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Plasmodium vivax Pvs25 is a 25 kDa surface protein expressed during the sexual stages of the Plasmodium vivax parasite, specifically on the surface of zygotes and ookinetes within the mosquito midgut [1, 2]. It is characterized by the presence of four epidermal growth factor (EGF)-like domains, which are essential for the parasite's development and survival during its transition from the human host to the mosquito vector [6, 8]. Pvs25 is a primary target for the development of transmission-blocking vaccines (TBVs), which aim to interrupt the malaria life cycle by preventing the parasite from infecting mosquitoes [4, 7]. When a vaccinated individual is bitten, the ingested antibodies bind to Pvs25 in the mosquito's gut, neutralizing the parasite and preventing the formation of oocysts [1, 11]. While Pvs25 is highly immunogenic in animal models, human clinical trials have faced challenges such as low antibody persistence and reactogenicity when paired with certain adjuvants like Montanide ISA 51 [2, 3]. Despite these hurdles, Pvs25 remains one of the most promising candidates for reducing the global burden of P. vivax malaria through herd immunity and transmission control [5, 6].
Induction of transmission-blocking antibodies that bind to the parasite surface in the mosquito midgut, preventing the transition from zygote to oocyst and blocking further transmission [1, 11].
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