Institute of Virology, Department of Infectious Diseases, University of Veterinary Medicine, Buenteweg 17, DE-30559 Hannover, Germany.
Virology. 2012 Nov 10;433(1):45-54. doi: 10.1016/j.virol.2012.06.029. Epub 2012 Aug 4.
The E(rns) 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 E(rns)-specific monoclonal antibodies were investigated. Mapping experiments using chimeric E(rns) proteins, site-directed mutagenesis and an overlapping peptide library identified one antigenic region located between amino acids (aa) 55 to 110 on the E(rns) protein of CSFV Alfort/187. The domain comprises three linear motifs *(64)TNYTCCKLQ(72), (73)RHEWNKHGW(81), and (88)DPWIQLMNR(96), 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 E(rns) and provide valuable information with regard to the development of E(rns)-based diagnostic tests.
经典猪瘟病毒（CSFV）的 E(rns)糖蛋白在生化和功能特性方面已经得到了详细研究，但其抗原结构知之甚少。为了确定 CSFV 特异性抗体识别的表位，研究了七种 E(rns)特异性单克隆抗体的结合位点。使用嵌合 E(rns)蛋白、定点突变和重叠肽文库进行的作图实验确定了 E(rns)蛋白上位于氨基酸 (aa) 55 至 110 之间的一个抗原区域 CSFV Alfort/187。该结构域包含三个线性基序 *(64)TNYTCCKLQ(72)、(73)RHEWNKHGW(81)和 (88)DPWIQLMNR(96)，以及位置 102 和 107 的两个 aa，它们对于与抗体的相互作用至关重要。此外，表位以正确构象呈现对于有效的抗体结合是必需的。这些发现使我们能够更好地理解 E(rns)的组织和结构，并为基于 E(rns)的诊断测试的开发提供了有价值的信息。
