ArticleThe Journal of cell biology1982
Loss of covalently labeled glycoproteins and glycolipids from the surface of newly transformed schistosomula of Schistosoma mansoni.
Article in The Journal of cell biology, 1982. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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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
16 citing papers in PubMed.
- Can antibody conjugated nanomicelles alter the prospect of antibody targeted therapy against schistosomiasis mansoni?PLoS neglected tropical diseases · 2023Article
- Article
- Pathogenicity of Trichobilharzia spp. for Vertebrates.Journal of parasitology research · 2012Article
- Aberrant receptor-mediated endocytosis of Schistosoma mansoni glycoproteins on host lipoproteins.PLoS medicine · 2006Article
- Schistosome larvae stimulate macrophage cytokine production through TLR4-dependent and -independent pathways.International immunology · 2005Article
- Specific binding of human low-density lipoprotein to the surface of schistosomula of Schistosoma mansoni and ingestion by the parasite.The American journal of pathology · 1991Article
- Characterization of [3H]palmitate- and [3H]ethanolamine-labelled proteins in the multicellular parasitic trematode Schistosoma mansoni.The Biochemical journal · 1988Article
- Human monocyte-derived macrophages are lysed by schistosomula of Schistosoma mansoni and fail to kill the parasite after activation with interferon gamma.The American journal of pathology · 1988Article
- The lateral diffusion of lipid probes in the surface membrane of Schistosoma mansoni.The Journal of cell biology · 1986Article
- Schistosomula of Schistosoma mansoni use lysophosphatidylcholine to lyse adherent human red blood cells and immobilize red cell membrane components.The Journal of cell biology · 1986Article
- Strategies to determine the molecular basis of chemical communication by trematodes.Journal of chemical ecology · 1986Article
- Human erythrocytes adhering to schistosomula of Schistosoma mansoni lyse and fail to transfer membrane components to the parasite.The Journal of cell biology · 1985Article
- The cercarial glycocalyx of Schistosoma mansoni.The Journal of cell biology · 1985Article
- Identification of surface antigens of schistosomula of Schistosoma mansoni recognized by antibodies from mice immunized by chronic infection and by exposure to highly irradiated cercariae.Infection and immunity · 1983Article
- Human neutrophils endocytose multivalent ligands from the surface of schistosomula of Schistosoma mansoni before membrane fusion.The Journal of cell biology · 1982Article
- Modulation of the host's immune response by schistosome larvae.Parasite immunologyReview
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Authors and funding
2 authors.
Funding
Abstract
Schistosomula of Schistosoma mansoni were labeled by oxidation with galactose oxidase or with periodate followed by reduction with NaB3H4 to study the loss of the surface membrane of these parasites in vitro. Grain counts of light microscope autoradiographs (LMARG) of radiolabeled schistosomula show that both galactose oxidase and periodate specifically label the surface of the organisms. Galactose oxidase labels 11 glycoproteins on the surface of skin and mechanical schistosomula, ranging in apparent molecular weight from 17,000 to greater than 105,000. These glycoproteins are lost from the surface of schistosomula with a halftime of 10-15 h in culture in defined medium. Most of these glycoproteins appear to be shed intact from the surface of the schistosomula rather than endocytosed and degraded, because greater than 50% of each of the lost proteins can be recovered by trichloroacetic acid precipitation of the culture medium and because there is no internalization of the radiolabels into cultured schistosomula examined by LMARG. In addition to glycoproteins, periodate labels at least seven glycolipids on the surface of mechanical schistosomula. After culture for 15 h, more than half of each of these periodate-labeled proteins and lipids are lost from the schistosomula, and their abundance relative to each other remains similar to that of freshly labeled organisms. Since both proteins and lipids are lost from the surface of the schistosomula at the same rate, we believe that we are observing a general loss of the parasite surface membrane.
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