Combining IP₃ affinity chromatography and bioinformatics reveals a novel protein-IP₃ binding site on Plasmodium...

Intracellular Ca²⁺ mobilization induced by second messenger IP₃ controls many cellular events in most of the eukaryotic groups. Despite the increasing evidence of IP₃-induced Ca²⁺ in apicomplexan parasites like Plasmodium, responsible for malaria infection, no protein with potential function as an IP₃-receptor has been identified. The use of bioinformatic analyses based on previously known sequences of IP₃-receptor failed to identify potential IP₃-receptor candidates in any Apicomplexa. In this work, we combine the biochemical approach of an IP₃ affinity chromatography column with bioinformatic meta-analyses to identify potential vital membrane proteins that present binding with IP₃ in Plasmodium falciparum. Our analyses reveal that PF3D7_0523000, a gene that codes a transport protein associated with multidrug resistance as a potential target for IP₃. This work provides a new insight for probing potential candidates for IP₃-receptor in Apicomplexa.