N-TERMINAL AMINO-ACID-SEQUENCES OF VACCINIA VIRUS STRUCTURAL PROTEINS

The N-terminal amino acid sequences of Vaccinia Virus structural prote ins were determined by direct sequencing following separation of the p roteins of purified intracellular mature virus by SDS-polyacrylamide g els. By comparing the sequences obtained with the published vaccinia v irus DNA sequences, specific open reading frames (ORFs) were identifie d. The structural proteins were encoded by the ORFs of HindIII, A3L (V P57K, 32K), A10L (VP62K, VP28K, VP22K), A12L (VP10K, VP4K), A13L (VP14 K), A14L (VP17-25K), A17L (VP23-29K), A27L (VP13.8K), D8L (VP32K), H3L (VP34-37K), L4R (VP27K), G7L (VPI6K), and 15L (VP13K). Four virus mem brane proteins contained transmembrane signals. The N-termini of prote ins indicated four types of cleavages. Ala-Gly-specific cleavage assoc iated with products of six ORFs. Phe-specific cleavage was found in tw o, Met-specific in three, and Arg-specific in the product of one ORF. Ala-Gly-specific cleavage processes seven core proteins encoded by fiv e ORFs and one membrane protein. The Met- and Arg-specific cleavages a re suggested to be nonessential for virus assembly because the major p ortions of the target membrane proteins remain unaffected. (C) 1994 Ac ademic Press, Inc.