Human papillomavirus type 52 L1 capsid protein (HPV52 L1)

The Human papillomavirus type 52 L1 capsid protein (HPV52 L1) is the primary structural component of the HPV52 virion, forming an icosahedral shell that encapsidates the viral genome [4, 18]. It plays a critical role in the viral life cycle by mediating the initial attachment of the virus to heparan sulfate proteoglycans on the host cell surface, triggering conformational changes that facilitate viral entry via endocytosis [4, 6]. HPV52 is classified as a high-risk HPV type, strongly associated with the development of cervical cancer and other anogenital malignancies [1, 5, 20]. In pharmaceutical applications, recombinant HPV52 L1 protein self-assembles into non-infectious virus-like particles (VLPs) that serve as the key antigenic component in prophylactic vaccines such as Gardasil 9 [1, 16]. These vaccines work by inducing the production of type-specific neutralizing antibodies that block the virus from infecting basal epithelial cells [2, 3]. While highly effective at preventing new infections, these L1-targeted vaccines are strictly prophylactic and do not treat established HPV52 infections or existing HPV-related cancers [16, 20]. Monitoring of anti-L1 antibody titers and HPV DNA serves as a biomarker for vaccine efficacy and infection status [7, 11].

Other names

Major capsid protein L1HPV52-L1Major structural protein L1MCP

Induction of neutralizing antibodies that prevent viral attachment and entry into host cells