Role of the Trypanosoma brucei natural cysteine peptidase inhibitor ICP in differentiation and virulence.

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 Microbiol

journal_title

Molecular microbiology

authors

Santos CC,Coombs GH,Lima AP,Mottram JC

doi

10.1111/j.1365-2958.2007.05970.x

subject

Has Abstract

pub_date

2007-11-01 00:00:00

pages

991-1002

issue

4

eissn

0950-382X

issn

1365-2958

pii

MMI5970

journal_volume

66

pub_type

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