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Significance New drugs targeting multiplePlasmodium parasite life stages are desperately needed to combat malaria drug resistance. The antihistamine clemastine inhibits multiple parasite forms with previously unknown molecular targets. We utilized a parallel chemoproteomic strategy to interrogate the mechanism of action of clemastine based on the global thermal and chemical protein denaturation profiling and found that clemastine binds to and destabilizes the essentialPlasmodium chaperonin TRiC/CCT. Treatment with clemastine affects the levels and morphology of the major TRiC substrate tubulin duringPlasmodium asexual reproduction. Our discovery that clemastine selectively modulatesPlasmodium TRiC over its human counterpart encourages future efforts to target parasite protein folding as a route to malaria control.

Plasmodium chaperonin TRiC/CCT identified as a target of the antihistamine clemastine using parallel chemoproteomic strategy