[The antigenic structure of the eastern equine encephalomyelitis virus studied by using monoclonal antibodies].

Thirty-three monoclonal antibodies (Mabs) interacting with the structural proteins of Eastern equine encephalomyelitis (EEE) virus were prepared. The mutual arrangement of the antigenic sites on the E1 and E2 glycoproteins was studied by competitive radioimmunoassay. At least four nonoverlapping sites were found on the E1. The E2 glycoprotein contained at least seven partially overlapping antigenic sites. Mabs to the sites E2-2 and E2-3 neutralized viral infectivity and blocked hemagglutination. Mabs to the site E2-1 blocked hemagglutination. Mabs to sites E2-2, 3, and 7 protected mice against lethal infection although the protective Mabs to sites E2-2b and E2-7 did not neutralize the virus. The antibodies to the other three sites of E2 and to all sites of E1 did not have any biological activity. The experimental results indicate the dominant role of E2 in antiviral immunity, over 98% of the observed protective effect being associated with the E2-2 site.