Forty-four monoclonal antibodies (MAbs) to the G isolate of bovine enteric coronavirus were used for the characterization of the peplomer proteins S and HE. Fourteen of these MAbs reacted with HE and the remaining 30 with the products of the S gene, S1 (19 MAbs), S2 (six MAbs) and gp200 (five MAbs). S1 and HE were found to carry major neutralization determinants, and S1 appeared to elicit the production of the MAbs displaying the highest neutralizing activity. The topography of the epitopes was assessed by means of a competitive binding assay; the 44 MAbs defined four independent antigenic domains on S1, two on S2, one on gp200 and two on HE. All the neutralizing anti-S1 MAbs mapped in antigenic sites A and B and all the neutralizing anti-HE MAbs in HE-B. Antigenic site S1-B was further subdivided into four subsites. Functional mapping was performed by testing a library of neutralization-resistant mutants against the neutralizing MAbs. Analysis of their reactivity in a neutralization test confirmed the overall distribution of epitopes in S1-B and HE-B.


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