Characterisation of a protective linear B cell epitope against feline parvoviruses
Identifieur interne : 003590 ( Main/Exploration ); précédent : 003589; suivant : 003591Characterisation of a protective linear B cell epitope against feline parvoviruses
Auteurs : Jan P. M. Langeveld [Pays-Bas] ; Jorge Martinez-Torrecuadrada [Espagne] ; Ronald S. Boshuizen [Pays-Bas] ; Rob H. Meloen [Pays-Bas] ; J. Ignacio Casal [Espagne]Source :
- Vaccine [ 0264-410X ] ; 2001.
English descriptors
- KwdEn :
- Teeft :
- Acid level, Aluminium hydroxide, Amino, Amino acid, Amino acids, Amino terminus, Antibody binding, Antibody titres, Antigenic, Antigenic site, Antigenic sites, Antipeptide, Antipeptide antibodies, Canine, Canine parvovirus, Casal, Coating antigen, Core sequence, Deletion scan, Elisa, Elsevier science, Epitope, Feline parvoviruses, Guinea pigs, Guinea pigs immunised, High dilution, Horse serum, Ignacio casal, Immunised, Lange6eld, Linear epitope, Linear epitopes, Maternal immunity, Minimal amount, Minimal dose, Minimal sequence, Monoclonal antibodies, Natural host, Negative effect, Neutralisation, Neutralising, Neutralising activity, Neutralising antibodies, Neutralising capability, Neutralising mabs, Neutralising titres, Nucleotide sequence, Parvovirus, Pepscan, Pepscan analysis, Peptide, Peptide qpdggqpavr, Peptide synthesis, Peptide vaccine, Rabbits immunised, Replacement analysis, Sequence gqpavrnera, Synthetic peptide, Synthetic peptides, Target animals, Terminus, Titre, Vaccine, Vaccine formulation, Viral disease, Virol, Virus neutralisation.
Abstract
Abstract: Monoclonal antibody 3C9 was the starting material in the definition of the epitope that led to the synthesis of the first efficient peptide vaccine against a viral disease (canine parvovirus) in the natural host (dog). In this report, we have analysed the specificity of the antibody at the single amino acid level and the contribution of each residue to the binding, using multiple length analysis. Moreover, a replacement analysis allowed determining those critical residues for the binding. Finally, in an attempt to optimise the production cost of the vaccine, we have determined that the minimal dose required for induction of protective antibodies can be as low as 0.5 μg of peptide. Also, KLH can be replaced as a carrier for a much cheaper alternative such as ovalbumine. All these findings implicate a substantial reduction in the cost of the vaccinal dose.
Url:
DOI: 10.1016/S0264-410X(00)00526-0
Affiliations:
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Le document en format XML
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<term>Minimal dose</term>
<term>Minimal sequence</term>
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<term>Neutralisation</term>
<term>Neutralising</term>
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<term>Neutralising antibodies</term>
<term>Neutralising capability</term>
<term>Neutralising mabs</term>
<term>Neutralising titres</term>
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<front><div type="abstract" xml:lang="en">Abstract: Monoclonal antibody 3C9 was the starting material in the definition of the epitope that led to the synthesis of the first efficient peptide vaccine against a viral disease (canine parvovirus) in the natural host (dog). In this report, we have analysed the specificity of the antibody at the single amino acid level and the contribution of each residue to the binding, using multiple length analysis. Moreover, a replacement analysis allowed determining those critical residues for the binding. Finally, in an attempt to optimise the production cost of the vaccine, we have determined that the minimal dose required for induction of protective antibodies can be as low as 0.5 μg of peptide. Also, KLH can be replaced as a carrier for a much cheaper alternative such as ovalbumine. All these findings implicate a substantial reduction in the cost of the vaccinal dose.</div>
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