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The **L1 major capsid protein of Human papillomavirus type 16** is the principal structural component of the HPV16 virion, forming the majority of the viral capsid and enabling the assembly of stable icosahedral particles. This ~55 kDa protein possesses the ability to spontaneously self-assemble into highly immunogenic virus-like particles (VLPs), which closely mimic the surface of native virions and serve as the primary antigen in current HPV vaccines. The L1 protein mediates essential viral functions, including the encapsidation and stabilization of the viral genome, initial attachment to host cells, and facilitation of viral entry. Its surface-exposed loops contain immunodominant, type-specific epitopes targeted by neutralizing antibodies. Because of its critical structural and antigenic properties, L1 is the foundation for HPV prophylactic vaccine development and is directly relevant to infection biology and HPV-induced cancers
Induction of neutralizing antibodies by presenting conformational epitopes on self-assembled VLPs, thereby conferring protective immunity against HPV infection, and blocking viral entry by antibody-mediated neutralization.
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