Monospecific Antisera Against Capsid Polypeptides of Poliovirus Type 1 Distinguish Antigenic Structures of Poliovirus Proteins

Wiegers, Klaus; Dernick, Rudolf

doi:10.1099/0022-1317-64-4-777

Cited by 14 publications

(2 citation statements)

References 25 publications

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“…P19S--- (49). The treated lysate and a control, untreated lysate were immunoprecipitated with various antisera, eluted, and analyzed on a 20-cm 12.5% polyacrylamide slab gel.…”

Section: P28-vp1--' Vp3mentioning

confidence: 99%

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

Grubman¹,

Robertson²,

Morgan³

et al. 1984

J Virol

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Pulse-chase labeling of foot-and-mouth disease virus-infected bovine kidney cells revealed stable and unstable viral-specific polypeptides. To identify precursor-product relationships among these polypeptides, antisera against a number of structural and nonstructural viral-specific polypeptides were used. Cell-free translations programmed with foot-and-mouth disease virion RNA or foot-and-mouth disease virus-infected bovine kidney cell lysates, which were shown to contain almost identical polypeptides, were immunoprecipitated with the various antisera. To further establish identity, some proteins were compared by partial protease digestion. Evidence for a membrane association of the polypeptides coded for by the middle genome region is also presented. A biochemical map of the foot-and-mouth disease virus genome was established from the above information.

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“…P19S--- (49). The treated lysate and a control, untreated lysate were immunoprecipitated with various antisera, eluted, and analyzed on a 20-cm 12.5% polyacrylamide slab gel.…”

Section: P28-vp1--' Vp3mentioning

confidence: 99%

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

Grubman¹,

Robertson²,

Morgan³

et al. 1984

J Virol

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“…Continuous and discontinuous neutralization epitopes. Circumstantial evidence for continuous neutralization epitopes on poliovirus polypeptides was obtained by immunization of animals with isolated polypeptides purified by a variety of different procedures (3,4,6,34,37). In some cases, synthetic peptides selected on the basis of hydrophilicity profiles of viral polypeptides were also found to induce a low neutralizing response (5,(9)(10)(11)43).…”

Section: Discussionmentioning

confidence: 99%

Molecular basis for linkage of a continuous and discontinuous neutralization epitope on the structural polypeptide VP2 of poliovirus type 1

Wiegers

Wetz

Dernick

1990

J Virol

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We obtained neutralizing monoclonal antibodies against a continuous neutralization epitope on VP2 of poliovirus type 1 strain Mahoney by using a combined in vivo-in vitro immunization procedure. The antibody-binding site was mapped to amino acid residues within the peptide segment (residues 164 through 170) of VP2 by competition with synthetic peptide and sequencing of resistant mutants. Cross-neutralization of these mutants with another neutralizing monoclonal antibody revealed a linkage of the continuous epitope and a discontinuous neutralization epitope involving both loops of the double-loop structure of VP2 at the twofold axis on the surface of the virion.

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Preparative separation of poliovirus structural polypeptides by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis, copper staining and electroelution, and induction of monospecific antisera

Tessmer

Dernick

1989

Electrophoresis

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Viral polypeptides were prepared by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) followed by copper staining and electroelution from gel slices. Poliovirus capsid polypeptide VP 1 isolated by this procedure induced monospecific antibodies in rabbits, i.e., antisera reacting only with the homologous polypeptide. Our results demonstrate the applicability of the described copper staining method as a rapid visualization step for preparing viral proteins after SDS-PAGE.

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Monospecific Antisera Against Capsid Polypeptides of Poliovirus Type 1 Distinguish Antigenic Structures of Poliovirus Proteins

Cited by 14 publications

References 25 publications

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

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

Molecular basis for linkage of a continuous and discontinuous neutralization epitope on the structural polypeptide VP2 of poliovirus type 1

Preparative separation of poliovirus structural polypeptides by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis, copper staining and electroelution, and induction of monospecific antisera

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