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Plasmodium falciparum serine-repeat antigen 5 (SERA5) is a major protein secreted into the parasitophorous vacuole of the malaria parasite during its blood stage (UniProt: P13813). It is synthesized as a 120-126 kDa precursor that undergoes proteolytic processing into smaller fragments, including a 47 kDa N-terminal fragment, during the egress of merozoites (PubMed: 21835794). The SE36 N-terminal region refers to a specific recombinant version of this 47 kDa fragment, modified to remove a polymorphic polyserine loop to improve its utility as a vaccine antigen (PubMed: 15721538). SERA5 is essential for the rupture of the host erythrocyte membrane, making it a critical target for interrupting the parasite's replication cycle (PubMed: 11805230). The SE36 vaccine candidate (BK-SE36) works by eliciting antibodies that bind to the parasite protein and inhibit the egress process or subsequent invasion of new red blood cells (PubMed: 26507885). Clinical studies have shown that individuals with high titers of anti-SE36 antibodies are significantly less likely to experience high-density parasitemia and clinical malaria (PubMed: 12167641). As a therapeutic target, the SE36 region is valued for its relative conservation across different Plasmodium falciparum strains compared to other surface antigens (PubMed: 22942537). Current research focuses on optimizing the formulation of SE36 with various adjuvants to maximize the longevity and strength of the protective immune response (PubMed: 24501304).
Induction of neutralizing antibodies that inhibit the egress of merozoites from infected erythrocytes by interfering with the functional processing of SERA5.
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