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The Human papillomavirus type 18 L1 major capsid protein forms the main structural component of the HPV virion. It self assembles into pentamers, which further organize into an icosahedral shell comprising 72 pentamers linked by disulfide bonds, giving rise to a particle about 50 nm in diameter. The L1 protein binds viral DNA within the virion and plays a critical role in stabilizing and protecting it during intracellular trafficking after cell entry. As the principal antigenic determinant on the virus surface, conformational epitopes on assembled L1 induce strong neutralizing antibody responses. Recombinant expression of this single viral gene enables formation of virus-like particles (VLPs), which are non-infectious yet immunologically indistinguishable from native virions—this property underlies its use in current prophylactic vaccines against oncogenic HPVs such as types 16 and 18.
Induces production of neutralizing antibodies that prevent infection by blocking virus entry into host cells
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