Serine-repeat antigen 5 (SERA5) N-terminal domain (SE36)

Serine-repeat antigen 5 (SERA5) is a major blood-stage protein of Plasmodium falciparum, the primary parasite causing human malaria (UniProt: P13813). It is synthesized as a 120 kDa precursor and processed into several fragments, including a 47 kDa N-terminal domain (P47) and a 50 kDa central domain (PubMed: 11742018). SERA5 is essential for the parasite's life cycle, specifically facilitating the egress of merozoites from infected erythrocytes by participating in the rupture of the parasitophorous vacuole membrane (PubMed: 21835794). The N-terminal domain, particularly the recombinant SE36 fragment, is a prominent vaccine candidate due to its high immunogenicity and relative conservation across different parasite strains (PubMed: 22949513). Antibodies directed against this domain have been shown to inhibit parasite growth in vitro and are associated with naturally acquired immunity in malaria-endemic regions (PubMed: 15722012). Clinical development of the BK-SE36 vaccine has demonstrated that targeting this domain can induce protective immune responses, making it a key focus for malaria prevention strategies (PubMed: 26434775).

Other names

P47SE36Serine-repeat antigen 5 N-terminal fragmentp47 domain of SERA5Serine-rich antigenSERPp126

Induction of neutralizing antibodies that inhibit the egress of merozoites from infected erythrocytes by blocking the functional activity of the SERA5 protein (PubMed: 26434775).