Processing of Plasmodium falciparum Merozoite Surface Protein MSP1 activates a Spectrin-binding function enabling parasite egress from RBCs

Das, S. and Hertrich, N. and Perrin, A.J. and Withers-Martinez, C. and Collins, C.R. and Jones, M.L. and Watermeyer, Jean M. and Fobes, E.T. and Martin, S.R. and Saibil, Helen R. and Wright, G.J. and Treeck, M. and Epp, C. and Blackman, M.J. (2015) Processing of Plasmodium falciparum Merozoite Surface Protein MSP1 activates a Spectrin-binding function enabling parasite egress from RBCs. Cell Host & Microbe 18 (4), pp. 433-444. ISSN 1931-3128.

Abstract

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 viability. Processing modifies the secondary structure of MSP1 and activates its capacity to bind spectrin, a molecular scaffold protein that is the major component of the host erythrocyte cytoskeleton. Parasites expressing an inefficiently processed MSP1 mutant show delayed egress, and merozoites lacking surface-bound MSP1 display a severe egress defect. Our results indicate that interactions between SUB1-processed merozoite surface MSP1 and the spectrin network of the erythrocyte cytoskeleton facilitate host erythrocyte rupture to enable parasite egress.

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