Human papillomavirus type 16 L1 capsid protein and E2 regulatory protein (HPV16 L1-E2)

This target represents the functional and structural association between the major capsid protein (L1) and the master regulatory protein (E2) of Human Papillomavirus type 16 (HPV16). L1 is the primary structural component of the viral capsid responsible for host cell surface binding and entry, while E2 is a multifunctional protein that regulates viral DNA replication and transcription by recruiting the E1 helicase to the viral origin (Sanders & Stenlund, 2001; Doorbar et al., 2012). Research has demonstrated a direct physical interaction between L1 and the C-terminal DNA-binding domain of E2, which enhances E2-dependent viral replication and transcription (He et al., 2016). This dual-protein entity is a key focus for 'next-generation' chimeric vaccines designed to provide both prophylactic protection via L1-neutralizing antibodies and therapeutic clearance of existing infections via E2-specific cellular immune responses (Jochmus et al., 1999; ResearchGate, 2007). While L1 is the target of current preventive vaccines like Gardasil, E2 is considered an ideal therapeutic target for early-stage lesions because its expression is often lost during the progression to invasive cancer when the viral genome integrates into the host DNA (MDPI, 2021).

Other names

HPV16 L1-E2 complexHPV16 L1-E2 chimeric proteinHPV16 L1-E2 fusionHuman papillomavirus type 16 L1 and E2

Prevention of viral entry via L1-neutralizing antibodies and induction of T-cell mediated cytotoxicity against E2-expressing infected cells to clear persistent infections.