Thrombospondin-related anonymous protein of Plasmodium falciparum (TRAP)

TRAP is a **key adhesin** and surface protein expressed in *Plasmodium falciparum* sporozoites and is crucial for **malaria parasite motility and host cell invasion**, especially of **human hepatocytes and mosquito salivary glands**[3][4][7]. Structurally, the protein contains both a **von Willebrand factor A (vWA) domain**—which includes a functional MIDAS (metal-ion-dependent adhesion site)—as well as a **thrombospondin type 1 repeat (TSR) domain** important for binding to **heparan sulfate and other sulfated glycoconjugates** on host cells[3][5][7]. TRAP is a **type 1 transmembrane protein**, with its extracellular domains mediating adhesion and its cytoplasmic tail interacting with intracellular motor proteins for gliding motility[1][3][7]. TRAP's **interactions with host kinases** and cell surface molecules are critical for parasite entry, and the protein is a subject of intense study as a **therapeutic and vaccine target** in malaria, with inhibition shown to block infection in vitro and in vivo[2][4][5].

Other names

Thrombospondin-related adhesion protein of Plasmodium falciparumTRAPThrombospondin-related anonymous proteinPfTRAPPlasmodium falciparum TRAP

Drugs/antibodies that inhibit TRAP function block sporozoite adhesion, motility, and invasion by interfering with its adhesive domains or ligand interactions, thereby preventing malaria infection initiation