Merozoite surface protein 8 (MSP‐8) of Plasmodium parasites play an important role in erythrocyte invasion and is a potential malaria vaccine candidate.
Proteins Pfs230 and Pfs48/45 are Plasmodium falciparum transmission-blocking (TB) vaccine candidates that form a membrane-bound protein complex on gametes. The biological role of Pfs230 or the Pfs230-Pfs48/45 complex remains poorly understood. Here, we present the crystal structure of recombinant Pfs230 domain 1 (Pfs230D1M), a 6-cysteine domain, in complex with the Fab fragment of a TB monoclonal antibody (mAb) 4F12. We observed the arrangement of Pfs230 on the surface of macrogametes differed from that on microgametes, and that Pfs230, with no known membrane anchor, may exist on the membrane surface in the absence of Pfs48/45.
We have read the publication of Molina-Franky and colleagues on Plasmodium falciparum pre-erythrocytic stage vaccine development (Malaria Journal, 2020;19:56).
Plasmodium invasion of red blood cells involves malaria proteins, such as reticulocyte-binding protein homolog 5 (RH5), RH5 interacting protein (RIPR), cysteine-rich protective antigen (CyRPA), apical membrane antigen 1 (AMA1) and rhoptry neck protein 2 (RON2), all of which are blood-stage malaria vaccine candidates. So far, vaccines containing AMA1 alone have been unsuccessful in clinical trials.
No abstract available
Malaria is a global health scourge for which a highly effective vaccine remains frustratingly elusive.
Despite appreciable immunogenicity in malaria-naive populations, many candidate malaria vaccines are considerably less immunogenic in malaria-exposed populations. This could reflect induction of immune regulatory mechanisms involving Human Leukocyte Antigen G (HLA-G), regulatory T (Treg), and regulatory B (Breg) cells. Here, we addressed the question whether there is correlation between these immune regulatory pathways and both plasmablast frequencies and vaccine-specific IgG concentrations.
Malaria is a leading cause of death in children; however, developing an effective vaccine has been challenging. Raj et al. now show that Plasmodium falciparum glutamic-acid-rich protein (PfGARP), an 80 kDa antigen expressed on the surface of erythrocytes infected by P. falciparum, is a malaria vaccine candidate for specifically targeting the blood stage of P. falciparum.
Despite ongoing efforts, a highly effective vaccine against Plasmodium falciparum remains elusive. Vaccines targeting the pre-erythrocytic stages of the P. falciparum life cycle are the most advanced to date, affording moderate levels of efficacy in field trials.