Processing of Plasmodium falciparum Merozoite Surface Protein MSP1 Activates a Spectrin-Binding Function Enabling Parasite Egress from RBCs

• Published in: Cell host & microbe Vol. 18; no. 4; pp. 433 - 444
• Main Authors: Das, Sujaan, Hertrich, Nadine, Perrin, Abigail J., Withers-Martinez, Chrislaine, Collins, Christine R., Jones, Matthew L., Watermeyer, Jean M., Fobes, Elmar T., Martin, Stephen R., Saibil, Helen R., Wright, Gavin J., Treeck, Moritz, Epp, Christian, Blackman, Michael J.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 14.10.2015; Cell Press
• Subjects: Erythrocytes - parasitology; Host-Pathogen Interactions; Humans; Merozoite Surface Protein 1 - chemistry; Merozoite Surface Protein 1 - metabolism; Merozoites - enzymology; Merozoites - physiology; Models, Biological; Plasmodium falciparum; Plasmodium falciparum - enzymology; Plasmodium falciparum - physiology; Protein Binding; Protein Conformation; Protein Processing, Post-Translational; Proteolysis; Protozoan Proteins - metabolism; Spectrin - metabolism; Subtilisins - metabolism

The malaria parasite Plasmodium falciparum replicates within erythrocytes, producing progeny merozoites that are released from infected cells via a poorly understood process called egress. The most abundant merozoite surface protein, MSP1, is synthesized as a large precursor that undergoes proteolyt...