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

@inproceedings{Das2015ProcessingOP,
  title={Processing of Plasmodium falciparum Merozoite Surface Protein MSP1 Activates a Spectrin-Binding Function Enabling Parasite Egress from RBCs},
  author={Sujaan Das and Nadine Hertrich and Abigail J. Perrin and Chrislaine Withers-Martinez and Christine R Collins and Matthew L. Jones and Jean M. Watermeyer and Elmar T. Fobes and Stephen R. Martin and Helen R Saibil and Gavin J. Wright and Moritz Treeck and Christian Epp and Michael J. Blackman},
  booktitle={Cell host & microbe},
  year={2015}
}
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 proteolytic maturation by the parasite protease SUB1 just prior to egress. The function of MSP1 and its processing are unknown. Here we show that SUB1-mediated processing of MSP1 is important for parasite… CONTINUE READING
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