摘要
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.
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.
作者
Fatoumata Gniné Fofana
Ayoub Ksouri
Cheickna Cisse
Oussema Souiai
Alia Benkahla
Hedmon Okella
Mamadou Sangare
Jeffrey G. Shaffer
Seydou Doumbia
Mamadou Wele
Fatoumata Gniné Fofana;Ayoub Ksouri;Cheickna Cisse;Oussema Souiai;Alia Benkahla;Hedmon Okella;Mamadou Sangare;Jeffrey G. Shaffer;Seydou Doumbia;Mamadou Wele(African Center of Excellence in Bioinformatics, University of Sciences, Techniques and Technologies of Bamako (USTTB), Bamako, Mali;Laboratory of BioInformatics BioMathematics, and BioStatistics (BIMS), Institut Pasteur de Tunis, University of Tunis El Manar, Tunis, Tunisia;School of Veterinary Medicine, University of California Davis, Tulare, USA;Department of Biostatistics and Data Science, Tulane University School of Public Health and Tropical Medicine, New Orleans, USA;University Clinical Research Centre (UCRC), USTTB, Bamako, Mali)
