Evidence for common, intertypic antigenic determinants on poliovirus capsid polypeptides

Blondel, B; Crainic, R; O, Akacem; Bruneau, P.; Girard, Marc; Horodniceanu, F

doi:10.1016/0042-6822(82)90280-x

Cited by 24 publications

(14 citation statements)

References 6 publications

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“…The emulsions were made by mixing equal volumes of the protein sample and complete Freund's adjuvant. After 3 wk, the initial injection was followed by three or four booster injections 2 …”

Section: Methodsmentioning

confidence: 99%

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Synthetic peptides from four separate regions of the poliovirus type 1 capsid protein VP1 induce neutralizing antibodies.

Chow¹,

Yabrov²,

Bittle³

et al. 1985

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

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Peptides from different regions of the poliovirus type 1 capsid protein VP1 were synthesized. Antibodies raised against these peptides in rabbits and rats recognized the cognate peptides and denatured VP1. Peptides from four regions of VP1 generated antisera with neutralizing titers specifically against poliovirus type 1. Antisera against all other regions of VP1 failed to neutralize virus infectivity, although some of the antisera clearly bound to native virions. Thus, the neutralizing determinants on VP1 reside in specific noncontiguous regions of the protein and can be defined by specific peptides from these regions. An animal's immunologic response against a viral antigen is a composite of many antibodies, of which those that neutralize infectivity comprise a specific subset. Because the neutralizing response plays a major protective role, the characterization of the antibodies, their specificities, and their functional role in the neutralization process is crucial to an understanding of the pathobiology of a virus. In addition, the definition of neutralizing epitopes should help in the understanding of initial virus-cell interactions.It previously has been shown that major neutralizing determinants are found on the poliovirus type 1 capsid protein designated VP1. The isolated, denatured VP1 is capable of inducing virion-neutralizing antibodies in rats (1) and rabbits (2). VP1 is immunoprecipitated by a neutralizing anti-virion monoclonal antibody, C-3 (3). In addition, using this monoclonal antibody, Wychowski et al. (4) have shown that a neutralization epitope was located within the region of amino acid residues 90-104 of VP1. Analysis of virion mutants that are resistant to neutralizing anti-virion monoclonal antibodies showed that a major neutralizing determinant for poliovirus type 3 was localized within VP1 in the region of amino acid residues 96-106 (5, 6). Characterization of a large set of neutralizing anti-virion monoclonal antibodies against poliovirus type 1 also indicated that the amino acid region 94-104 of VP1 contained a neutralizing determinant (7). In addition, an additional amino acid region (residues 70-80) was recognized by some monoclonal antibodies (7). Thus, it appears that VP1 potentially possesses several neutralizing determinants.To further characterize the neutralization response against VP1 and to structurally characterize the neutralization epitopes, we derived a partial antigenic map of VP1, using antisera made against synthetic peptides from different regions throughout the VP1 protein. We report here that synthetic peptides spanning four separate regions of the VP1 sequence will induce neutralizing antibodies. These serotype-specific antibodies recognize VP1 and the intact mature poliovirus virion. The ability of these four regions to generate neutralizing antibodies is independent of the choice of immunizing host. METHODSSynthesis and Coupling of Peptides. The peptides were synthesized by R. Houghten, with solid-phase methods using a Beckman model 990B peptide synthe...

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“…The emulsions were made by mixing equal volumes of the protein sample and complete Freund's adjuvant. After 3 wk, the initial injection was followed by three or four booster injections 2 …”

Section: Methodsmentioning

confidence: 99%

“…The isolated, denatured VP1 is capable of inducing virion-neutralizing antibodies in rats (1) and rabbits (2). VP1 is immunoprecipitated by a neutralizing anti-virion monoclonal antibody, C-3 (3).…”

mentioning

confidence: 99%

Synthetic peptides from four separate regions of the poliovirus type 1 capsid protein VP1 induce neutralizing antibodies.

Chow¹,

Yabrov²,

Bittle³

et al. 1985

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

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“…In one study, none of the antisera raised against VP1, VP2, VP3, or VP4 were neutralizing (13). In a more recent study, the antiserum from only one out of two rabbits injected with VP1 showed any neutralizing activity (14). The antigenic specificity of the antiserum was not characterized further.…”

mentioning

confidence: 99%

Isolated poliovirus capsid protein VP1 induces a neutralizing response in rats.

Chow¹,

Baltimore²

1982

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

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Antibodies were raised in rats against the poliovirus type 1 capsid proteins, VP1, VP2, and VP3. Antibodies directed against VP1 from type 1 poliovirus (Mahoney) neutralized type 1 but not type 2 poliovirus. Antibodies raised against VP2 and VP3 failed to neutralize type 1 virus. Thus, VP1 appears to be a neutralizing antigen for poliovirus and in its denatured form presents to the immune system its neutralizing determinants.The poliovirion has been shown to exist in two basic antigenic forms, N (or D) and C (or H), that are not crossreactive. The N antigenic form is associated with mature infectious virus (1). C antigenicity is observed in empty capsids isolated from infected cells, in mature virions that have been heated, modified, or degraded, and in virions that were bound to and eluted from membranes of suspectible cells (2-6). By using nonsusceptible animals for immunization, neutralizing sera have been found to recognize the N antigenic state and have been obtained only when native virions are injected. These neutralizing sera bind to native virions but do not recognize C antigenic structures. Similarly, C-antigen-specific antibodies recognize heated or disrupted virions and procapsid structures but do not bind to native virions (7)(8). Recently, a hybridoma cell line producing neutralizing monoclonal antibodies has been generated from mice that were injected with native virions (9). In addition to binding to native virions, this antibody recognizes the 70S procapsid and the 14S assembly subunit, indicating that subunits of the virion previously thought to lack N antigenic sites do exhibit a neutralizing determinant. This raises the possibility that neutralizing antibodies could be induced by subunits of the virions and not only by the intact mature virion.The determination of which of the poliovirus proteins can elicit a neutralizing response has proven elusive. The poliovirion contains four capsid proteins: VP1, VP2, VP3, and VP4. Neutralizing sera raised against mature virus and the monoclonal antibody do not recognize any of the capsid proteins selectively (9). The conversion of N-reactive virions to C-reactive particles is typically accompanied with the loss of VP4, suggesting initially that VP4 might be the neutralizing determinant (10,11). Topological studies, however, indicate that VP4 is not located at the capsid surface (12). Several attempts to raise a neutralizing antiserum by using single isolated capsid proteins have yielded equivocal results. In one study, none of the antisera raised against VP1, VP2, VP3, or VP4 were neutralizing (13). In a more recent study, the antiserum from only one out of two rabbits injected with VP1 showed any neutralizing activity (14). The antigenic specificity of the antiserum was not characterized further.We present here data showing that all rats injected with isolated VP1 develop neutralizing antibodies to poliovirus. Rats injected with VP2 or VP3 generate antibodies that precipitate the cognate proteins and bind to virions but have no neutralizing ab...

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“…Furthermore, they seem to be strong immunogens because they are also found with other antisera raised against individual polypeptides isolated and purified by different methods (Romanova et al, 1981;Blondel et al, 1982).…”

Section: Discussionmentioning

confidence: 99%

“…Recently, it was shown that an intertypic cross-reaction was found not only on non-structural but also on structural polypeptides (Romanova et al, 1981). Blondel et al (1982), who prepared antisera against isolated polypeptides of poliovirus, type 1, strain Mahoney, found an intertypic crossreaction on completely denatured homologous polypeptides of all three serotypes. They also t Formerly known as Drzeniek.…”

Section: Introductionmentioning

confidence: 99%

Evidence for Conformational Changes of Poliovirus Precursor Particles during Virus Morphogenesis

Wiegers

Dernick²

1985

Journal of General Virology

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SUMMARYAntisera raised against isolated structural polypeptides VP1, VP2 and VP3 of poliovirus type 1, strain Mahoney, reveal a differential reaction against mature virus and its precursor particles. During virus morphogenesis antigenic sites recognized by VPI and VP2 antisera are lost stepwise from the surface of precursor particles. These sites are cross-reacting between serotypes and are also lost from precursor particles of type 2 (MEF-1) and type 3 (Saukett). They are absent on the surface of mature virus of all three serotypes. In contrast, the VP3 antiserum recognizes sites expressed maximally on the surface of infectious virus of type 1 (Mahoney). This antiserum did not show significant intertypic cross-reactions with virus particles, empty capsids or 14S particles of poliovirus types 2 and 3. However, it does recognize intertypic crossreacting sites, like the VPI and VP2 antisera, on denatured polypeptides and 5S particles of each serotype.

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Evidence for common, intertypic antigenic determinants on poliovirus capsid polypeptides

Cited by 24 publications

References 6 publications

Synthetic peptides from four separate regions of the poliovirus type 1 capsid protein VP1 induce neutralizing antibodies.

Synthetic peptides from four separate regions of the poliovirus type 1 capsid protein VP1 induce neutralizing antibodies.

Isolated poliovirus capsid protein VP1 induces a neutralizing response in rats.

Evidence for Conformational Changes of Poliovirus Precursor Particles during Virus Morphogenesis

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