Plasmodium falciparum Multiple Epitope-Thrombospondin Related Adhesion Protein (ME-TRAP)

Plasmodium falciparum Multiple Epitope-Thrombospondin Related Adhesion Protein (ME-TRAP) is a synthetic fusion protein designed as a pre-erythrocytic malaria vaccine candidate (PubMed: 15729370). It consists of a Multiple Epitope (ME) string—a sequence of 20 T-cell and B-cell epitopes from various P. falciparum antigens—fused to the full-length Thrombospondin Related Adhesion Protein (TRAP) (PubMed: 24511057). TRAP is a member of the thrombospondin-related anonymous protein family and is essential for sporozoite gliding motility and hepatocyte invasion (UniProt: P17072). By targeting the parasite before it enters the bloodstream, ME-TRAP aims to induce robust CD8+ and CD4+ T-cell responses capable of identifying and destroying infected hepatocytes (PubMed: 26159651). Clinical trials typically utilize viral vectors like Chimpanzee Adenovirus 63 (ChAd63) and Modified Vaccinia virus Ankara (MVA) to deliver the ME-TRAP transgene in a heterologous prime-boost strategy (PubMed: 21364683).

Other names

Thrombospondin-related anonymous proteinTRAPSporozoite surface protein 2SSP2P. falciparum TRAPME-TRAP fusion protein

The mechanism involves the induction of high-frequency, polyfunctional CD8+ and CD4+ T cells that secrete interferon-gamma (IFN-γ) to target and eliminate malaria-infected hepatocytes, alongside the production of antibodies that inhibit sporozoite motility and invasion (PubMed: 24511057, PubMed: 26159651).