What question did this study set out to answer?

To evaluate the capacity of chemically modified and cleaved foot-and-mouth disease virus capsid protein VPT to stimulate neutralizing antibodies and to assess N-terminal sequence homology across three viral serotypes.

January 1, 1979Intervirology

Foot-and-Mouth Disease Virus Immunogenic Capsid Protein VPT: N-Terminal Sequences and Immunogenic Peptides Obtained by CNBr and Tryptic Cleavages

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To evaluate the capacity of chemically modified and cleaved foot-and-mouth disease virus capsid protein VPT to stimulate neutralizing antibodies and to assess N-terminal sequence homology across three viral serotypes.
Treated the ~30 kDa capsid protein VPT with chemical modifications (glutaraldehyde, carboxymethylation, maleylation, citraconylation) and cleaved it using cyanogen bromide (CNBr) or trypsin.
Assayed neutralizing antibody induction in guinea pig models following inoculation with modified proteins and cleavage peptides.
Sequenced and aligned the initial 26 N-terminal amino acids of VPT across virus types A12 (strain 119), C3 (Resende), and O1 (Brugge).
Chemical treatment with glutaraldehyde, carboxymethylation, maleylation, or citraconylation abolished VPT immunogenicity, though de-citraconylation partially restored the antibody response.
CNBr cleavage of type A12 VPT generated an immunogenic ~13 kDa peptide, while tryptic virion cleavage yielded an immunogenic ~16 kDa doublet (VPTab).
Sequence analysis revealed approximately 85% amino acid homology across the first 26 N-terminal residues among types A12, C3 Resende, and O1 Brugge.

Structured PICO

Population

Guinea pigs and foot-and-mouth disease virus (types A12 strain 119, C3 Resende, and O1 Brugge)

Intervention

Chemical modifications (glutaraldehyde treatment, carboxymethylation, maleylation, citraconylation, de-citraconylation) and CNBr or tryptic cleavages of the immunogenic capsid protein (VPT)

Outcome

Ability to induce neutralizing antibody in guinea pigs and N-terminal amino sequence homologysurrogate

Chemical modifications alter the immunogenicity of the foot-and-mouth disease virus capsid protein VPT, which shares high N-terminal sequence homology across different virus types.

Discussion

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Implication

Chemical modifications of VPT may guide FMDV epitope mapping; leaves open translation of N-terminal homology to cross-protection.

Cite This Study

Bachrach et al. (1979) studied this question.

synapsesocial.com/papers/6a95ab9f6b8b09e0de4bcbeb https://doi.org/10.1159/000149070

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Foot-and-Mouth Disease Virus Immunogenic Capsid Protein VPT: N-Terminal Sequences and Immunogenic Peptides Obtained by CNBr and Tryptic Cleavages

Key Points

Structured PICO

Discussion

Implication

Cite This Study

Foot-and-Mouth Disease Virus Immunogenic Capsid Protein VPT: N-Terminal Sequences and Immunogenic Peptides Obtained by CNBr and Tryptic Cleavages

Key Points

Structured PICO

Discussion

Implication

Cite This Study

Also Consider

Also Consider