Amino Acid Sequences of Plant and Animal Viral Proteins

Abstract

This chapter will present currently available primary structure data on the proteins of a variety of plant and animal viruses. Excellent descriptions of methods for the determination of amino acid sequences of proteins are found in several review articles and books (Hirs, 1967; Schroeder, 1968; Blackburn, 1970; Needleman, 1970; Starbuck, 1970; Hirs and Timasheff, 1972; Niall, 1973; Perham, 1975) and therefore will not be presented here. Since the pioneering studies on TMV in the early 1960s which contributed to establishing the principle of colinearity of gene and protein, sequencing efforts have contributed to an understanding of evolutionary relationships among other plant and animal viruses. Such data can also provide practical end points such as the design of synthetic vaccines; this may be especially crucial in cases where complete freedom from viral nucleic acids is essential. The continuing development of sensitive automated microsequencing procedures utilizing stepwise Edman degradation, high-sensitivity methods for identification of amino acids, radiolabeled reagents, and proteins with intrinsic radioactivity (Edman and Begg, 1967; Jacobs et al., 1974; McKean et al., 1974; Jacobs and Niall, 1975; Brauer et al., 1975; Oroszlan et al., 1975a; Silver and Hood, 1975; Ballou et al., 1976; Bridgen, 1976; Henning et al., 1976; Vitetta et al., 1976; Zimmerman et al., 1976) will allow data gathering on minor (by mass) virion polypeptides, for example, the reverse transcriptases of retroviruses, which until recently would have required the availability of enormous amounts of virus. The concluding section on retrovirus proteins, the major interest of the authors’ laboratory, will summarize sequence data and recent evidence of viral groupings based on immunological data.