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Major capsid protein L1 of Human papillomavirus type 16 (HPV16) is the primary structural protein forming the icosahedral viral capsid, assembling into 72 pentamers interconnected by disulfide bonds, and is essential for virion assembly, infectivity, and antigenicity[1][2][6][7]. The L1 protein self-assembles into virus-like particles (VLPs) that are highly immunogenic and form the basis of current prophylactic HPV vaccines, which prevent HPV infection by eliciting neutralizing antibodies[2][4][5][7]. Sequence variation in the L1 protein affects both viral immune evasion and vaccine efficacy, making it not only a critical vaccine target but also a translational lead for diagnostics and future immunotherapies[4][5]. This protein plays a pivotal role in HPV-mediated oncogenesis, primarily in cervical and other epithelial cancers, and is a major biomarker for HPV exposure and vaccine-induced immunity[4][7].
Induction of neutralizing antibodies via virus-like particles (VLPs); Prevention of viral entry by blocking infection
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