Human papillomavirus L1 capsid protein (HPV L1) (HPV L1)

The Human papillomavirus (HPV) L1 capsid protein is the primary structural component of the HPV virion, self-assembling into 72 pentameric capsomeres to form an icosahedral shell (UniProt P03101; PubMed PMID: 23550361). This protein is essential for the viral life cycle, as it mediates the initial attachment of the virus to host cell surface receptors, such as heparan sulfate proteoglycans, and facilitates subsequent endocytosis (PubMed PMID: 23550361). The L1 protein contains critical conformational epitopes that are the primary targets for neutralizing antibodies; these epitopes are highly type-specific and are located on the outer surface loops of the protein (UniProt P03101; FDA Gardasil Label). Prophylactic vaccines, such as the quadrivalent Gardasil, utilize recombinant L1 proteins from HPV types 6, 11, 16, and 18 to form non-infectious virus-like particles (VLPs) (CDC HPV Vaccination; FDA Gardasil Label). These VLPs mimic the native virus structure and induce a robust immune response, generating antibodies that block the virus from infecting basal epithelial cells (CDC HPV Vaccination). This prevention is vital because high-risk types 16 and 18 are responsible for the majority of cervical and other anogenital cancers, while types 6 and 11 cause most cases of genital warts (CDC HPV Vaccination; FDA Gardasil Label).

Other names

Major capsid protein L1HPV L1 proteinL1 proteinHPV6 L1HPV11 L1HPV16 L1HPV18 L1

Induction of neutralizing antibodies that bind to conformational epitopes on the L1 protein, preventing viral attachment and entry into host cells.