CHIA-YI CHANGHuang, Chin-ChengChin-ChengHuangDeng, Ming-ChungMing-ChungDengHuang, Yeou-LiangYeou-LiangHuangLin, Yu-JuYu-JuLinLiu, Hsin-MengHsin-MengLiuLin, Yeou-LiangYeou-LiangLinFUN-IN WANG2022-11-112022-11-11201201681702https://www.scopus.com/inward/record.uri?eid=2-s2.0-84855610774&doi=10.1016%2fj.virusres.2011.09.019&partnerID=40&md5=e3ea76bbaf9c7db698dc921cb0888652https://scholars.lib.ntu.edu.tw/handle/123456789/624621Envelope glycoprotein E2 of classical swine fever virus (CSFV) is the major antigen that induces neutralizing antibodies in infected pigs. The conformational epitope(s) on B/C domains were mapped to the N-terminal 90 residues of E2 between amino acids 690 and 779 (Chang et al., 2010a). To mimic the conformational epitopes, a set of synthetic cyclized peptides spanning the B/C domains of E2 were used to react with monoclonal antibodies (mAbs) against E2 and with swine anti-CSFV polyclonal sera. All antibodies recognized a highest common element, 753RYLASLHKKALPTSV 767, on the double-looped peptides. This epitope region has not been revealed previously in the literature. Both substitution-scanning of residues 753RYLASLHKKALPTSV 767 on a double-looped peptide and site-directed mutagenesis of expressed E2 demonstrated that residues 761K, 763L and 764P were critical for the reactivity with mAbs. In addition, the up- and downstream residues 753R, 754Y, 755L and 765T were also crucial. Alignment showed that this stretch of amino acids was relatively conserved among various CSFVs. Thus, we identified a motif 753RYLASLHKKALPT 765, which may be part of group-specific antigen and important for the structural integrity of conformational epitope recognition. © 2011 Elsevier B.V.Antigen mimicking; Classical swine fever virus; Conformational epitope; Cyclized peptide; E2 glycoprotein; Epitope reconstructionamino acid; glycoprotein E2; monoclonal antibody; article; conformation; controlled study; diagnostic test; mutagenesis; nonhuman; Pestivirus; priority journal; protein expression; Amino Acid Substitution; Animals; Antibodies, Monoclonal; Antibodies, Viral; Antigens, Viral; Classical swine fever virus; Cysteine; DNA Mutational Analysis; Epitope Mapping; Epitopes; Peptides, Cyclic; Swine; Viral Envelope Proteins; Classical swine fever virus; Suidaejournal article10.1016/j.virusres.2011.09.019219456362-s2.0-84855610774