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Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
Published on: March 24, 2017
Characterization of monoclonal antibodies to bovine enteric coronavirus and antigenic variability among Quebec
1Centre de Recherche en Virologie, Institut Armand-Frappier, Université du Québec, Laval-des-Rapides, Canada.
Abstract:
Twenty monoclonal antibodies (MAbs) were prepared against the Mebus strain of bovine enteric coronavirus, 14 of them reacting with the peplomeric S (gp 100) glycoprotein. Competition binding assays allowed the definition of at least 4 distinct antigenic domains for the S glycoprotein, designated as A, B, C, and D; epitopes associated to neutralizing activity being located in sites A, B, and C. One MAb directed to the hemagglutinin HE (gp 140/gp 65) glycoprotein inhibited the hemagglutinating activity of the virus, but had no neutralizing activity. Comparison of Quebec enteropathogenic BCV isolates using polyclonal antiserum and MAbs directed to the S glycoprotein confirmed their close antigenic relationship, but also revealed the occurrence of at least three distinct antigenic subgroups. Antigenic domain D was highly conserved among BCV isolates, as well as non-neutralizing epitopes assigned to antigenic domains A and C. The Minnesota strain of turkey enteric coronavirus could be distinguished from BCV isolates by MAbs directed to epitopes of antigenic domain C, whereas human coronavirus HCV-OC 43 could be distinguished by MAbs directed to epitopes of antigenic domain A. The porcine hemagglutinating encephalomyelitis virus could be distinguished from the other hemagglutinating coronaviruses by neutralizing epitopes located on antigenic domains A, B, and C.
Insights
Monoclonal antibodies identified distinct antigenic domains on bovine enteric coronavirus, aiding in differentiating viral strains and understanding immune responses. This research provides critical insights into coronavirus antigenicity and strain variation.
Area of Science:
- Virology
- Immunology
- Molecular Biology
Background:
- Bovine enteric coronavirus (BCV) causes significant enteric disease in cattle.
- Understanding the antigenic properties of BCV is crucial for developing effective diagnostics and vaccines.
- Monoclonal antibodies (MAbs) are valuable tools for dissecting viral antigenicity.
Purpose of the Study:
- To characterize the antigenic domains of the bovine enteric coronavirus S glycoprotein.
- To differentiate between various BCV isolates and related coronaviruses.
- To identify neutralizing and non-neutralizing epitopes on viral surface glycoproteins.
Main Methods:
- Production and characterization of 20 monoclonal antibodies against the Mebus strain of BCV.
- Competition binding assays to define antigenic domains (A, B, C, D) of the S glycoprotein.
- Analysis of MAb reactivity against different BCV isolates and other coronaviruses (turkey enteric coronavirus, human coronavirus OC43, porcine hemagglutinating encephalomyelitis virus).
Main Results:
- 14 MAbs reacted with the S glycoprotein, defining at least 4 antigenic domains (A-D).
- Neutralizing activity was associated with epitopes in domains A, B, and C.
- One MAb against the HE glycoprotein inhibited hemagglutination but lacked neutralizing activity.
- BCV isolates showed close antigenic relationships but formed at least three distinct subgroups.
- Domain D and non-neutralizing epitopes in domains A and C were highly conserved.
- Specific MAbs distinguished BCV from turkey and human coronaviruses, and from porcine hemagglutinating encephalomyelitis virus.
Conclusions:
- The S glycoprotein of BCV possesses at least four distinct antigenic domains.
- Epitopes in domains A, B, and C are critical for viral neutralization.
- Monoclonal antibodies are effective tools for classifying BCV strains and related coronaviruses.
- Conserved and variable epitopes provide targets for diagnostic and vaccine development.
