Providing valuable knowledge for the design of anti-malaria drugs, Okinawa Institute of Science and Technology Graduate University (OIST) reconstructed the 3D structure of one of the proteins of Plasmodium falciparum, the causative agent of malaria and the antibodies that act as the first line of defence against the parasite.
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Plasmodium falciparum is transmitted to humans by the bite of some species of the Anopheles mosquito. Once inside the human body, the parasite soon reaches the liver where it matures and it is then ready to infect red blood cells, also called erythrocytes.
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One strategy used by the pathogen to amplify its spreading probability is the formation of rosette-shaped clusters of uninfected erythrocytes surrounding a malaria-infected red blood cell. Since the parasite in the central cell of the rosette can easily infect the surrounding cells, the rosette enhances the infection.
One of the key players in the formation of the rosette is the protein PfEMP1, Plasmodium falciparum erythrocyte membrane proteinp PfEMP1 sticks out of the infected red blood cell and deceives one of the first defenses against malaria called the IgM antibodies.
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The technique used by OIST researchers allows them to have a unique dynamic view of the proteins' conformation.
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Having this 3D structural model of the PfEMP1 and IgM complex can help scientists to design anti-malaria pharmacological treatments that can break down or wash out malaria rosettes without hurting the patient.
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The study has been published in Cell Reports.