Human papillomavirus L1 capsid protein (high-risk non-vaccine types) (HPV L1)

The L1 capsid protein is the primary structural component of the Human Papillomavirus (HPV) virion, forming an icosahedral shell that protects the viral genome (Source: NIH/NCI). It plays a critical role in the viral life cycle by mediating attachment to host cell surface receptors, such as heparan sulfate proteoglycans, which is essential for viral entry into basal epithelial cells (Source: PubMed, PMID: 25103078). High-risk HPV types are the established causative agents of cervical cancer and other anogenital and oropharyngeal malignancies (Source: WHO). While current 9-valent vaccines (e.g., Gardasil 9) provide protection against the most prevalent high-risk types, they do not cover all oncogenic variants, such as HPV 35, 39, 51, 56, 59, 66, and 68 (Source: CDC). These non-vaccine high-risk types contribute to approximately 10-15% of cervical cancer cases globally, with certain types like HPV 35 showing higher prevalence in specific populations (Source: PubMed, PMID: 31536127). Prophylactic strategies targeting the L1 proteins of these additional types involve the development of expanded multi-valent virus-like particle (VLP) vaccines designed to induce potent neutralizing antibody responses (Source: PubMed, PMID: 30135565). By blocking the initial infection stage, these vaccines aim to provide comprehensive protection against the full spectrum of oncogenic HPV types.

Other names

Major capsid protein L1HPV L1 proteinL1 structural proteinVirus-like particle L1Late protein 1

Induction of type-specific neutralizing antibodies that bind to the L1 protein on the virion surface, sterically hindering the virus from interacting with host cell receptors (e.g., heparan sulfate proteoglycans) and preventing viral internalization into basal epithelial cells (Source: NIH/NCI, PubMed, PMID: 25103078).