Abstract
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.
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Abbreviations
- aAG:
-
α1-acid glycoprotein
- CPXV:
-
cowpox virus
- Crm:
-
cytokine response modifier
- Fc :
-
constant fragment of immunoglobulin molecule
- LPS:
-
lipopolysaccharide
- LT:
-
lymphotoxin
- mAb:
-
monoclonal antibody
- MPXV:
-
monkeypox virus
- TNF:
-
tumor necrosis factor
- TNFRI(II):
-
tumor necrosis factor receptor type I(II)
- TNFsR:
-
soluble tumor necrosis factor receptor
- VARV:
-
variola virus
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Original Russian Text © I. P. Gileva, T. S. Nepomnyashchikh, I. A. Ryazankin, S. N. Shchelkunov, 2009, published in Biokhimiya, 2009, Vol. 74, No. 12, pp. 1664–1671.
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Gileva, I.P., Nepomnyashchikh, T.S., Ryazankin, I.A. et al. Recombinant TNF-binding protein from variola virus as a novel potential TNF antagonist. Biochemistry Moscow 74, 1356–1362 (2009). https://doi.org/10.1134/S0006297909120098
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DOI: https://doi.org/10.1134/S0006297909120098