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- Title
gp 58/68, a parasite component that contributes to the escape of the trypomastigote form of <em>T. cruzi</em> from damage by the human alternative complement pathway.
- Authors
Fischer, E.; Ouaissi, M. A.; Velge, P.; Cornette, J.; Kazatchkine, M. D.
- Abstract
A glycoprotein of apparent molecular weight 58,000 (unreduced)/68,000 (in its reduced form) (gp 58/68), which is one of the fibronectin/collagen receptors of Trypanosoma cruzi, was purified to homogeneity from the trypomastigote forms of the Tehuantepec and Y strains of the parasite. Purified gp 58/68 inhibited formation of cell-bound and fluid-phase alternative pathway C3 convertase in a dose-dependent fashion, as assessed using purified human complement components. Gp 58/68 differed from the human regulatory proteins H, DAF, MCP and CR1 and from previously reported regulatory proteins on the parasite membrane in that it was unable to enhance decay dissociation of preformed alternative pathway C3 convertase sites, did not serve as a co-factor for I- mediated cleavage of C3b and had no inhibitory activity on the classical pathway convertases. The inhibitory effect of gp 58/68 was most likely dependent on an interaction of the protein with factor B rather than with C3b. Op 58/68 provides trypomastigotes with an additional potential mechanism for escaping complement lysis by the human alternative pathway.
- Subjects
GLYCOPROTEINS; TRYPANOSOMA cruzi; COMPLEMENT (Immunology); MOLECULAR weights; CELL membranes; COLLAGEN; FLUIDS
- Publication
Immunology, 1988, Vol 65, Issue 2, p299
- ISSN
0019-2805
- Publication type
Article