A protective anti-peptide antibody against the immunodominant site of the A24 Cruzeiro strain of foot-and-mouth disease virus and its reactivity with other subtype viruses containing the same minimum binding sequence

Eight neutralizing and two non-neutralizing antifoot-and-mouth disease virus (FMDV) bovine IgG1 and IgG2 monoclonal antibodies (BMAbs) recognize conformationally dependent epitopes. The majority of those shown to neutralize virus passively protected mice from virus challenge, regardless of isotype. Well-characterized anti-FMDV mouse MAbs, representing five independent neutralizing epitopes on O 1 serotype virus, were examined with each of the ten BMAbs in a competition-based ELISA. Five of the neutralizing BMAbs (C48, C65, C74, C83 and MH6) were shown to be directed against epitopes on, or in close proximity to, that previously defined as neutralizing antigenic site 2. Another neutralizing BMAb, MH5, bound to an epitope on, or in close proximity to antigenic site 3. Two neutralizing BMAbs (C2 and C96) simultaneously

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“…This was performed using a twodimensional micro-neutralization technique previously described by Barnett et al (1996).…”

Section: Rna Extraction and Sequencing Of Bmab Selected Virus Mutantsmentioning

confidence: 99%

Monoclonal antibodies, against O1 serotype foot-and-mouth disease virus, from a natural bovine host, recognize similar antigenic features to those defined by the mouse.

Barnett

Samuel

Püllen

et al. 1998

Journal of General Virology

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“…A chemically synthesized peptide corresponding to the region including amino acids 141 to 159 of VP1 of the serotype A, subtype 12, virus (VP1 141-159 ), with the sequence CH 3 ). An additional cysteine residue (represented by the double-underlined letter) was added at the N terminus of the peptide to facilitate its conjugation to KLH.…”

Section: Synthetic Peptidesmentioning

confidence: 99%

Intranasal Immunization of Guinea Pigs with an Immunodominant Foot-and-Mouth Disease Virus Peptide Conjugate Induces Mucosal and Humoral Antibodies and Protection against Challenge

Fischer

Rood

Barrette

et al. 2003

J Virol

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Guinea pigs immunized intranasally with a keyhole limpet hemocyanin-linked peptide, corresponding to the prominent G-H loop of the VP1 protein of foot-and-mouth disease virus, raised substantial levels of antipeptide and virus-neutralizing antibodies in sera and of peptide-specific secretory immunoglobulin A in nasal secretions. In groups of animals immunized intranasally without adjuvant, 86 percent were fully protected upon challenge with homotypic virus. Surprisingly, animals given the peptide conjugates plus the mucosal adjuvant cholera toxin were afforded only partial protection in that primary lesions were observed in most animals, although spread to other feet was prevented. These results indicate that intranasal inoculation with the peptide offers a potential route of vaccination against foot-and-mouth disease and may be useful for eliciting protection in the upper respiratory tracts of susceptible animals.

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Infectious bursal disease subviral particles displaying the foot-and-mouth disease virus major antigenic site

Remond¹,

Costa²,

Sabine³

et al. 2009

Vaccine

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A protective anti-peptide antibody against the immunodominant site of the A24 Cruzeiro strain of foot-and-mouth disease virus and its reactivity with other subtype viruses containing the same minimum binding sequence

Cited by 9 publications

References 34 publications

Monoclonal antibodies, against O1 serotype foot-and-mouth disease virus, from a natural bovine host, recognize similar antigenic features to those defined by the mouse.

Monoclonal antibodies, against O1 serotype foot-and-mouth disease virus, from a natural bovine host, recognize similar antigenic features to those defined by the mouse.

Intranasal Immunization of Guinea Pigs with an Immunodominant Foot-and-Mouth Disease Virus Peptide Conjugate Induces Mucosal and Humoral Antibodies and Protection against Challenge

Infectious bursal disease subviral particles displaying the foot-and-mouth disease virus major antigenic site

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