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Plasmodium falciparum Gametocyte Culture and Mosquito Infection Through Artificial Membrane Feeding
Published on: July 3, 2020
Proteomic analysis of Plasmodium falciparum schizonts reveals heparin-binding merozoite proteins
Yan Zhang1, Ning Jiang, Huijun Lu
1Key Laboratory of Zoonosis, Ministry of Education, Jilin University, Xian Da Lu 5333, Changchun 130062, China.
Abstract:
The malaria parasite Plasmodium falciparum utilizes host glycosaminoglycans (GAGs) as receptors for erythrocyte invasion and intravascular sequestration. Heparin and heparan sulfate (HS) are GAGs which can block erythrocyte invasion of the P. falciparum merozoite, albeit the molecular mechanisms remain poorly understood. Characterization of these heparin-binding merozoite proteins and key ligands in the host-parasite interplay will lead to a better understanding of the mechanism of erythrocyte invasion by malaria parasites. Here, schizont-derived proteins that bind heparin were enriched by affinity chromatography, and 6062 peptides from 811 P. falciparum-derived proteins were identified by two-dimensional liquid chromatography-mass spectrometry (LC/LC-MS/MS). The proteins were categorized into 14 functional groups ranging from pathogenesis, protein catabolic process to signal transduction. Proteins with predominant peptide counts were found to mainly originate from the rhoptry organelle of merozoites and the parasitized erythrocyte membrane. The profile of the heparin/HS-binding proteome of P. falciparum suggests they have important functions in the biology of the parasite.
Insights
Malaria parasites use host glycosaminoglycans (GAGs) to invade red blood cells. Researchers identified key parasite proteins that bind GAGs, offering insights into malaria invasion mechanisms.
Area of Science:
- Parasitology
- Molecular Biology
- Biochemistry
Background:
- Plasmodium falciparum malaria parasites use host glycosaminoglycans (GAGs) for red blood cell invasion and sequestration.
- Heparin and heparan sulfate (HS) are GAGs that inhibit merozoite invasion, but the underlying molecular mechanisms are unclear.
Purpose of the Study:
- To identify and characterize heparin-binding proteins from P. falciparum merozoites.
- To elucidate the molecular mechanisms of host GAGs in blocking parasite invasion.
Main Methods:
- Affinity chromatography was used to enrich schizont-derived proteins that bind heparin.
- Two-dimensional liquid chromatography-mass spectrometry (LC/LC-MS/MS) identified 811 P. falciparum proteins from 6062 peptides.
Main Results:
- Identified proteins were classified into 14 functional groups, including pathogenesis and signal transduction.
- Proteins with high peptide counts were primarily located in merozoite rhoptries and the infected erythrocyte membrane.
- The identified heparin/HS-binding proteome suggests significant roles in parasite biology.
Conclusions:
- The study identified key heparin-binding proteins involved in Plasmodium falciparum invasion.
- Understanding these interactions can lead to new strategies for blocking malaria parasite entry into red blood cells.
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