https://scholars.lib.ntu.edu.tw/handle/123456789/624620
標題: | Identification of conformational epitopes and antigen-specific residues at the D/A domains and the extramembrane C-terminal region of E2 glycoprotein of classical swine fever virus | 作者: | CHIA-YI CHANG Huang, Chin-Cheng Deng, Ming-Chung Huang, Yeou-Liang Lin, Yu-Ju Liu, Hsin-Meng Lin, Yeou-Liang FUN-IN WANG |
關鍵字: | Antigenic specificity; Classical swine fever virus; Conformational epitope; E2 glycoprotein; Homodimerization | 公開日期: | 2012 | 卷: | 168 | 期: | 44563 | 起(迄)頁: | 56-63 | 來源出版物: | Virus Research | 摘要: | Envelope glycoprotein E2 of classical swine fever virus (CSFV) is the major antigen that induces neutralizing antibodies in infected pigs. Previous studies revealed that both conformation-dependent and linear epitopes are most present within domains B/C/D/A in the N-terminal half of E2. However, studies of antigenicity beyond the B/C domains remain limited. This study revealed that conformational epitopes were present on the D/A domains as well as the proximal C-terminal of E2, since the mutation of cysteine abrogated their bindings to monoclonal antibodies (mAbs). The residue R845 at domain A and E902 at the C-terminal region were critical for specific binding to mAbs, further supporting the presence of antigenic determinants on these regions. Substitutions of cysteines in domains D/A not only abrogated the binding to mAbs directed to D/A, but also affected the binding of the downstream C-terminal region to its specific mAbs, suggesting a close interaction between the two conformational epitopes. Mutations on the five proximal cysteines at positions 869, 877, 893, 896 and 930 in the C-terminal region only affected the binding to its specific mAbs binding sites. In addition, mutation on the three distal C-terminal cysteines at positions 945, 966, and 983 resulted in loss of E2 homodimerization. This study demonstrates new antigenic epitopes on D/A domains and C-terminal of E2 that have not been reported before, and that the nine cysteines in the C-terminal function differently in either maintaining the antigenic structure or in intermolecular dimerization of E2. © 2012 Elsevier B.V. |
URI: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84864408569&doi=10.1016%2fj.virusres.2012.06.013&partnerID=40&md5=13fb40228755b7554e621e2e750c8086 https://scholars.lib.ntu.edu.tw/handle/123456789/624620 |
ISSN: | 01681702 | DOI: | 10.1016/j.virusres.2012.06.013 | SDG/關鍵字: | cysteine; epitope; glycoprotein E2; virus envelope protein; amino acid substitution; antigen binding; antigen specificity; article; Baculovirus; binding site; carboxy terminal sequence; conformational transition; controlled study; dimerization; nonhuman; Pestivirus; priority journal; protein domain; protein expression; protein interaction; site directed mutagenesis; virus mutation; Amino Acid Motifs; Amino Acid Sequence; Animals; Antibodies, Viral; Cell Membrane; Classical Swine Fever; Classical swine fever virus; Epitope Mapping; Molecular Sequence Data; Protein Structure, Tertiary; Swine; Viral Envelope Proteins; Classical swine fever virus; Suidae |
顯示於: | 獸醫學系 |
在 IR 系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。