Recombinant Plasmodium falciparum merozoite surface protein 3 (PfMSP3F) and a 24-kDa fragment from its N terminus (MSP3N) that includes the essential conserved domain, which elicits the maximum antibody (Ab)-dependent cellular inhibition (ADCI), were expressed as soluble proteins in Escherichia coli. Both proteins were found to be stable in both soluble and lyophilized forms.
To explore the mechanism(s) by which IgA may mediate a protective effect, we generated fully human IgA specific for the C-terminal 19-kDa region of Plasmodium falciparum merozoite surface protein 1 (PfMSP119), a major target of protective immune responses.
Plasmodium falciparum, the causative agent of the most severe form of malaria in humans invades erythrocytes using multiple ligand-receptor interactions.
The role of the F1 and F2 domains in erythrocyte invasion and binding was elucidated with mAbs.
Evidence for cross-reactive responses was much stronger when variants within one allele class were tested, which has implications for the rational development of genotype-transcending PfMSP3-based vaccines.
Gathering knowledge about the proteins involved in erythrocyte invasion by Plasmodium merozoites is the starting point for developing new strategies to control malarial disease.
Considering that antigens included in a subunit malaria vaccine should be both accessible to the immune system and lack genetic diversity or have very limited polymorphism, we have analyzed the genetic diversity of three msp genes (msp-7A, msp-7K and msp-10) in different geographical regions of Colombia. The results showed that these genes follow the neutral model of evolution and also display low genetic diversity.
Erythrocyte invasion by the merozoite is an obligatory stage in Plasmodium parasite infection and essential to malaria disease progression.
All the clinical symptoms of malaria result from the invasion of human erythrocytes by the parasite's merozoites.