Biochemistry (Moscow)

, Volume 74, Issue 12, pp 1356–1362

Recombinant TNF-binding protein from variola virus as a novel potential TNF antagonist

  • I. P. Gileva
  • T. S. Nepomnyashchikh
  • I. A. Ryazankin
  • S. N. Shchelkunov


Gel-filtration chromatographic separation of the lysate of Sf21 insect cells infected with recombinant baculovirus BVi67 containing the gene for TNF-binding protein (CrmB) of variola virus (VARV) revealed that hTNF-cytotoxicity neutralization activity is associated with a fraction corresponding mainly to high molecular weight proteins (above 500 kDa) and less with fractions corresponding to proteins of 270 or 90 kDa. The recombinant VARV-CrmB protein has been purified by affinity chromatography. Difference in the experimentally determined and estimated (according to amino acid composition) VARV-CrmB molecular weight is due to glycosylation of the recombinant protein expressed in the insect cells. VARV-CrmB neutralizes in vitro the cytotoxic effect of hTNF and hLTα, and its TNF-neutralizing activity is two to three orders of magnitude higher compared to the analogous effects of type I and II soluble TNF receptors, comparable with the activity of mAb MAK195, and somewhat lower than the effect of the commercial drug Remicade.

Key words

tumor necrosis factor TNF-binding protein variola virus viroceptors septic shock 



α1-acid glycoprotein


cowpox virus


cytokine response modifier


constant fragment of immunoglobulin molecule






monoclonal antibody


monkeypox virus


tumor necrosis factor


tumor necrosis factor receptor type I(II)


soluble tumor necrosis factor receptor


variola virus


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Copyright information

© Pleiades Publishing, Ltd. 2009

Authors and Affiliations

  • I. P. Gileva
    • 1
  • T. S. Nepomnyashchikh
    • 1
  • I. A. Ryazankin
    • 1
  • S. N. Shchelkunov
    • 1
  1. 1.FGUN State Research Center of Virology and Biotechnology VectorKoltsovo, Novosibirsk RegionRussia

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