Treatment of Semliki Forest virus with Nonidet-P40, sodium deoxycholate or Tween 80 + ether destroyed virus infectivity but preserved complement fixing, haem-agglutinating and neutralizing antibody blocking activities. All treatments split the virus into intact cores and fragments of envelope, but Nonidet gave the best separation of these components. Only the virus envelope had haemagglutinating and neutralizing antibody-blocking activities. Immunodiffusion tests showed that the envelope and core proteins were serologically distinct.

Further treatment of envelope fragments with dilute trypsin liberated at least three antigens, which could be separated by column chromatography. In immuno-diffusion tests, antigens 2 and 3 were serologically distinct, but both gave reactions of partial identity with antigen 1. All antigens fixed complement, but only antigen 1 was associated with haemagglutinating and neutralizing antibody-blocking activities. Sephadex gel filtration indicated that antigen 1 had a particle weight greater than 200,000 daltons, that antigen 3 had a molecular weight of about 9000, and that antigen 2 was intermediate in size.


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