{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T14:58:20Z","timestamp":1791644300164,"version":"4.3.4"},"reference-count":53,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2007,10,18]],"date-time":"2007-10-18T00:00:00Z","timestamp":1192665600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2007,11]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>ICP is a chagasin\u2010family natural tight binding inhibitor of Clan CA, family C1 cysteine peptidases (CPs). We investigated the role of ICP in <jats:italic>Trypanosoma brucei<\/jats:italic> by generating bloodstream form <jats:italic>ICP<\/jats:italic>\u2010deficient mutants (\u0394<jats:italic>icp<\/jats:italic>). A threefold increase in CP activity was detected in lysates of \u0394<jats:italic>icp<\/jats:italic>, which was restored to the levels in wild type parasites by re\u2010expression of the gene in the null mutant. \u0394<jats:italic>icp<\/jats:italic> displayed slower growth in culture and increased resistance to a trypanocidal synthetic CP inhibitor. More efficient exchange of the variant surface glycoprotein (VSG) to procyclin during differentiation from bloodstream to procyclic form was observed in \u0394<jats:italic>icp<\/jats:italic>, a phenotype that was reversed in the presence of synthetic CP inhibitors. Furthermore, we showed that degradation of anti\u2010VSG IgG is abolished when parasites are pretreated with synthetic CP inhibitors, and that parasites lacking <jats:italic>ICP<\/jats:italic> degrade IgG more efficiently than wild type. In addition, \u0394<jats:italic>icp<\/jats:italic> reached higher parasitemia than wild type parasites in infected mice, suggesting that <jats:italic>ICP<\/jats:italic> modulates parasite infectivity. Taken together, these data suggest that CPs of <jats:italic>T.\u2003brucei<\/jats:italic> bloodstream form play a role in surface coat exchange during differentiation, in the degradation of internalized IgG and in parasite infectivity, and that their function is regulated by ICP.<\/jats:p>","DOI":"10.1111\/j.1365-2958.2007.05970.x","type":"journal-article","created":{"date-parts":[[2007,10,18]],"date-time":"2007-10-18T12:54:10Z","timestamp":1192712050000},"page":"991-1002","source":"Crossref","is-referenced-by-count":30,"title":["Role of the <i>Trypanosoma brucei<\/i> natural cysteine peptidase inhibitor ICP in differentiation and virulence"],"prefix":"10.1111","volume":"66","author":[{"given":"Camila C.","family":"Santos","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Graham H.","family":"Coombs","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana Paula C. 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