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The Human papillomavirus type 58 (HPV58) L1 major capsid protein is the primary structural protein of the HPV58 virion, a high-risk genotype significantly associated with cervical cancer, particularly in East Asian populations (Chan et al., 2013, PMID: 23801630). This protein has the intrinsic ability to self-assemble into virus-like particles (VLPs) that are morphologically and immunologically similar to the native virus but lack the infectious viral genome (UniProt P26538). The L1 protein is responsible for binding to host cell receptors, such as heparan sulfate proteoglycans, to facilitate viral entry (PubMed: 25108118). In pharmaceutical applications, HPV58 L1 VLPs are a critical component of the 9-valent HPV vaccine (Gardasil 9), where they serve as the antigen to induce protective neutralizing antibodies (FDA, 2014). These antibodies prevent the virus from infecting host cells, thereby reducing the risk of developing HPV-related precancerous lesions and malignancies. However, L1-targeted vaccines are prophylactic and do not provide therapeutic benefits for individuals already harboring a persistent HPV58 infection. The protein's structure is characterized by a jelly-roll beta-barrel fold, and its assembly into pentamers is essential for the formation of the icosahedral capsid (PubMed: 25108118).
Induction of neutralizing antibodies via virus-like particle (VLP) immunization
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