Abstract
Three viral proteins were separated from the TC-83 strain of Venezuelan equine encephalomyelitis virus by discontinuous polyacrylamide gel electrophoresis after disruption with sodium dodecyl sulfate and beta-2-mercaptoethanol. These proteins were inoculated into rabbits and the resultant antisera were tested for immunological activity by gel precipitation, plaque reduction neutralization, hemagglutination inhibition (HI), complement fixation, fluorescence microscopy, and mouse protection studies. All proteins were capable of stimulating precipitating antibody in rabbits, but the largest protein (VP 1), which is contained in the envelope, stimulated the production of detectable neutralizing and HI antibody against the intact virion. The other two proteins yielded little or no neutralizing or HI antibody.