MOLECULAR STRUCTURE OF ANIMAL VIRUSES AND CELLS BY COMPUTATIONAL ANALYSIS

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Picornaviruses cause disease typified by polio, colds, hepatitis, and foot-and-mouth diseases. Sequences of these viruses have been examined for relationships among them and to other known and hypothetical proteins. Secondary structures of the RNAs have been found to vary with respect to pathological and sequences variances. Adenoviruses are studied with a goal to understanding early events in virus replication wherein the cell's metabolism is subverted to viral functions, and late events during which assembly and morphogenesis occurs. Early viral proteins, whose existence was known from biochemical studies, have been analyzed by comparing their sequences to cellular proteins of known function. Physical association between the viral E3 glycoprotein and cellular MHC proteins correlates with homology between their sequences. Techniques of biochemistry, virology, electron microscopy and computer analysis are used to study picornaviruses and adenoviruses. Analyses of proteins and nucleic acids have been developed and implemented. Graphic representations revealing homology, and reverse complementarity are coupled numerical methods to aid the prediction of secondary structure, splicing, promoters, and recombination in nucleic acid molecules. Programs are developed and installed in a VAX 11/750 system designed for sequence analysis. Structures of up to 2000 bases have been predicted. Methods to assess the significance of predictions use Monte Carlo simulations, evolutionary comparisons and biochemical data. Protein secondary structure is being predicted from amino acid sequences. New sequences are compared with computerized databases to detect relationships with known proteins. Reovirus protein sigma-1 has been found to have a heptapeptide pattern typical of a coiled-coil, alpha-helical structure.