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Major capsid protein L1 of Human papillomavirus type 52 forms the icosahedral outer shell of the virus. L1 self-assembles into pentamers that are arranged to make up the viral capsid, playing a key role in protecting viral genetic material and mediating the initial attachment to host cell surface receptors, facilitating entry via endocytosis. L1 is the principal target for neutralizing antibodies and is the molecular basis for current prophylactic HPV vaccines. Its high immunogenicity and structural mimicry of the native virus enable the formation of effective virus-like particles for vaccine platforms[1][2][5].
Elicitation of neutralizing antibody responses by vaccine-induced L1 virus-like particles
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