Antigenic domains analysis of classical swine fever virus E2 glycoprotein by mutagenesis and conformation-dependent monoclonal antibodies
Journal
Virus Research
Journal Volume
149
Journal Issue
2
Pages
183-189
Date Issued
2010
Author(s)
Huang, Chin-Cheng
Lin, Yu-Ju
Deng, Ming-Chung
Chen, Hui-Chun
Tsai, Chiung-Hui
Chang, Wei-Ming
Abstract
Glycoprotein E2 of classical swine fever virus (CSFV) is the major antigenic protein exposed on the outer surface of the virion that induces main neutralizing antibodies during infection in pigs. This study displays the differences in antigenicity of E2 between vaccine and field strains of CSFV by their variable reaction patterns between expressed proteins and monoclonal antibodies (mAbs). The D/A domains of various CSFVs were relatively conserved and recognized by all mAbs against the A domain. However, mAbs against B/C domains were able to differentiate field viruses TD/96/TWN (subgroup 2.1) and 94.4/IL/94/TWN (subgroup 3.4) from the vaccine virus LPC/AHRI (subgroup 1.1). By analysis of expressed truncated proteins, the epitope(s) on B/C domains were mapped to the N-terminal 90 residues of E2 between amino acids 690 and 779. Site-directed mutagenesis further showed that residues 693C, 737C, 771L, 772L, 773F and 774D were critical for the reactivity of E2 protein with mAbs. Thus, the B/C domains are responsible for antigen specificity among various CSFVs, and the disulfide bond and motif 771LLFD774 are essential for the structural integrity of its conformational recognition. These data significantly increase our understanding of the antigenic structure of E2 for antibody binding. © 2010 Elsevier B.V.
Subjects
Antigenic domain; Classical swine fever virus; E2 glycoprotein; Monoclonal antibodies; Site-directed mutagenesis
SDGs
Other Subjects
epitope; glycoprotein E2; monoclonal antibody; monoclonal antibody C2; monoclonal antibody L150; monoclonal antibody L7; monoclonal antibody T23; monoclonal antibody T33; monoclonal antibody T4; monoclonal antibody V2; monoclonal antibody V8; monoclonal antibody WH303; unclassified drug; amino acid substitution; amino terminal sequence; animal cell; antigen binding; antigen recognition; antigen specificity; antigenicity; article; binding affinity; controlled study; disulfide bond; nonhuman; Pestivirus; priority journal; protein domain; protein expression; protein motif; site directed mutagenesis; virus strain; Amino Acid Sequence; Animals; Antibodies, Monoclonal; Antibodies, Viral; Antigens, Viral; Classical swine fever virus; Conserved Sequence; Epitopes; Molecular Sequence Data; Mutagenesis; Protein Structure, Tertiary; Sequence Alignment; Sequence Deletion; Swine; Viral Envelope Proteins; Classical swine fever virus; Suidae
Type
journal article