Identification of a common conformational epitope on the glycoprotein e2 of classical swine fever virus and border disease virus
Journal
Viruses
Journal Volume
13
Journal Issue
8
Date Issued
2021-08-01
Author(s)
Huang, Yu Liang
Meyer, Denise
Postel, Alexander
Tsai, Kuo Jung
Liu, Hsin Meng
Yang, Chia Huei
Huang, Yu Chun
Berkley, Nicholas
Deng, Ming Chung
Becher, Paul
Crooke, Helen
Abstract
Classical swine fever virus (CSFV) shares high structural and antigenic homology with bovine viral diarrhea virus (BVDV) and border disease virus (BDV). Because all three viruses can infect swine and elicit cross-reactive antibodies, it is necessary to differentiate among them with regard to serological diagnosis of classical swine fever. To understand the mechanism of cross-reactivity, it is important to define common or specific epitopes of these viruses. For this purpose, epitope mapping of six monoclonal antibodies (mAbs) was performed using recombinant expressed antigenic domains of CSFV and BDV E2 proteins. One CSFV-specific conformational epitope and one CSFV and BDV common epitope within domain B/C of E2 were identified. Site-directed mutagenesis confirmed that residues G725 and V738/I738 of the CSFV-specific epitope and P709/L709 and E713 of the second epitope are important for mAbs binding. Infection of CSFV in porcine cells was significantly reduced after pre-incubation of the cells with the domain B/C of E2 or after pre-incubation of CSFV with the mAbs detecting domain B/C. 3D structural modeling suggested that both epitopes are exposed on the surface of E2. Based on this, the identified epitopes represent a potential target for virus neutralization and might be involved in the early steps of CSFV infection.
Subjects
Attachment | Border disease virus | Classical swine fever virus | Conformational epitope | Cross reactivity | Entry | Epitope mapping | Glycoprotein E2
SDGs
Publisher
MDPI
Type
journal article