TITLE:
Docking of Human Band 3 Anion Transporter Proteins with Their Plasmodium falciparum Interactors Based on Short Linear Motifs
AUTHORS:
Fatoumata Gniné Fofana, Ayoub Ksouri, Cheickna Cisse, Oussema Souiai, Alia Benkahla, Hedmon Okella, Mamadou Sangare, Jeffrey G. Shaffer, Seydou Doumbia, Mamadou Wele
KEYWORDS:
Malaria, Protein-Protein Docking, Protein-Protein Interaction, Short Linear Motifs
JOURNAL NAME:
American Journal of Molecular Biology,
Vol.14 No.4,
August
27,
2024
ABSTRACT: Plasmodium (P.) falciparum is a pathogen that causes severe forms of malaria. Protein interactions have been shown to occur between P. falciparum and human erythrocytes in human blood. The Band 3 Anion Transporter (B3AT) protein is considered the main invasive pathway for the parasite in erythrocytes that causes clinical symptoms for malaria in humans. The interactions between P. falciparum parasites and erythrocytes along this receptor have previously been explored. Short linear motifs (SLIMs) are short linear mediator sequences that involve several biological processes, acting as mediators of protein interactions identifiable by computational tools such as SLiMFinder. For a given protein, the identification of SLIMs allows predicting its interactors. Using the SLIMs approach, protein-protein interaction network analyses between P. falciparum and its human host, were used to identify a tryptophan-rich protein, A5K5E5_PLAVS as an essential interactor of B3AT. To better understand the interaction mechanism, a guided protein-protein docking approach based on SLIM motifs was performed for human B3AT and A5K5E5_PLAVS. The highlights of this important interaction between P. falciparum and its human host have the potential to pave the way to identify new therapeutic candidates.