Abstract
A purified Plasmodium falciparum serine protease (gp76) implicated in erythrocyte invasion, degrades human erythrocyte band 3 and glycophorin A. Inhibition studies using synthetic peptides derived from the presumed band 3 enzymatic cleavage sites and the observed uptake of fluorescent phospholipids following gp76 treatment, suggest that band 3 degradation by this serine protease participates in the formation of the parasitophorous vacuole by restructuring the red cell cytoskeleton. These results provide a rationale for the elaboration of specific inhibitors to block red cell invasion by malaria parasites.
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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Anion Exchange Protein 1, Erythrocyte / metabolism*
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Chymotrypsin / metabolism
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Erythrocytes / parasitology*
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Glycophorins / metabolism
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Humans
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Liposomes / metabolism
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Microscopy, Confocal
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Microscopy, Fluorescence
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Molecular Sequence Data
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Peptides / pharmacology
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Plasmodium falciparum / enzymology*
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Plasmodium falciparum / physiology
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Serine Endopeptidases / metabolism*
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Serine Proteinase Inhibitors / pharmacology
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Vacuoles / metabolism
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Vacuoles / parasitology
Substances
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Anion Exchange Protein 1, Erythrocyte
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Glycophorins
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Liposomes
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Peptides
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Serine Proteinase Inhibitors
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Serine Endopeptidases
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Chymotrypsin