Microneme Protein 5 Regulates the Activity of Toxoplasma Subtilisin 1 by Mimicking a Subtilisin Prodomain *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 287, Issue: 43, Page: 36029-36040
2012
- 22Citations
- 29Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations22
- Citation Indexes22
- 22
- CrossRef15
- Captures29
- Readers29
- 29
Article Description
Toxoplasma gondii is the model parasite of the phylum Apicomplexa, which contains obligate intracellular parasites of medical and veterinary importance. Apicomplexans invade host cells by a multistep process involving the secretion of adhesive microneme protein (MIC) complexes. The subtilisin protease TgSUB1 trims several MICs on the parasite surface to activate gliding motility and host invasion. Although a previous study showed that expression of the secretory protein TgMIC5 suppresses TgSUB1 activity, the mechanism was unknown. Here, we solve the three-dimensional structure of TgMIC5 by nuclear magnetic resonance (NMR), revealing that it mimics a subtilisin prodomain including a flexible C-terminal peptide that may insert into the subtilisin active site. We show that TgMIC5 is an almost 50-fold more potent inhibitor of TgSUB1 activity than the small molecule inhibitor N -[ N -( N -acetyl- l -leucyl)- l -leucyl]- l -norleucine (ALLN). Moreover, we demonstrate that TgMIC5 is retained on the parasite plasma membrane via its physical interaction with the membrane-anchored TgSUB1.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925820625790; http://dx.doi.org/10.1074/jbc.m112.389825; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84867813772&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/22896704; https://linkinghub.elsevier.com/retrieve/pii/S0021925820625790; http://www.jbc.org/lookup/doi/10.1074/jbc.M112.389825; https://syndication.highwire.org/content/doi/10.1074/jbc.M112.389825; https://dx.doi.org/10.1074/jbc.m112.389825
Elsevier BV
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