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Major capsid protein L1 of Human papillomavirus type 18 is the principal structural protein forming the icosahedral outer shell of the HPV18 virion, consisting of 72 pentameric capsomers linked by disulfide bonds to create a highly stable viral particle approximately 50 nm in diameter. L1 can self-assemble into virus-like particles (VLPs) in vitro, which, while non-infectious, mimic the native capsid and serve as highly effective immunogens in prophylactic vaccines against HPV infection and HPV-initiated cancers. Each HPV type’s L1 has unique surface loop structures containing epitopes for neutralizing antibody binding, explaining the type-specificity of immune protection. L1 plays a critical role in viral genome protection and intracellular trafficking during infection, and vaccines harness the immunogenicity of recombinant L1 VLPs to prevent HPV transmission and subsequently HPV-related cancer.
Induction of neutralizing antibody response (vaccines with recombinant L1 VLPs stimulate protective immunity via antibody-mediated neutralization); Physical prevention of viral infection (neutralizing antibodies block entry of HPV18 virions into host cells)
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