Targeting an essential Plasmodium cold shock protein to block growth and transmission of malaria parasite.

Cold shock proteins are characterized by the presence of one or more cold shock domains that bestow them with nucleic acid binding ability. Although cold shock proteins are well characterized in bacteria, plants and humans, there is no information on their existence and role in malaria parasite. Here, we have identified and delineated the function of a cold shock protein of () 'CoSP'. We demonstrate that CoSP exhibits nucleic acid binding properties and regulates gene expression. CoSP promotes microtubule assembly by interacting with α/β tubulin. We identified a human cold shock protein LIN28A inhibitor 'LI71' as a binding partner of CoSP which inhibited CoSP-DNA and α/β tubulin interactions and, also inhibited the development of asexual blood stages and gametocyte stage of malaria parasite. Because CoSP is essential for parasite survival, characterization of its interacting partners may form the basis for development of future anti-malarials.