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dc.contributor.authorHeuzenroeder, M.en
dc.contributor.authorBarton, M.en
dc.contributor.authorVanniasinkam, T.en
dc.contributor.authorPhumoonna, T.en
dc.identifier.citationEpitope Mapping Protocols, 2009 / Ch.10, pp.137-144en
dc.description.abstractThe aim of this chapter is to provide a strategy for mapping linear antibody epitopes of protein antigens in order to discover candidates for vaccines or diagnostic tests. A set of overlapping peptides was designed and synthesised based upon a known amino acid sequence of the target protein, virulence-associated protein A (VapA) of the bacterium Rhodococcus equi, an important pulmonary pathogen in foals. The peptides were biotinylated and used in an ELISA to screen immune sera from foals. These biotinylated peptides were coated directly onto micro titre plates that had been pre-coated with NeutrAvidin™. A linear B-cell epitope was identified by a universal recognition of sera to the synthetic peptides which corresponds to a particular fragment of the VapA protein.en
dc.description.statementofresponsibilityMichael W. Heuzenroeder, Mary D. Barton, Thiru Vanniasinkam and Tongted Phumoonnaen
dc.publisherHumana Pressen
dc.relation.ispartofseriesMethods in Molecular Biology ; v. 524en
dc.subjectEpitope mapping; Linear B-cell epitope; Biotinylated peptides; ELISA; VapA; Rhodococcus equien
dc.titleLinear B-cell epitope mapping using enzyme-linked immunosorbent assay for libraries of overlapping synthetic peptidesen
dc.typeBook chapteren
Appears in Collections:Animal and Veterinary Sciences publications

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