Abstract
As the malarial parasite Plasmodium falciparum develops inside the erythrocyte, parasite-derived membrane structures, referred to as Maurer's clefts, play an important role in parasite development by delivering parasite proteins to the host cell surface, and participating in the assembly of the cytoadherence complex, essential for the pathogenesis of cerebral malaria. PfSBP1 is an integral membrane protein of the clefts, interacting with an erythrocyte cytosolic protein, identified here as the human Lantibiotic synthetase component C-like protein LANCL1. LANCL1 is specifically recruited to the surface of Maurer's clefts in P. falciparum mature blood stages. We propose that the interaction between PfSBP1 and LANCL1 is central for late steps of the parasite development to prevent premature rupture of the red blood cell membrane.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Carrier Proteins / metabolism*
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Erythrocyte Membrane / metabolism
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Erythrocytes / metabolism*
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Fluorescent Antibody Technique
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Humans
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Intracellular Membranes / metabolism
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Membrane Proteins / metabolism*
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Molecular Sequence Data
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Molecular Weight
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Peptide Fragments / metabolism
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Plasmodium falciparum / growth & development
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Plasmodium falciparum / metabolism*
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Protein Binding
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Protozoan Proteins / metabolism*
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Receptors, G-Protein-Coupled / chemistry
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Receptors, G-Protein-Coupled / genetics
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Receptors, G-Protein-Coupled / metabolism*
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Recombinant Fusion Proteins / metabolism
Substances
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Carrier Proteins
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LANCL1 protein, human
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Membrane Proteins
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Peptide Fragments
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Pfsbp1 protein, Plasmodium falciparum
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Protozoan Proteins
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Receptors, G-Protein-Coupled
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Recombinant Fusion Proteins