, Volume 74, Issue 12, pp 1356-1362
Date: 07 Jan 2010

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

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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.

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.