Biopolym. Cell. 1988; 4(3):139-144, 150.
Structure and Function of Biopolymers
Hydrodynamic characteristics of the 12S-oligomer of the protein of inclusion bodies of a nuclear polyhedrosis virus of the silkworm (Bombyx mori)
1Lylo V. V., 2Serebryani S. B.
  1. Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukrainian SSR
    Kiev, USSR
  2. Institute of Organic Chemistry, Academy of Sciences of the Ukrainian SSR
    Kiev, USSR


The molecular weight of the polyhedral protein was obtained by two techniques: sedimentation equilibrium (M=333000 Da) and sedimentation-diffusion (M = 344000 Da). Itshyd-rodynamic characteristics (sedimentation constant s020, w = 11.9 S and diffusion constant D020, w = 3.2·10–7 cm2/g) were determined as well. Frictional and axial ratios of protein molecules approximated by ellipsoids of revolution were calculated by the data obtained earlier for the monomer and in this work for the oligomer. Taking account of the protein partial solvation the monomer has a semiaxis ratio of 13 and the oligomer has also an asymmetrical shape with a semiaxis ratio of 4.5. The model of 12 monomer molecules packing in one oligomer molecule, similar to a keratin model, is suggested.


[1] Summers MD, Egawa K. Physical and chemical properties of Trichoplusia ni granulosis virus granulin. J Virol. 1973;12(5):1092-103.
[2] Morgan C, Bergold GH, Moore DH, Rose HM. The macromolecular paracrystalline lattice of insect viral polyhedral bodies demonstrated in ultrathin sections examined in the electron microscope. J Biophys Biochem Cytol. 1955;1(3):187-90.
[3] Hall CE. Measurement of globular protein molecules by electron microscopy. J Biophys Biochem Cytol. 1960;7:613-8.
[4] Bergold GH. Fine structure of some insect viruses. J Insect Pathol. 1963; 5(1):111-128.
[5] Bergold GH. The molecular structure of some insect virus inclusion bodies. J Ultrastruct Res. 1963;8:360-78.
[6] Arnott HJ, Smith KM. An ultrastructural study of the development of a granulosis virus in the cells of the moth Plodia interpunctella (Hbn.). J Ultrastruct Res. 1967;21(3):251-68.
[7] Engstrom A, Kilkson R. Molecular organization in the polyhedra of Porthetria dispar nuclear-polyhedrosis. Exp Cell Res. 1968;53(1):305-10.
[8] Engstrom A. The arrangement of the protein molecules in nuclear-polyhedrosis inclusion. Biochem Exp Biol. 1974; 11(1):7-13.
[9] Summers MD, Arnott HJ. Ultrastructural studies on inclusion formation and virus occlusion in nuclear polyhedrosis and granulosis virus-infected cells of Trichoplusia ni (Hübner). J Ultrastruct Res. 1969;28(5):462-80.
[10] Harrap KA. The structure of nuclear polyhedrosis viruses. I. The inclusion body. Virology. 1972;50(1):114-23.
[11] Hughes KM. The macromolecular lattices of polyhedra. J Invertebr Pathol. 1978; 31(2):217-224.
[12] Chung KL, Brown M, Faulkner P. Studies on the Morphogenesis of Polyhedral Inclusion Bodies of a Baculovirus Autographa Californica NPV. J Gen Virol. 1980; 46(2):335-47.
[13] Bergold G. H. Die Isolierung des Poliedervirus und die Natur der Polieder. Z Naturforsch. 1947; 2b:122-143.
[14] Bergold G. H. Biochemistry of insect viruses. The viruses. Biochemical, biological and biophysical properties. Eds F. M. Burnet, W. M. Stanley. New York : Acad, press, 1959:505-23.
[15] Bergold GH. The nature of nuclear polyhedrosis viruses. Insect pathology. Ed. E A. Steinhaus. New York : Acad, press, 1963. Vol. 1:413-456.
[16] Kozlov EA, Soguliaeva VM, Levitina TL, Vereshchak V, Serebrianyĭ SV. Purification of the polyhedral protein of nuclear polyhedrosis virus of mulberry silkworm and association of the protein in solution. Biokhimiia. 1969;34(4):679-85.
[17] Scott HA, Young SY 3rd, McMasters JA. Isolation and some properties of components of nuclear polyhedra from the cabbage looper, Trichoplusia ni. J Invertebr Pathol. 1971;18(2):177-82.
[18] Longworth JF, Robertson JS, Payne CC. The purification and properties of inclusion body protein of the granulosis virus of Pieris brassicae. J Invertebr Pathol. 1972; 19(1):42-50.
[19] Eppstein DA, Thoma JA. Characterization and serology of the matrix protein from a nuclear-polyhedrosis virus of Trichoplusia ni before and after degradation by an endogenous proteinase. Biochem J. 1977;167(2):321-32.
[20] Rohrmann GF. Characterization of N-polyhedrin of two baculovirus strains pathogenic for Orgyia pseudotsugata. Biochemistry. 1977;16(8):1631-4.
[21] Scharnhorst DW, Weaver RF. Structural analysis of the matrix protein from the nuclear polyhedrosis virus of Heliothis zea. Virology. 1980;102(2):468-72.
[22] Kozlov EA, Lylo VV, Kibirev VK, Serebryaniy SB. Secondary structure and processes of association - dissociation in solutions of protein inclusion bodies nuclear polyhedrosis virus of the silkworm Bombyx mori. Molekulyaranaya biologiy. 1981. Is. 29: 42-48.
[23] 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.
[24] Summers MD, Smith GE. Trichoplusia ni granulosis virus granulin: a phenol-soluble, phosphorylated protein. J Virol. 1975;16(5):1108-16.
[25] Cibulsky RJ, Harper JD, Guolauskas TT. Biochemical comparison of polyhedral protein from five nuclear polyhedrosis viruses infecting plusiine larvae (Lepidoptera: Noctuidae). J Invertebr Pathol. 1977; 29(2):182-91.
[26] 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.
[27] Kozlov E. A., Sidorova N. M., Serebryani S. B. Proteolytic cleavage of polyhedral protein during dissolution of inclusion bodies of the nuclear-polyhedrosis virus of Bombyx mori and Galleria mellonella under alkaline conditions. J Invertebr Pathol. 1975; 25(1):97-101.
[28] 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.
[29] Kozlov EA, Levitina TL, Gusak NM, Ovander MN, Serebryany SB. 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.
[30] Lylo VV, Serebryany SB. Preparation of the inclusion body protein 11S oligomer of the nuclear polyhedrosis virus of the silkworm Bombyx mori. Biokhimiia. 1986; 56(1):45-50.
[31] Elias H. G. Ultrazentrifugen-methoden. Miinchen : Beckman Instruments GmbH, 1961. 232 p.
[32] Cohn EJ, Edsall JT. Proteins, amino acids and peptides. New York : Reinhold publ. co., 1943. 372 p.
[33] Chernyak VYa. Ed. IV Berezin. Study on biopolymers on the analytical ultracentrifuge with photoelectric scanning absorption optical system. Physico-chemical methods molecular biology. Moscow, Mosk Univ press, 1978; 65-95.
[34] Tsvetkov VM, Eskin VE, Frenkel' SYa. Macromolecules structure in solution. Moscow, Nauka, 1964; 719 p.
[35] Bowen TJ, Rowe AJ. An Introduction to Ultracentrifugation. John Wiley & Sons,1970; 171 p.
[36] Chernyak VY, Magretova NN. An "all-speed" autocalibration method for sedimentation equilibrium in dilute homogeneous and multicomponent solutions. I. Theory, a computation scheme, and verification by computer-simulated experiments. Anal Biochem. 1982;123(1):101-9.
[37] Tenford C. Physical chemistry of polymers. Moscow, Khimiya, 1965; 625 p.
[38] Kuntz ID. Hydration of macromolecules. III. Hydration of polypeptides. J Amer Chem Soc. 1971; 93(2):514-516.
[39] Cantor C, Schimmel P. Biophysical Chemistry. Moscow, Mir, 1984; Vol. 2. 315 p.
[40] Crewther WG, Fraser RDB, Lennox FG, Lindley H. The chemistry of keratins. In: Advances in Protein Chemistry . Eds C. B. Anfinsen et al. New York : Acad, press, 1965. Vol. 20:191-346.