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The Human papillomavirus type 31 L1 major capsid protein is the primary structural component of the HPV-31 virus, which is categorized as a high-risk, oncogenic human papillomavirus (UniProt P17388). The L1 protein self-assembles into pentamers (capsomers) that form the icosahedral shell of the virion and plays a critical role in the initial stages of infection by mediating binding to host cell receptors, such as heparan sulfate proteoglycans (PubMed: 25101570). Because HPV-31 is strongly associated with the development of cervical, vulvar, and anal cancers, its L1 protein serves as a vital antigen in prophylactic vaccines (NCI). The recombinant L1 protein, produced as virus-like particles (VLPs), is a core component of the nonavalent HPV vaccine, where it triggers the production of neutralizing antibodies that block viral entry and protect against persistent infection (FDA: Gardasil 9 Label). Prophylactic targeting of this protein has proven highly effective in reducing the global burden of HPV-related malignancies.
Induction of neutralizing antibodies against the L1 protein to prevent viral attachment and entry into host cells.
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