Abstract:
:ICP is a chagasin-family natural tight binding inhibitor of Clan CA, family C1 cysteine peptidases (CPs). We investigated the role of ICP in Trypanosoma brucei by generating bloodstream form ICP-deficient mutants (Deltaicp). A threefold increase in CP activity was detected in lysates of Deltaicp, which was restored to the levels in wild type parasites by re-expression of the gene in the null mutant. Deltaicp 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 Deltaicp, a phenotype that was reversed in the presence of synthetic CP inhibitors. Furthermore, we showed that degradation of anti-VSG IgG is abolished when parasites are pretreated with synthetic CP inhibitors, and that parasites lacking ICP degrade IgG more efficiently than wild type. In addition, Deltaicp reached higher parasitemia than wild type parasites in infected mice, suggesting that ICP modulates parasite infectivity. Taken together, these data suggest that CPs of T. brucei 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.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Santos CC,Coombs GH,Lima AP,Mottram JCdoi
10.1111/j.1365-2958.2007.05970.xsubject
Has Abstractpub_date
2007-11-01 00:00:00pages
991-1002issue
4eissn
0950-382Xissn
1365-2958pii
MMI5970journal_volume
66pub_type
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