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The Human papillomavirus (HPV) L1 protein is the major structural component of the viral capsid and serves as the primary target for prophylactic vaccines [1, 2]. This protein has the unique ability to self-assemble into virus-like particles (VLPs) that present highly organized conformational epitopes, which are essential for inducing a protective immune response [4]. HPV types 16 and 18 are high-risk genotypes responsible for approximately 70% of cervical cancers worldwide, while HPV 58 is a high-risk type with significant prevalence in East Asia [3, 6]. Vaccines such as Gardasil 9 and Cervarix utilize recombinant L1 VLPs to elicit high titers of neutralizing antibodies that specifically bind to these conformational epitopes [5]. This binding prevents the virus from attaching to the basement membrane and entering the basal epithelial cells, thereby blocking the initiation of infection [4]. Consequently, targeting these L1 epitopes provides effective protection against HPV-related malignancies, including cervical, vulvar, vaginal, and anal cancers [5].
Induction of neutralizing antibodies that bind to conformational epitopes on the L1 protein, preventing viral attachment to the basement membrane and subsequent entry into host basal epithelial cells [4, 5].
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