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Plasmodium falciparum merozoite surface protein 2 (MSP2) is a highly abundant, glycosylphosphatidylinositol (GPI)-anchored protein essential for the survival of the malaria parasite during the blood stage (UniProtKB - P04922). It is characterized by a dimorphic structure, where alleles are classified into either the 3D7-like or the FC27-like family based on their central variable regions (Adda et al., 2009). The FC27-like allele contains unique tandem repeats that are highly immunogenic and serve as a primary target for the host's immune system (McCallum et al., 2008). MSP2 is an intrinsically disordered protein, a feature that likely aids in its role during erythrocyte invasion and immune evasion (Foley et al., 2016). As a major vaccine candidate, it has been included in formulations like the Combination B vaccine, which showed a reduction in parasite density in clinical trials (Genton et al., 2002). However, the extreme polymorphism of the FC27 and 3D7 families presents a significant challenge, as vaccine-induced immunity is often strain-specific (Flueck et al., 2009).
Induction of opsonizing and invasion-inhibiting antibodies that target the merozoite surface to prevent red blood cell entry (Genton et al., 2002).
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