Post by aqt on Jan 13, 2010 15:50:03 GMT -5
Myxoma Virus
oma...cancer
tumor necrosis factor.....what was in the agro? creates gall in the plants...remember sky?
www.jbc.org/content/271/23/13333.abstract
Abstract
The myxoma virus T2 (M-T2) gene expresses a secreted protein that contains significant sequence similarity to the ligand binding domains of the cellular tumor necrosis factor (TNF) receptors, specifically inhibits the cytolytic activity of rabbit TNFá and is an important virulence factor for myxoma virus infection in rabbits. M-T2 protein was overexpressed from vaccinia virus vectors, purified to apparent homogeneity, and found to specifically protect mouse and rabbit cells from lysis by rabbit TNFá at molar ratios comparable with the soluble versions of the host tumor necrosis factor receptors. M-T2 secreted from virus-infected cells is detected as both a monomer and a disulfide-linked dimer, both of which were shown by Scatchard analysis to bind rabbit TNFá (Kd values of 170 pM and 195 pM, respectively), values that are comparable with the affinities of mammalian TNFs with their receptors. In contrast to the rabbit ligand, M-T2 interacts with mouse TNFá with a much lower affinity, Kd of 1.7 nM, and was unable to inhibit the cytolytic activity of this ligand on mouse cells. Although both monomeric and dimeric forms bound rabbit TNFá with comparable affinity, the dimeric M-T2 protein was a far more potent inhibitor of rabbit TNFá, presumably because it can more effectively prevent dimerization of TNF receptors than can the M-T2 monomer.
aqt
oma...cancer
tumor necrosis factor.....what was in the agro? creates gall in the plants...remember sky?
www.jbc.org/content/271/23/13333.abstract
Abstract
The myxoma virus T2 (M-T2) gene expresses a secreted protein that contains significant sequence similarity to the ligand binding domains of the cellular tumor necrosis factor (TNF) receptors, specifically inhibits the cytolytic activity of rabbit TNFá and is an important virulence factor for myxoma virus infection in rabbits. M-T2 protein was overexpressed from vaccinia virus vectors, purified to apparent homogeneity, and found to specifically protect mouse and rabbit cells from lysis by rabbit TNFá at molar ratios comparable with the soluble versions of the host tumor necrosis factor receptors. M-T2 secreted from virus-infected cells is detected as both a monomer and a disulfide-linked dimer, both of which were shown by Scatchard analysis to bind rabbit TNFá (Kd values of 170 pM and 195 pM, respectively), values that are comparable with the affinities of mammalian TNFs with their receptors. In contrast to the rabbit ligand, M-T2 interacts with mouse TNFá with a much lower affinity, Kd of 1.7 nM, and was unable to inhibit the cytolytic activity of this ligand on mouse cells. Although both monomeric and dimeric forms bound rabbit TNFá with comparable affinity, the dimeric M-T2 protein was a far more potent inhibitor of rabbit TNFá, presumably because it can more effectively prevent dimerization of TNF receptors than can the M-T2 monomer.
aqt