Biopolym. Cell. 1985; 1(3):121-124.
Structure and Function of Biopolymers
Some physicochemical properties of the protein of inclusion bodies of the Nuclear polyhedrosis and Granulosis viruses of Agrotis segetum
1Kozlov E. A., 1Levitina T. L., 1Gusak N. M., 1Serebryany S. B.
  1. Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR
    Kiev, USSR

Abstract

Dodecylsulphate-polyacrylamide gel electrophoresis has shown that polyhedra and gra-nula of the nuclear polyhedrosis (NPV) and granulosis viruses (GV) of Agrotis sege-ium consist of protein with molecular weight of 28000 and 27500, respectively. Using the dansylation method it was shown that glycine and methionine are N-terminal amino acids of the polyhedral (polyhedrin) and granule (granulin) proteins, respectively. Ami-no acid composition is determined and fingerprints are compiled for the both proteins. According to physicochemical properties granulin of GV and polyhedrin of NPV of the baculoviruses, affecting the same host, differ to a greater extent from polyhedrins of NPV affecting various hosts.

References

[1] Miller L. K. A virus vector for genetic engineering in invertebrates. In: Genetic Engineering in the Plant Sciences Eds. P. Lurquin, A. Kleinhofs. N. Y.: Praeger Publishers, 1981, p. 203-224.
[2] Kozlov E. A., Levitina T. L., Katsman M. S., Gusak N. M., Serebryany S. B. Reconstruction of the polypeptide chain of the inclusion body protein of the silkworm nuclear polyhedrosis virus. Complete amino acid sequence. Russian Journal of Bioorganic Chemistry. 1978; 4(8):1048-1053.
[3] Levitina T. L., Kozlov E. A., Ovander M. N., Serebryany S. B. Tryptic peptides of inclusion body protein in nuclear polyhedrosis virus of Porthetria dispar. Russian Journal of Bioorganic Chemistry. 1981; 7(7):985-995.
[4] Gusak N. M., Kozlov E. A., Ovander M. N., Serebryany S. B. Tryptic peptides of inclusion body protein of nuclear polyhedrosis virus of Galleria mellonella. Russian Journal of Bioorganic Chemistry. 1981; 7(7):996-1007.
[5] Bergold GH. Die isolierung des poliedervirus und die natur der polieder. Z Naturforsch., 1947, 2b:122-143.
[6] Kavsan VM, Katsman MS, Serebriani? SB. [Extraction of polyhedral protein from Borrelinavirus bombycis by treating polyhedrons with acetic acid]. Mikrobiol Zh. 1970;32(3):355-9. Ukrainian.
[7] Meisel D. Fractionation of proteins and nucleic acids, by electrophoresis in polyacrylamide gel. In the book.: Methods of Virology and Molecular Biology, Wiley, 1972:267-293.
[8] Kozlov EA, Levitina TL, Radavskii IuL, Soguliaeva VM, Sidorova NM. Determination of the molecular weight of the protein of the inclusion bodies of the nuclear polyhedrosis virus of the silkworm Bombyx mori. Biokhimiia. 1973;38(5):1015-9.
[9] Weiner AM, Platt T, Weber K. Amino-terminal sequence analysis of proteins purified on a nanomole scale by gel electrophoresis. J Biol Chem. 1972;247(10):3242-51.
[10] Shaw E. Site-specific reagents for chymotrypsin and trypsin. Methods Enzymol. 1967, 11:677-686.
[11] Easley CW. Combinations of specific color reactions useful in the peptide mapping technique. Biochim Biophys Acta. 1965;107(2):386-8.
[12] Ozols J. Amino acid sequence of rabbit liver microsomal cytochrome b5. J Biol Chem. 1970;245(19):4863-74.
[13] Hirs C H W. Determination of cystein as cystic acid. Methods Enzymol., 1967, 11, p. 59-62.
[14] Kozlov EA, Sidorova NM, Serebryani SB. Proteolytic cleavage of polyhedral protein during dissolution of inclusion bodies of the nuclear polyhedrosis viruses of Bombyx mori and Galleria mellonella under alkaline conditions. J Invertebr Pathol. 1975;25(1):97-101.
[15] Eppstein DA, Thoma JA. Alkaline protease associated with the matrix protein of a virus infecting the cabbage looper. Biochem Biophys Res Commun. 1975;62(2):478-84.
[16] Kozlov EA, Levitina TL, Gusak NM, Larionov GV, Veremeichenko SN. Comparative biochemical studies of polyhedral proteins of nuclear polyhedrosis viruses. Biokhimiia. 1978;43(12):2189-95.
[17] Tarasevich LM Kitik VS Relationships viruses and mixed viral infections scoop. In book.: Viruses scoop. Kishinev: Shtiintsa, 1982, p. 35-46.
[18] Kozlov EA, Levitin TL, Husak NM, etc. The possible role of protease inclusion bodies in the baculovirus infection. Molekulyarnaya biologiya, 1982, 31:32-35.
[19] Rohrmann GF, Pearson MN, Bailey TJ, Becker RR, Beaudreau GS. N-Terminal polyhedrin sequences and occluded Baculovirus evolution. J Mol Evol. 1981;17(6):329-33.
[20] Summers MD, Smith GE. Trichoplusia ni granulosis virus granulin: a phenol-soluble, phosphorylated protein. J Virol. 1975;16(5):1108-16.
[21] Kozlov EA, Levitina TL, Sidorova NM, Radavski YL, Serebryani SB. Comparative chemical studies of the polyherdral proteins of the nuclear polyhedrosis viruses of Bombyx mori and Galleria mellonella. J Invertebr Pathol. 1975;25(1):103-7.
[22] Kozlov E. A., Levitina T. L., Gusak N. M., Ovander M. N., Serebryany S. B. Comparison of amino acid sequences of inclusion body proteins of nuclear polyhedrosis viruses of Bombyx mori, Porthetria dispar and Galleria mellonella. Russian Journal of Bioorganic Chemistry. 1981; 7(7):1008-1015.