Analysis of the Conformation and Function of the Plasmodium falciparum Merozoite Proteins MTRAP and PTRAMP

• DOI: 10.1128/ec.00039-12
• Publication Date: 2012-03-31T03:17:18Z
• Authors: Onyinyechukwu Uchime; Raul Herrera; Karine Reiter; Svetlana Kotova; Richard L. Shimp; Kazutoyo Miura; Dominique Jones; Jacob Lebowitz; Xavier Ambroggio; Darrell E. Hurt; Albert J. Jin; Carole Long; Louis H. Miller; David L. Narum
• Keywords: Microneme; Circumsporozoite protein; Gliding motility

Thrombospondin repeat (TSR)-like domains are structures involved with cell adhesion. Plasmodium falciparum proteins containing TSR play crucial roles in parasite development. In particular, the preerythrocytic P. circumsporozoite protein is hepatocyte invasion. The importance of these two other malaria proteins, merozoite-specific thrombospondin-related anonymous (MTRAP) and apical membrane (PTRAMP), were assessed using near-full-length recombinant composed extracellular produced Escherichia coli. MTRAP thought to be released from invasive organelles identified as micronemes during merozoite invasion mediate motility host through an interaction aldolase, actin binding moving junction. PTRAMP function remains unknown. this study, conformation (rMTRAP) appeared a highly extended (2 nm by 33 nm, width length, respectively), whereas rPTRAMP had less structure. Using erythrocyte assay, rMTRAP but not bound human erythrocytes; was mediated domain. MTRAP- general PTRAMP-specific antibodies failed inhibit development vitro. Altogether, bifunctional that binds receptor motor.