The Core Protein of Alphaviruses

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Abstract
The primary structure of the core protein of Sindbis virus have been established by protein chemical characterization of peptides derived by enzymatic digestion with trypsin, pepsin and thermolysin and by chemical cleavage with CNBr. The peptide chain consists of 264 amino acids and has the composition Asp8, Asn8, Thr17, Ser12, Glu12, Gln14, Pro28, Gly24, Ala22, Val16, Met10, Ile8, Leu14, Tyr4, Phe9, His6, Lys25, Arg23 and Trp4 and a MW of 29,382. Comparison of this structure with the primary structure of the Semliki-Forest virus core protein revealed several important common characteristics of alphavirus core porteins. The N-terminal halves (1-110) of the proteins are rich in basic amino acids and proline. The C-terminal part (.apprxeq. 110-264/267)is highly conserved: 70% of the amino acid residues are in identical positions. The conserved part contains a possible catalytic center for the presumed protease activity of the core protein. The similarities between the primary structures of both core proteins are reflected in their predicted secondary structures.