Plasmodium falciparum thrombospondin-related adhesion protein and multi-epitope string (ME-TRAP) (ME-TRAP)

Plasmodium falciparum thrombospondin-related adhesion protein and multi-epitope string (ME-TRAP) is a recombinant vaccine antigen targeting the pre-erythrocytic stage of malaria. The TRAP portion is a type I transmembrane protein localized in the micronemes of sporozoites, where it plays a critical role in gliding motility and hepatocyte invasion by binding to host receptors like heparan sulfate proteoglycans and integrins [2, 10]. The multi-epitope (ME) string is a synthetic construct containing multiple T-cell epitopes from several Plasmodium antigens, including CSP and LSA-1, designed to enhance the breadth of the cellular immune response [3, 12]. ME-TRAP is primarily utilized in viral-vectored vaccine platforms, such as ChAd63 and MVA, administered in a heterologous prime-boost schedule [7, 14]. The mechanism of action involves the induction of high-frequency, antigen-specific CD8+ T cells that recognize and eliminate infected hepatocytes, preventing the development of the symptomatic blood stage of the disease [3, 12]. Clinical trials have demonstrated that ME-TRAP is safe and highly immunogenic, although its protective efficacy has varied across different populations and trial settings [6, 11].

Other names

Thrombospondin-related anonymous proteinPfTRAPME-TRAPMulti-epitope string-thrombospondin-related adhesion proteinThrombospondin-related adhesive protein

Induction of T-cell mediated immunity, specifically CD8+ T cells, to target and eliminate Plasmodium-infected hepatocytes during the pre-erythrocytic stage.