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The Human papillomavirus type 16 L1 capsid protein is the major structural protein of the HPV16 virion. It is responsible for forming pentameric capsomers that self-assemble into an icosahedral viral shell with 72 pentamers, resulting in a particle size of about 50 nm in diameter[7][3][1]. L1 encapsulates the viral double-stranded DNA and, together with the minor capsid protein L2, mediates viral entry by binding to host cell surface molecules such as heparan sulfate[4][6]. L1 contains several conformational and linear neutralizing epitopes, critical for immunogenicity and used as antigens in prophylactic HPV vaccines[6][5]. It plays a key role in infection, persistence, and oncogenic risk of HPV16, the most common oncogenic HPV strain linked to cervical and other anogenital cancers[5][1]. The L1 capsid protein is a well-established therapeutic and preventive vaccine target but is not a classical drug target for small molecules or direct pharmacological inhibition[3][7].
Induces neutralizing antibodies that prevent HPV16 infection by blocking viral attachment and entry into host cells Acts as a vaccine antigen, eliciting adaptive immune response
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