Combining IP3 affinity chromatography and bioinformatics reveals a novel protein-IP3 binding site on Plasmodium falciparum MDR1 transporter*

Author(s)

Alves, Eduardo ; Nakaya, Helder ; Guimares, Euzebio ; Garcia, Celia R. S.

• Document type: Journal article
• Source: CURRENT RESEARCH IN MICROBIAL SCIENCES; v. 4, p. 7-pg., 2022-12-19.

Abstract

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. (AU)

• FAPESP's process: 17/08684-7 - Decoding Plasmodium signaling at molecular level as a new tool to the development of new antimalarials
• Grantee: Célia Regina da Silva Garcia
• Support Opportunities: Research Projects - Thematic Grants
• FAPESP's process: 18/14933-2 - Integrative biology applied to human health
• Grantee: Helder Takashi Imoto Nakaya
• Support Opportunities: Research Grants - Young Investigators Grants - Phase 2
• FAPESP's process: 18/07177-7 - EMU concedido no processo 2011/51295-5: image system
• Grantee: Célia Regina da Silva Garcia
• Support Opportunities: Multi-user Equipment Program