Human papillomavirus 52 L1 major capsid protein (HPV52 L1)

The Human papillomavirus 52 (HPV52) L1 major capsid protein is the primary structural component of the HPV52 virion, a high-risk oncogenic virus associated with cervical and other anogenital cancers (1.2.1, 1.2.4). It has the unique ability to spontaneously self-assemble into virus-like particles (VLPs) that are morphologically and immunologically indistinguishable from the native virus but lack the viral genome, making them non-infectious (1.3.2, 1.3.4). Biologically, the L1 protein mediates the initial attachment of the virus to heparan sulfate proteoglycans on the surface of host basal keratinocytes, triggering conformational changes that facilitate viral entry via endocytosis (1.4.2, 1.4.3). In the context of pharmacology, the L1 protein is the central antigenic component of prophylactic vaccines, such as the nonavalent Gardasil 9, which induces high titers of neutralizing antibodies to prevent infection (1.2.2, 1.2.3). While highly effective as a preventive measure, L1-targeted vaccines do not provide therapeutic benefits for existing infections or established lesions (1.2.3, 1.3.5). Furthermore, the loss of L1 protein expression in cervical cytology is utilized as a clinical biomarker to predict the progression of low-grade lesions to high-grade cervical intraepithelial neoplasia (1.5.1, 1.5.3).

Other names

L1 proteinMajor capsid proteinLate protein L1HPV52 L1 proteinCapsid protein L1

Induction of neutralizing antibodies that bind to the L1 protein on the viral surface, thereby blocking viral attachment to host cell receptors and preventing entry into host cells.