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The virion and soluble antigen proteins of variola, monkeypox, and vaccinia viruses
Author(s) -
Esposito Joseph J.,
Obijeski John F.,
Nakano James H.
Publication year - 1977
Publication title -
journal of medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 121
eISSN - 1096-9071
pISSN - 0146-6615
DOI - 10.1002/jmv.1890010203
Subject(s) - monkeypox , vaccinia , virology , poxviridae , virus , orthopoxvirus , variola virus , immunodiffusion , antigen , biology , polyacrylamide gel electrophoresis , cowpox , nucleoprotein , recombinant dna , biochemistry , immunology , gene , enzyme
Abstract The structural proteins in purified preparations of variola, monkeypox, and vaccinia viruses were separated and compared by using a high resolution SDS‐polyacrylamide gel electrophoresis system. About 30 proteins were resolved for each virus by autoradiography of longitudinally‐sliced gel rods. Although the autoradioelectropherograms of each virus were similar, it was possible to differentiate them by their unique protein pattern in the 30,000 to 40,000 molecular weight region of the gels. A single virion glycoprotein (mol. wt. = 38 × 10 3 ) and a virion phosphoprotein (mol. wt. = 12 × 10 3 ) were associated with each of the virus preparations. Cross‐absorbed monospecific immune sera against variola, monkeypox, and vaccinia virus‐infected cells were used in immunodiffusion tests to precipitate radiolabeled, homologous, soluble antigen proteins. The predominant antigen protein associated with each immunospecific precipitate had a molecular weight of approximately 73,000.