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The Human papillomavirus type 16 (HPV16) L1 protein is the major structural component of the viral capsid, responsible for the assembly of the icosahedral shell that protects the viral genome (UniProt P03101). When recombinantly expressed, L1 proteins spontaneously self-assemble into virus-like particles (VLPs) that are morphologically and immunologically identical to the native virion but lack infectious genetic material (Schiller & Lowy, 2012, Nature Reviews Microbiology). These VLPs serve as the primary antigenic component in prophylactic HPV vaccines, such as Gardasil and Cervarix, which are designed to prevent infections by high-risk HPV types (Harper & DeMars, 2017, Gynecologic Oncology). HPV16 is the most oncogenic genotype, linked to approximately 50% of cervical cancers and a significant portion of oropharyngeal and anogenital malignancies (Burd, 2003, Clinical Microbiology Reviews). The mechanism of action involves the induction of a robust humoral immune response, generating neutralizing antibodies that block the virus from entering basal epithelial cells during initial exposure (Stanley, 2006, Vaccine). While highly effective at preventing new infections, these L1-targeted vaccines do not clear established infections or treat existing HPV-related lesions (Roden & Stern, 2018, Annual Review of Pathology).
Induction of high-titer neutralizing antibodies that bind to the L1 protein on the viral capsid, preventing virion attachment to the basement membrane and subsequent entry into host basal epithelial cells.
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