ArticleThe Journal of experimental medicine1994
Functional and antigenic similarities between a 94-kD protein of Schistosoma mansoni (SCIP-1) and human CD59.
Article in The Journal of experimental medicine, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
26 citing papers in PubMed, 78 citations in OpenAlex.
- The grand escape - how pathogens outsmart the human complement system.Immunobiology · 2025Review
- Innate Immune Response to Helminth Infections.Advances in experimental medicine and biology · 2025Review
- Fasciola hepatica is refractory to complement killing by preventing attachment of mannose binding lectin (MBL) and inhibiting MBL-associated serine proteases (MASPs) with serpins.PLoS pathogens · 2022Article
- Schistosome immunomodulators.PLoS pathogens · 2021Review
- Human serum activates the tegument of female schistosomes and supports recovery from Praziquantel.Parasitology research · 2021Article
- Revisiting the Mechanisms of Immune Evasion Employed by Human Parasites.Frontiers in cellular and infection microbiology · 2021Review
- Ancient but Not Forgotten: New Insights Into MPEG1, a Macrophage Perforin-Like Immune Effector.Frontiers in immunology · 2020Review
- Behind Enemy Lines: Immunomodulatory Armamentarium of the Schistosome Parasite.Frontiers in immunology · 2020Review
- Complement Evasion: An Effective Strategy That Parasites Utilize to Survive in the Host.Frontiers in microbiology · 2019Review
- The mystery behind membrane insertion: a review of the complement membrane attack complex.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- PathogenicFrontiers in microbiology · 2017Article
- Streptococcus pneumoniae phosphoglycerate kinase is a novel complement inhibitor affecting the membrane attack complex formation.The Journal of biological chemistry · 2014Article
- New insights into the reaction of Schistosoma mansoni cercaria to the human complement system.Parasitology research · 2014Article
- Article
- On the three-finger protein domain fold and CD59-like proteins in Schistosoma mansoni.PLoS neglected tropical diseases · 2013Article
- Protease-dependent mechanisms of complement evasion by bacterial pathogens.Biological chemistry · 2012Review
- Trichinella spiralis paramyosin binds to C8 and C9 and protects the tissue-dwelling nematode from being attacked by host complement.PLoS neglected tropical diseases · 2011Article
- Enzymatic shaving of the tegument surface of live schistosomes for proteomic analysis: a rational approach to select vaccine candidates.PLoS neglected tropical diseases · 2011Article
- A high-affinity inhibitor of human CD59 enhances complement-mediated virolysis of HIV-1: implications for treatment of HIV-1/AIDS.Journal of immunology (Baltimore, Md. : 1950) · 2010Article
- Immune effector mechanisms against schistosomiasis: looking for a chink in the parasite's armour.Trends in parasitology · 2009Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Schistosomiasis is a parasitic disease affecting approximately 200 million people, primarily in the third world. Schistosoma mansoni, one of the causative agents of this disease, parasitize the human mesenteric and portal blood systems while successfully evading host immune responses. During parasite penetration into the mammalian host and shortly afterwards, the larvae rapidly convert from being sensitive to being resistant to C-mediated killing. Treatment of the C-resistant parasitic forms with trypsin renders the parasite susceptible to C attack, thus indicating the presence of C inhibitory protein(s) on the parasite surface. We describe here an intrinsic schistosome C inhibitory protein (SCIP-1) that exhibits antigenic and functional similarities with the human C-inhibitor CD59. Like CD59, SCIP-1 is capable of inhibiting formation of the C membrane attack complex (MAC), probably by binding to C8 and C9 of the C terminal pathway. In addition, SCIP-1 is apparently also membrane-anchored via glycosyl phosphatidylinositol as it can be specifically released with phosphatidylinositol-specific phospholipase C. Soluble SCIP-1, partially purified from Nonidet P-40 extracts of schistosome tegument is capable of inhibiting hemolysis of sensitized sheep erythrocytes and of rabbit erythrocytes by human C. Anti-human CD59 antibodies block this activity of SCIP-1 and in addition, upon binding to intact parasites, render them vulnerable to killing by human and guinea pig C. SCIP-1 is located on the surface of C-resistant forms of the parasite, i.e., 24-h cultured mechanical schistosomula and in vivo-derived adult worms as revealed by immunofluorescence and immunogold electron microscopy studies. These results identify one of the mechanisms schistosomes use to escape immune attack.
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