Abstract
The Erns glycoprotein of classical swine fever virus (CSFV) has been studied in detail concerning biochemical and functional properties, whereas less is known about its antigenic structure.In order to define epitopes recognized by CSFV-specific antibodies, the binding sites of seven Erns-specific monoclonal antibodies were investigated. Mapping experiments using chimeric Erns proteins, site-directed mutagenesis and an overlapping peptide library identified one antigenic region located between amino acids (aa) 55 to 110 on the Erns protein of CSFV Alfort/187. The domain comprises three linear motifs ⁎64TNYTCCKLQ72, 73RHEWNKHGW81, and 88DPWIQLMNR96, respectively, and two aa at position 102 and 107 that are crucial for the interaction with antibodies. Additionally, the presentation of the epitope in a correct conformation is mandatory for an efficient antibody binding. These findings allow a better understanding of the organization and the structure of the Erns and provide valuable information with regard to the development of Erns-based diagnostic tests.
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