Thrombospondin-related adhesion protein (TRAP) (TRAP)

Thrombospondin-related adhesion protein (TRAP), also known as SSP2, is a vital transmembrane protein found on the surface of Plasmodium falciparum sporozoites (UniProt: P17072). It is essential for the parasite's gliding motility and the subsequent invasion of human hepatocytes, making it a primary target for pre-erythrocytic malaria vaccines (PubMed: 25535344). The Multiple Epitope-Thrombospondin Related Adhesion Protein (ME-TRAP) is a recombinant antigen construct that links a multi-epitope string—containing B-cell, cytotoxic T-lymphocyte, and T-helper cell epitopes—to the TRAP protein (PubMed: 21422313). This construct is frequently utilized in viral vector-based vaccine platforms, such as ChAd63 and MVA, to induce potent cellular immunity (ClinicalTrials.gov: NCT01623570). The mechanism involves priming the immune system to recognize and eliminate sporozoites or infected liver cells via CD8+ T-cell-mediated responses before the parasite enters the bloodstream. While ME-TRAP vaccines have shown high immunogenicity and a favorable safety profile in clinical trials, they are often evaluated in combination with other antigens to enhance protective efficacy against malaria infection (PubMed: 24106147).

Other names

Multiple Epitope-Thrombospondin Related Adhesion ProteinME-TRAPSporozoite surface protein 2SSP2PfTRAP

Induction of antigen-specific cellular immune responses, specifically CD8+ and CD4+ T-cell mediated immunity, to target and eliminate malaria sporozoites and infected hepatocytes during the pre-erythrocytic stage (PubMed: 21422313).