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The Plasmodium vivax circumsporozoite protein (PvCSP) is the most abundant surface protein on the sporozoite stage of the malaria parasite and is essential for its life cycle [1, 2]. It facilitates sporozoite development within the mosquito oocyst and enables migration to the salivary glands, as well as subsequent motility within the human dermis and invasion of host hepatocytes [4, 5]. The protein's structure includes a central repetitive region flanked by conserved N-terminal and C-terminal domains, which mediate binding to heparan sulfate proteoglycans on liver cells [2, 4]. PvCSP is a primary target for the development of pre-erythrocytic vaccines, which aim to induce protective antibodies that block the parasite's entry into the liver [6, 8]. Successful immunization against PvCSP could potentially prevent both the primary blood-stage infection and the formation of dormant hypnozoites, which are responsible for malaria relapses [2, 13]. However, the high degree of genetic polymorphism among P. vivax strains, particularly in the central repeat regions (variants VK210 and VK247), remains a significant challenge for achieving broad and lasting vaccine efficacy [1, 5, 11].
Induction of neutralizing antibodies that bind to the central repeat region and functional domains of PvCSP to block sporozoite motility and prevent hepatocyte invasion [2, 3, 8, 14].
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