Chikungunya virus (CHIKV) was purified and subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis in discontinuous buffer systems. Three bands were revealed by staining with Coomassie blue; two of them (E1 and E2) were associated with the membrane, and one (C) with the core. Their molecular weights were estimated to be 56,000 (E1), 52,000 (E2), and 36,000 (C), irrespective of the concentration of acrylamide in the gels. The molar ratios of E1, E2, and C were almost equal when the sample buffer was Tris-HC1, whereas they were different when phosphate buffer was used.Chikungunya virus (CHIKV) is an alphavirus belonging to the Togaviridae, spherical in shape, 50-60 nm in size, and possessing a core structure surrounded by a membrane which has fine projections. The core structure, 30 nm in diameter, appears in the cytoplasm of infected cells and its envelopment takes place by budding through plasma membranes during the maturation process (11,16,22). These morphological characteristics are in common with those described for other members of alphaviruses, such as Western equine encephalitis (WEE) (17), Semliki Forest (SF) (1), and Sindbis (Sb) (3).Current knowledge of the chemical properties of CHIKV, however, is inadequate. While Igarashi et al (12) reported that CHIKV has 2 species of protein, a core protein and a hemagglutinin, the possibility that additional protein(s) can be identified should be considered, since it has been shown that SbV and SFV possess three and four structural proteins, respectively (18, 9). This paper describes experiments in which three species of CHIKV protein have been separated and characterized.