Major capsid protein L1 (HPV L1) (HPV L1)

The Human papillomavirus (HPV) L1 capsid protein is the primary structural component of the HPV virion, forming an icosahedral shell that encapsulates and protects the viral genome (UniProt). It plays a vital role in the viral life cycle by mediating the initial attachment of the virus to heparan sulfate proteoglycans on the host cell surface and facilitating subsequent entry via endocytosis (NIH). Due to its high immunogenicity and ability to self-assemble into non-infectious virus-like particles (VLPs), the L1 protein is the central target for prophylactic HPV vaccines (PubMed). These vaccines, such as Gardasil and Cervarix, elicit a robust immune response characterized by the production of neutralizing antibodies that block viral infection (NIH). In clinical diagnostics, the presence or loss of L1 protein expression in cervical cells serves as a significant biomarker for assessing the risk of progression from low-grade lesions to high-grade squamous intraepithelial lesions and invasive cancer (PubMed).

Other names

Human papillomavirus L1 capsid proteinL1 structural proteinLate protein L1HPV L1 protein

Prophylactic vaccines utilize recombinant L1 proteins that self-assemble into virus-like particles (VLPs) to induce the production of high-titer neutralizing antibodies. These antibodies bind to the L1 protein on the surface of the virion, preventing the virus from attaching to heparan sulfate proteoglycans on the host cell basement membrane and subsequently blocking viral entry and infection (NIH, PubMed).