Antigenic comparison of foot-and-mouth disease virus serotypes with monoclonal antibodies

Grubman, Marvin J.; Morgan, D. O.

doi:10.1016/0168-1702(86)90055-9

Cited by 24 publications

(8 citation statements)

References 29 publications

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“…Viral variants were selected by their ability to grow in the presence of nMAbs. Seven antibodies which have been previously characterized (9,25,47) were used to select the variants. Table 1 shows a brief characterization of the nMAbs.…”

Section: Resultsmentioning

confidence: 99%

“…Antibody 6HC4, however, reacts with the variant to the same extent as with wt. The significance of antibody reactivity with a viral variant which cannot be neutralized by that antibody is not clear but has been noted for FMDV type 01-resistant variants (62) and also for type A1, nMAbs which bind but do not neutralize other type A subtypes as well as other serotypes (25).…”

Section: Resultsmentioning

confidence: 99%

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Analysis of neutralizing antigenic sites on the surface of type A12 foot-and-mouth disease virus

Baxt

Vakharia

Moore

et al. 1989

J Virol

151

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A series of seven neutralizing monoclonal antibodies (nMAbs) directed against type A12 foot-and-mouth disease virus was used to generate neutralization-resistant variants. Both plaque reduction neutralization and microneutralization assays showed that the variants were no longer neutralized by. the nMAbs used to generate them, although some of the variants still reacted with the nMAbs at high antibody concentrations. Results of cross-neutralization studies by both plaque reduction neutralization and microneutralization assays suggested the presence of at least one immunodominant antigenic site on the surface of type A12 foot-and-mouth disease virus, along with evidence of a second antigenic site on the viral surface. Two of the variants had reduced virulence in tissue culture as evidenced by their inability to inhibit cellular protein synthesis and a marked reduction in virus-induced cellular morphological alterations. Nucleotide sequencing of the variant genomes placed three epitopes of the major antigenic site on VP1 and the fourth epitope on VP3 and VP1. The one epitope of the minor site appears to reside only on VP1.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Analysis of neutralizing antigenic sites on the surface of type A12 foot-and-mouth disease virus

Baxt

Vakharia

Moore

et al. 1989

J Virol

151

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“…Results of neutralization assays with these viruses and nMAbs paralleled the results of EITB, but not of EID assays. Absence of correlation between binding of some antibodies to virions and neutralization of infectivity has previously been observed for FMDV (Grubman & Morgan, 1986;Mateu et al, 1988;.…”

Section: Resultsmentioning

confidence: 99%

A single amino acid substitution affects multiple overlapping epitopes in the major antigenic site of foot-and-mouth disease virus of serotype C

Mateu

Martı́nez

Capucci

et al. 1990

Journal of General Virology

182

172

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Neutralizing monoclonal antibodies (nMAbs) elicited against foot-and-mouth disease virus (FMDV) of serotype C were assayed with field isolates and variant FMDVs using several immunoassays. Of a total of 36 nMAbs tested, 23 recognized capsid protein VP1 and distinguished at least 13 virion conformationindependent epitopes involved in neutralization of FMDV C. Eleven epitopes of FMDV C-S8cl have been located in segments 138-156 or 192-209 of VP1 by quantifying the reactivity of nMAbs with synthetic peptides and with nMAb-resistant mutants of FMDV C-S8cl carrying defined amino acid substitutions. The main antigenic site of FMDV C-S8cl (VP1 residues 138 to 150) consists of multiple (at least 10), distinguishable, overlapping epitopes. Some amino acid replacements abolished one of the epitopes, whereas other replacements affected several epitopes in this region. The conservative substitution His(146) --, Arg, found in many nMAb-resistant mutants analysed, abolished the reactivity of the virus with all nMAbs that recognized epitopes in the main antigenic site of FMDV C-S8cl. This indicates that a minimum genetic change can result in a highly amplified phenotypic effect, as regards the antigenicity of FMDV.

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“…A direct consequence of the genetic variability of FMDV is its remarkable antigenic diversity (1,2). Attempts to quantify such diversity and classify FMDV isolates have included the early serological subtyping (8) and the more recent analyses of reactivity with monoclonal antibodies (mAbs) (9)(10)(11). Knowledge of the types and frequency of occurrence of amino acid substitutions that lead to variations in viral epitopes is relevant to the design of new synthetic vaccines, whose efficacy may be hampered by the rapid antigenic variation of RNA viruses in nature (7,(10)(11)(12).…”

Section: Sd6mentioning

confidence: 99%

Implications of a quasispecies genome structure: effect of frequent, naturally occurring amino acid substitutions on the antigenicity of foot-and-mouth disease virus.

Mateu

Martı́nez

Rocha

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

109

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We provide evidence that the quasispecies nature (extreme genetic heterogeneity) of foot-and-mouth disease virus is relevant to the virus evading an immune response.A monoclonal antibody neutralizing the viral infectivity ( Foot-and-mouth disease virus (FMDV) is a picornavirus that causes the economically most important viral disease of cattle and other cloven-hooved animals (1, 2). As for most other RNA genomes, FMDV populations are genetically heterogeneous (3-5) and show the potential for very rapid evolution (6, 7). A direct consequence of the genetic variability of FMDV is its remarkable antigenic diversity (1, 2). Attempts to quantify such diversity and classify FMDV isolates have included the early serological subtyping (8) and the more recent analyses of reactivity with monoclonal antibodies (mAbs) (9)(10)(11). Knowledge of the types and frequency of occurrence of amino acid substitutions that lead to variations in viral epitopes is relevant to the design of new synthetic vaccines, whose efficacy may be hampered by the rapid antigenic variation of RNA viruses in nature (7,(10)(11)(12) In recent years, we have emphasized that FMDV shows a quasispecies structure (3-5), probably shared by most other RNA genetic elements (6, 7, 12, 24). This concept, which originated in theoretical work by Eigen and his colleagues (25)(26)(27), was first shown experimentally to adequately describe populations of phage QP3 (28) and later other RNA genomes as well (reviewed in refs. 6, 7, 12, and 24). According to the quasispecies structure, each FMDV genome population includes one or several "master" sequence(s)-which may nevertheless represent a small proportion of molecules (4, 24, 28)-and a "mutant spectrum" consisting of a distribution of single and multiple residue mutants (4,12,24,27,28). The proportion of each mutant depends on the frequency with which it arises by mutation and on its competitive growth with all other variants (present and arising) in the replicating population (26-28). Mutant viruses with chemically conservative amino acid substitutions, prone to behave in a quasineutral fashion, are more likely to be represented in a viral quasispecies than variants with mutations that adversely affect fitness even if viable, as documented with phage QB (28). In the present study we show that chemically conservative amino acid substitutions fixed at the main antigenic determinant of FMDV C during one epizootic-and that are also found frequently among other FMDV isolatesgreatly affected the interaction with one neutralizing mAb (n-mAb), SD6. This antibody recognizes an epitope surrounding a conserved amino acid sequence of VP1, proposed to be a receptor binding site (17, 18, 44). The effect of these naturally occurring amino acid changes has been mimicked with substituted synthetic peptides, which bind n-mAb SD6 to the same extent as complete variant viruses, thus providing an in vitro assay for epitopic variation of FMDV. MATERIALS AND METHODSViruses. The origin of the FMDV field isolates (C-S isolates) has b...

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Antigenic comparison of foot-and-mouth disease virus serotypes with monoclonal antibodies

Cited by 24 publications

References 29 publications

Analysis of neutralizing antigenic sites on the surface of type A12 foot-and-mouth disease virus

Analysis of neutralizing antigenic sites on the surface of type A12 foot-and-mouth disease virus

A single amino acid substitution affects multiple overlapping epitopes in the major antigenic site of foot-and-mouth disease virus of serotype C

Implications of a quasispecies genome structure: effect of frequent, naturally occurring amino acid substitutions on the antigenicity of foot-and-mouth disease virus.

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