the entire population of a virus preparation was studied with emphasis on the antigenic specificity of the antibody-virus reaction. Antibody to FMDV recognized multiple antigenic determinants. Immunoabsorbent fractionation of the serum into 12S subunit cross-reactive and 140S virion-specific antibody revealed that these multiple antigenic determinants are factors in determining the neutralizing ability of the antibody. Antibody specific to the infective 140S virion neutralized virus effectively, whereas antibody reactive with both the 140S virion and 12S non-infective component did so ineffectively. Neutralization was independent of viral aggregation, strain, or type heterogeneity, dissociation of the immune complex, heterogeneity of antibody class, or incubation time. The non-neutralized fraction of virus was not due to insufficient antibody in the system, was demonstrated to be complexed with antibody ('sensitized') and could be neutralized with anti-globulin serum. The findings demonstrate the heterogeneity of antibody specificity of FMDV in serum preparations and relate the importance of antibody specificity to the neutralization of virus in vitro.

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Year:  1981        PMID: 6169797     DOI: 10.1099/0022-1317-55-2-415

Source DB:  PubMed          Journal:  J Gen Virol        ISSN: 0022-1317            Impact factor:   3.891


  6 in total

1.  Proteolytic processing of foot-and-mouth disease virus polyproteins expressed in a cell-free system from clone-derived transcripts.

Authors:  V N Vakharia; M A Devaney; D M Moore; J J Dunn; M J Grubman
Journal:  J Virol       Date:  1987-10       Impact factor: 5.103

2.  An enzyme-linked immunosorbent assay (ELISA) for the primary diagnosis of foot-and-mouth disease. Characterization and comparison with complement fixation.

Authors:  P Have; J C Lei; K Schjerning-Thiesen
Journal:  Acta Vet Scand       Date:  1984       Impact factor: 1.695

3.  Specificity of antibodies elicited by a synthetic peptide having a sequence in common with a fragment of a virus protein, the hepatitis B surface antigen.

Authors:  A R Neurath; S B Kent; N Strick
Journal:  Proc Natl Acad Sci U S A       Date:  1982-12       Impact factor: 11.205

4.  Biochemical map of polypeptides specified by foot-and-mouth disease virus.

Authors:  M J Grubman; B H Robertson; D O Morgan; D M Moore; D Dowbenko
Journal:  J Virol       Date:  1984-05       Impact factor: 5.103

5.  Monoclonal antibodies against foot-and-mouth disease virus 146S and 12S particles.

Authors:  K C McCullough; R Butcher
Journal:  Arch Virol       Date:  1982       Impact factor: 2.574

6.  Epitopes on foot-and-mouth disease virus outer capsid protein VP1 involved in neutralization and cell attachment.

Authors:  B Baxt; D O Morgan; B H Robertson; C A Timpone
Journal:  J Virol       Date:  1984-08       Impact factor: 5.103

  6 in total

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