Combining IP3affinity chromatography and bioinformatics reveals a novel protein-IP3binding site onPlasmodium falciparumMDR1 transporter Article Swipe
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· 2021
· Open Access
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· DOI: https://doi.org/10.1101/2021.03.25.437059
· OA: W3136984653
Intracellular Ca 2+ mobilization induced by second messenger IP 3 controls many cellular events in most of the eukaryotic groups. Despite the increasing evidence of IP 3 -induced Ca 2+ in apicomplexan parasites like Plasmodium , responsible for malaria infection, no protein with potential function as an IP 3 -receptor has been identified. The use of bioinformatic analyses based on previously known sequences of IP 3 -receptor failed to identify potential IP 3 -receptor candidates in any Apicomplexa . In this work, we combine the biochemical approach of an IP 3 affinity chromatography column with bioinformatic meta-analyses to identified potential vital membrane proteins that present binding with IP 3 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 IP 3 . This work provides a new insight for probing potential candidates for IP 3 -receptor in Apicomplexa .
