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The Human papillomavirus type 18 L1 capsid protein (HPV18 L1) is the primary structural component of the HPV18 virion, a high-risk genotype significantly associated with cervical adenocarcinoma and other mucosal cancers [1]. This protein self-assembles into pentameric capsomers, with 72 capsomers forming the icosahedral shell that encapsulates and protects the viral DNA genome [2]. The L1 protein is critical for the viral life cycle, mediating the initial attachment of the virus to heparan sulfate proteoglycans on the host's basement membrane or cell surface, which is a necessary step for viral entry into basal keratinocytes [3]. As the major surface-exposed protein, L1 is the principal target for neutralizing antibodies and serves as the antigen for recombinant virus-like particle (VLP) vaccines [4]. Prophylactic vaccines, including Gardasil 9 and Cervarix, utilize these VLPs to induce a robust humoral immune response that prevents primary infection by HPV18 [5]. However, targeting the L1 protein is a preventive strategy and does not provide therapeutic clearance of established intracellular infections or pre-existing HPV-related lesions [6].
Induction of neutralizing antibodies that bind to the L1 protein on the surface of the virion, thereby preventing viral attachment to host cell receptors and subsequent entry into basal epithelial cells.
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