The Plasmodium vivax MSP1P-19 is involved in binding of reticulocytes through interactions with the membrane proteins band3 and CD71.

Autor:	Zuo S; Laboratory of Pathogen Infection and Immunity, Department of Clinical Medicine, Wuxi School of Medicine, Jiangnan University, Wuxi, Jiangsu, China., Lu J; Laboratory of Pathogen Infection and Immunity, Department of Clinical Medicine, Wuxi School of Medicine, Jiangnan University, Wuxi, Jiangsu, China., Sun Y; Laboratory of Pathogen Infection and Immunity, Department of Clinical Medicine, Wuxi School of Medicine, Jiangnan University, Wuxi, Jiangsu, China; Affiliated Hospital of Jiangnan University, Wuxi, Jiangsu, China., Song J; Affiliated Hospital of Jiangnan University, Wuxi, Jiangsu, China., Han S; Laboratory of Pathogen Infection and Immunity, Department of Clinical Medicine, Wuxi School of Medicine, Jiangnan University, Wuxi, Jiangsu, China., Feng X; Laboratory of Pathogen Infection and Immunity, Department of Clinical Medicine, Wuxi School of Medicine, Jiangnan University, Wuxi, Jiangsu, China., Han ET; Department of Medical Environmental Biology and Tropical Medicine, School of Medicine, Kangwon National University, Chuncheon, Gangwon-do, Republic of Korea., Cheng Y; Laboratory of Pathogen Infection and Immunity, Department of Clinical Medicine, Wuxi School of Medicine, Jiangnan University, Wuxi, Jiangsu, China. Electronic address: woerseng@126.com.
Jazyk:	angličtina
Zdroj:	The Journal of biological chemistry [J Biol Chem] 2024 May; Vol. 300 (5), pp. 107285. Date of Electronic Publication: 2024 Apr 16.
DOI:	10.1016/j.jbc.2024.107285
Abstrakt:	The parasite Plasmodium vivax preferentially invades human reticulocytes. Its merozoite surface protein 1 paralog (PvMSP1P), particularly the 19-kDa C-terminal region (PvMSP1P-19), has been shown to bind to reticulocytes, and this binding can be inhibited by antisera obtained by PvMSP1P-19 immunization. The molecular mechanism of interactions between PvMSP1P-19 and reticulocytes during P. vivax invasion, however, remains unclear. In this study, we analyzed the ability of MSP1P-19 to bind to different concentrations of reticulocytes and confirmed its reticulocyte preference. LC-MS analysis was used to identify two potential reticulocyte receptors, band3 and CD71, that interact with MSP1P-19. Both PvMSP1P-19 and its sister taxon Plasmodium cynomolgi MSP1P-19 were found to bind to the extracellular loop (loop 5) of band3, where the interaction of MSP1P-19 with band3 was chymotrypsin sensitive. Antibodies against band3-P5, CD71, and MSP1P-19 reduced the binding activity of PvMSP1P-19 and Plasmodium cynomolgi MSP1P-19 to reticulocytes, while MSP1P-19 proteins inhibited Plasmodium falciparum invasion in vitro in a concentration-dependent manner. To sum up, identification and characterization of the reticulocyte receptor is important for understanding the binding of reticulocytes by MSP1P-19. Competing Interests: Conflict of interest The authors declare no conflicts of interest with the contents of this article. (Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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