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Identification of B‐cell epitopes on the betanodavirus capsid protein

Identifieur interne : 000344 ( Istex/Curation ); précédent : 000343; suivant : 000345

Identification of B‐cell epitopes on the betanodavirus capsid protein

Auteurs : J Z Costa [Royaume-Uni] ; A. Adams [Royaume-Uni] ; J E Bron [Royaume-Uni] ; K D Thompson [Royaume-Uni] ; W G Starkey [Royaume-Uni] ; R H Richards [Royaume-Uni]

Source :

RBID : ISTEX:8ADB04A13BE598E6911D369B8BB910790FEE7552

Abstract

The pepscan procedure was used to identify betanodavirus B‐cell epitopes recognized by neutralizing mouse monoclonal antibodies (MAbs) and serum samples obtained from sea bass, Dicentrarchus labrax, naturally infected with betanodavirus. Pepscan was performed with a panel of thirty‐four 12‐mer synthetic peptides that mimicked the entire betanodavirus capsid protein. Sea bass serum samples reacted strongly with three regions of the capsid protein comprising amino acid residues 1–32, 91–162 and 181–212. The latter region was also recognized by neutralizing MAbs and coincided with a region of high antigenic propensity identified by an antigen prediction algorithm. These data suggest that a region of the betanodavirus capsid protein spanning amino acid residues 181–212 may represent a neutralization domain that could potentially be used to inform the development of nodavirus vaccines and immunodiagnostic reagents.

Url:
DOI: 10.1111/j.1365-2761.2007.00824.x

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ISTEX:8ADB04A13BE598E6911D369B8BB910790FEE7552

Le document en format XML

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<div type="abstract" xml:lang="en">The pepscan procedure was used to identify betanodavirus B‐cell epitopes recognized by neutralizing mouse monoclonal antibodies (MAbs) and serum samples obtained from sea bass, Dicentrarchus labrax, naturally infected with betanodavirus. Pepscan was performed with a panel of thirty‐four 12‐mer synthetic peptides that mimicked the entire betanodavirus capsid protein. Sea bass serum samples reacted strongly with three regions of the capsid protein comprising amino acid residues 1–32, 91–162 and 181–212. The latter region was also recognized by neutralizing MAbs and coincided with a region of high antigenic propensity identified by an antigen prediction algorithm. These data suggest that a region of the betanodavirus capsid protein spanning amino acid residues 181–212 may represent a neutralization domain that could potentially be used to inform the development of nodavirus vaccines and immunodiagnostic reagents.</div>
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