Human papillomavirus type 45 L1 major capsid protein (HPV45 L1)

The Human papillomavirus type 45 L1 major capsid protein is the primary structural component of the HPV-45 virion, a high-risk genotype significantly associated with invasive cervical cancer. The L1 protein self-assembles into 72 pentameric capsomers to form the icosahedral shell of the virus, a process essential for protecting the viral genome and facilitating transmission [Source: UniProt P36740]. Biologically, L1 mediates the initial attachment of the virus to host cells by binding to heparan sulfate proteoglycans on the basement membrane or cell surface, which triggers the endocytic pathway required for infection [Source: PubMed PMID: 24009362]. HPV-45 is particularly noted for its strong association with cervical adenocarcinoma, making its L1 protein a critical target for cancer prevention strategies. In pharmacotherapy, the HPV45 L1 protein is utilized as a recombinant antigen in the nonavalent HPV vaccine (Gardasil 9). The protein is expressed in yeast (Saccharomyces cerevisiae) to form non-infectious virus-like particles (VLPs) that mimic the native virus's structure [Source: FDA Gardasil 9 Label]. These VLPs serve as potent immunogens that stimulate the production of type-specific neutralizing antibodies, providing long-term prophylactic protection against HPV-45 infection and its associated malignancies. While it is not currently a target for small-molecule therapeutics, its role in vaccine-mediated immunity is a cornerstone of global public health efforts to eliminate cervical cancer [Source: National Cancer Institute].

Other names

Major capsid protein L1L1 proteinHPV-45 L1Human papillomavirus 45 L1

Induction of neutralizing antibodies via virus-like particle (VLP) immunization