Detection by monoclonal antibodies of an antigenic determinant critical for poliovirus neutralization present on VP1 and on heat-inactivated virions

Blondel, B; O, Akacem; Crainic, R; Couillin, P.; Horodniceanu, F

doi:10.1016/s0042-6822(83)80027-0

Cited by 78 publications

(50 citation statements)

References 14 publications

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“…Although empty particles are not thought to be direct precursors of mature virions, they may function as reservoirs of capsid components (11)(12)(13). For poliovirus, empty particles are unstable, readily converting from D-type native antigenicity to a state with altered antigenic properties (C-type) (9,14,15). EV71 cultured for vaccine development produces both full virions and empty particles, and the content of empty particles is at least 2-fold more than the full virion in the final production yield (16).…”

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confidence: 99%

Crystal Structures of Enterovirus 71 (EV71) Recombinant Virus Particles Provide Insights into Vaccine Design

Lyu

Wang

et al. 2015

Journal of Biological Chemistry

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Background:No HFMD vaccine is available. Results: Structures of EV71 recombinant virus particles were determined showing that the inserted foreign peptide is exposed on the particle surface without capsid structural changes and that virus uncoating is not affected. Conclusion: VP1 BC loop is suitable for foreign peptide insertion for the generation of recombinant EV71 viruses. Significance: The results provide insights into vaccine development.

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confidence: 99%

Crystal Structures of Enterovirus 71 (EV71) Recombinant Virus Particles Provide Insights into Vaccine Design

Lyu

Wang

et al. 2015

Journal of Biological Chemistry

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“…However, Hinuma et al (1970) and Urasawa et al (1979) (1982) and Icenogle et al (1981) reported the presence of neutralization epitopes on naturally occurring 80S particles and on 14S precursor subunits, while Blondel et al (1983) a n d Thorpe et al (1982) isolated neutralizing monoclonal antibodies which react with H(heated) antigen, The three hybridomas isolated in this study also secreted monoclonal antibodies capable of binding to N and H antigenic particles. Thus, it became evident that the N and H…”

Section: Discussionmentioning

confidence: 64%

“…radiation, or high pH (Mayer et al, 1957;Roizman et al, 1959;Boey6 & Van Elsen, 1967, Katagiri et al, 1967, 1971Breindl, 1971). Monoclonal antibody preparations produced by hybridoma cells have proved useful for studying the antigenic structure of several antigenic components of poliovirus (Icenogle et al, 1981;Brioen et al, 1982;Emini et al, 1982;Thorpe et al, 1982;Blondel et al, 1983). Emini et al (1982) and Icenogle et al (1981) established hybridomas producing neutralizing monoclonal antibodies that react with N antigen (145S) and, to a lesser extent, with naturally occurring empty capsids (80S, H antigen) and 14S precursor subunits, but not with heat-treated virion [80S, H(heated) antigen].…”

Section: Discussionmentioning

confidence: 99%

“…Emini et al (1982) and Icenogle et al (1981) established hybridomas producing neutralizing monoclonal antibodies that react with N antigen (145S) and, to a lesser extent, with naturally occurring empty capsids (80S, H antigen) and 14S precursor subunits, but not with heat-treated virion [80S, H(heated) antigen]. In contrast, Blondel et al (1983) and Thorpe et al (1982) described neutralizing monoclonal antibodies reactive with both N and H(heated) antigens. In this study, we isolated three hybridomas secreting monoclonal antibodies (2A 12, 4C4 and 6H8) which react with N and H(heated) antigenic particles of poliovirus, and confirmed that one of the antibodies, 4C4, had neutralizing activity.…”

Section: Discussionmentioning

confidence: 99%

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Monoclonal Antibodies Reactive with Different Sites of N and H Antigenic Particles of Poliovirus

Taniguchi¹,

Urasawa²,

Urasawa³

1983

Journal of General Virology

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SUMMARYWe established three hybridomas (designated 2A12, 4C4 and 6H8) secreting monoclonal antibodies which react with N and H(heated) antigenic particles of poliovirus type 1 (Mahoney strain). One of these monoclonal antibodies, 4C4, had virus-neutralizing activity, while the other two were non-neutralizing. A solid-phase radioimmunoassay and a neutralization test indicated that the specificity of the neutralizing monoclonal antibody 4C4 was the same as that of the monospecific antibody HN31, previously prepared by us by absorbing poliovirus antiserum with an equine serum inhibitor-resistant mutant (M-HN31) of poliovirus. Furthermore, by means of immune electron microscopy, it was revealed that the combining site of the 4C4 neutralizing monoclonal antibody is on or around vertices of the N and H antigenic particles, while the other two monoclonal antibodies are directed to the entire surface of the antigens.Two antigens have been found in poliovirus: the N antigen associated with infectious complete particles and the H antigen, which includes naturally occurring empty capsids and 80S particles converted from N antigen by exposure to heat, u.v. radiation, or high pH (Mayer et al., 1957;Roizman et al., 1959; Boey6 & Van Elsen, 1967, Katagiri et al., 1967, 1971Breindl, 1971). Monoclonal antibody preparations produced by hybridoma cells have proved useful for studying the antigenic structure of several antigenic components of poliovirus (Icenogle et al., 1981;Brioen et al., 1982;Emini et al., 1982;Thorpe et al., 1982;Blondel et al., 1983). Emini et al. Icenogle et al. (1981) established hybridomas producing neutralizing monoclonal antibodies that react with N antigen (145S) and, to a lesser extent, with naturally occurring empty capsids (80S, H antigen) and 14S precursor subunits, but not with heat-treated virion [80S, H(heated) antigen]. In contrast, Blondel et al. (1983) and Thorpe et al. (1982) described neutralizing monoclonal antibodies reactive with both N and H(heated) antigens. In this study, we isolated three hybridomas secreting monoclonal antibodies (2A 12, 4C4 and 6H8) which react with N and H(heated) antigenic particles of poliovirus, and confirmed that one of the antibodies, 4C4, had neutralizing activity.In another approach to investigate the antigenic properties of poliovirus, Urasawa et al. (1974, 1976) employed three kinds of equine serum inhibitor-resistant mutants of poliovirus Mahoney strain (M-HN31, M-HN11 and M-H33) which were obtained by propagating the strain in the presence of equine inhibitory sera (HN31, HNll and H33 respectively) with different neutralization specificities. By absorbing anti-Mahoney serum with the three inhibitor-resistant mutants, three kinds of neutralizing antibodies (HN31, HNll and H33 antibodies) recognizing different antigenic determinants of poliovirus were prepared (Urasawa et at., t974, 1976). In neutralization tests (Urasawa et al., 1979) and electron microscopy using the monospecific antibodies thus obtained~ it was found that one antibody (HN31 antibody...

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“…The identification of the poliovirus capsid polypeptide recognized by neutralizing antibodies was also approached through chemical crosslinking of the antibodies to their virion binding sites. Two distinct neutralization epitopes were localized in this fashion to VP1 (10).Recently, we generated a hybridoma cell line producing neutralizing monoclonal antibodies from mice injected with heatinactivated virions (C particles) (14). In addition to binding to heat-denatured and to native virus, this antibody, C3, was found to selectively immunoprecipitate VP1.…”

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confidence: 99%

Localization of a poliovirus type 1 neutralization epitope in viral capsid polypeptide VP1.

Werf¹,

Wychowski²,

Bruneau³

et al. 1983

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

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Poliovirus type 1 cDNA sequences coding for viral capsid polypeptide VP1 were inserted into the fi-lactamase sequence of Escherichia coli plasmid pBR322. Resulting recombinant plasmid pSWll9 expressed in Escherichia coli a VPI-filactamase fusion protein that reacted with antibodies raised against poliovirus capsid polypeptide VP1 and with a monoclonal poliovirus type 1 neutralizing antibody, C3. Deletions of various lengths were generated within the VP1 sequence. The hybrid proteins expressed by the deleted plasmids did not react any more with C3 when the region of VP1 amino acids 95-110 (poliovirus nucleotides 2,754-2,806) was deleted. Therefore, the C3 epitope responsible for virus neutralization is most probably located in this region of the capsid polypeptide.Poliovirus, the causative agent of poliomyelitis, is a picornavirus. These are small viruses with a RNA genome of plus-strand polarity enclosed in a capsid composed of 60 copies each of four structural polypeptides, VP1, VP2, VP3, and VP4. Antibodies that neutralize virus infectivity are the major factor in protection against disease. The purified capsid polypeptides from several picornaviruses have been shown to induce a neutralizing antibody response in animals (1-4). In the case of foot-and-mouth disease virus (FMDV), for example, purified capsid polypeptide VP1 isolated from virions or prepared by DNA recombinant technology (1, 2, 5) was shown to protect susceptible animals against the disease. Moreover, synthetic peptides representing the sequence of the VP1 neutralization epitope have been used successfully as "subunit vaccine" (6, 7).In the case of poliovirus, however, the induction of neutralizing antibodies and the virus neutralization process are still poorly understood processes. Neutralizing sera raised against native poliovirions (D particles) and neutralizing monoclonal antibodies generated from mice immunized with native virions fail to react with the isolated viral capsid polypeptides (8)(9)(10). This suggests that the epitope(s) they recognize result, at least in part, from the three-dimensional arrangement of the proteins in the virion. Attempts have been made to raise neutralizing antisera by using single isolated capsid polypeptides, and a neutralizing antibody response was obtained by inoculating animals with purified VP1 but not with purified VP2 or VP3 (11,12). In a more recent study, however, another neutralization epitope was identified on VP3 or VP4 (13). The identification of the poliovirus capsid polypeptide recognized by neutralizing antibodies was also approached through chemical crosslinking of the antibodies to their virion binding sites. Two distinct neutralization epitopes were localized in this fashion to VP1 (10).Recently, we generated a hybridoma cell line producing neutralizing monoclonal antibodies from mice injected with heatinactivated virions (C particles) (14). In addition to binding to heat-denatured and to native virus, this antibody, C3, was found to selectively immunoprecipitate VP1. The fact that ...

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Detection by monoclonal antibodies of an antigenic determinant critical for poliovirus neutralization present on VP1 and on heat-inactivated virions

Cited by 78 publications

References 14 publications

Crystal Structures of Enterovirus 71 (EV71) Recombinant Virus Particles Provide Insights into Vaccine Design

Crystal Structures of Enterovirus 71 (EV71) Recombinant Virus Particles Provide Insights into Vaccine Design

Monoclonal Antibodies Reactive with Different Sites of N and H Antigenic Particles of Poliovirus

Localization of a poliovirus type 1 neutralization epitope in viral capsid polypeptide VP1.

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