ArticleParasitology research2007
Cryptosporidium parvum: identification and characterization of an acid phosphatase.
Article in Parasitology research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 13 citations in OpenAlex.
- Oxidative stress control by apicomplexan parasites.BioMed research international · 2015Review
- Vacuolar protein sorting receptor in Giardia lamblia.PloS one · 2012Article
- The many roles of NOX2 NADPH oxidase-derived ROS in immunity.Seminars in immunopathology · 2010Review
- Leishmania mexicana promastigotes secrete a protein tyrosine phosphatase.Parasitology research · 2010Article
- Francisella acid phosphatases inactivate the NADPH oxidase in human phagocytes.Journal of immunology (Baltimore, Md. : 1950) · 2010Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acid phosphatases are putative virulence factors in different pathogenic microorganisms. Acid phosphatases can also inhibit the respiratory burst of human neutrophils. In Cryptosporidium parvum, a protozoan parasitic, the study of enzymes is limited. In this paper, we report the presence of a membrane-bound acid phosphatase activity in C. parvum oocysts. The enzymatic activity was inhibited by protein tyrosine phosphatase inhibitors such as sodium orthovanadate, ammonium molybdate, and sodium tungstate and was not affected by protein serine/threonine phosphatase inhibitors such as okadaic acid and calyculin. Antibodies against the catalytic domain of human placental PTPase 1B cross-reacted with two molecules of 30 and 31 kDa present in membrane fraction of a Cryptosporidium oocyst homogenate. This is the first demonstration of acid phosphatase activity in Cryptosporidium.
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Registered trials
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