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A Simple Protocol for Platelet-mediated Clumping of Plasmodium falciparum-infected Erythrocytes in a Resource Poor Setting
Published on: May 16, 2013
The Plasmodium vivax MSP1P-19 is involved in binding of reticulocytes through interactions with the membrane proteins
Shenghuan Zuo1, Jiachen Lu1, Yifan Sun2
1Laboratory of Pathogen Infection and Immunity, Department of Clinical Medicine, Wuxi School of Medicine, Jiangnan University, Wuxi, Jiangsu, China.
Abstract:
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.
Insights
Plasmodium vivax merozoite surface protein 1 paralog (PvMSP1P-19) binds reticulocytes. This study identified band3 and CD71 as receptors, crucial for understanding parasite invasion mechanisms.
Area of Science:
- Malariology
- Molecular Parasitology
- Cell Biology
Background:
- Plasmodium vivax preferentially invades reticulocytes.
- The merozoite surface protein 1 paralog (PvMSP1P), specifically the PvMSP1P-19 region, binds reticulocytes.
- The precise molecular interactions during P. vivax invasion remain unclear.
Purpose of the Study:
- To investigate the molecular mechanism of PvMSP1P-19 binding to reticulocytes.
- To identify specific reticulocyte receptors involved in P. vivax invasion.
Main Methods:
- Analysis of PvMSP1P-19 binding to varying reticulocyte concentrations.
- Liquid chromatography-mass spectrometry (LC-MS) to identify interacting proteins.
- Chymotrypsin sensitivity assays.
- In vitro invasion assays using antibodies and recombinant proteins.
Main Results:
- PvMSP1P-19 confirmed reticulocyte preference.
- Band3 and CD71 identified as potential reticulocyte receptors for PvMSP1P-19.
- PvMSP1P-19 and P. cynomolgi MSP1P-19 bind to the extracellular loop 5 of band3.
- Antibodies against band3-P5, CD71, and MSP1P-19 inhibited binding.
- MSP1P-19 proteins inhibited P. falciparum invasion in vitro.
Conclusions:
- Band3 and CD71 are identified as key reticulocyte receptors for PvMSP1P-19.
- Understanding these interactions is vital for developing strategies against P. vivax malaria.
- The study elucidates critical steps in the P. vivax invasion pathway.
