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The Major capsid protein L1 of Human papillomavirus type 18 is a ~55 kD structural protein and the principal component of the HPV virion's outer shell. It self-assembles into pentameric capsomers, which further organize into icosahedral capsids with T=7 symmetry, forming virus-like particles (VLPs) in recombinant systems. The L1 protein contains conserved surface loops that mediate type-specific antibody recognition, making it a potent immunogen and the basis for prophylactic HPV vaccines that prevent infections and HPV-related cancers. It is recognized as a prime vaccine antigen since antibodies directed against L1 are highly type-specific and neutralize infection by blocking viral entry into epithelial cells. Structural studies confirm that the L1 protein is highly conserved among different HPV types, with characteristic surface features enabling both virus assembly and vaccine efficacy.
Induction of type-specific neutralizing antibodies via antigenic epitopes in the L1 protein, preventing HPV virion binding and entry into host cells Elicitation of an adaptive immune response directed at the viral capsid surface
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