Human papillomavirus type 16 L1 protein assembly interface (HPV16 L1 interface)

The Human papillomavirus type 16 (HPV16) L1 pentamer–pentamer interface is a critical structural site responsible for the assembly and stability of the viral capsid. The L1 protein, the major capsid component, organizes into pentameric units called capsomeres, which then interlock via their C-terminal invading arms to form a stable T=7 icosahedral shell (Modis et al., 2002, EMBO J). This interface involves the docking of the h4 helix from one pentamer into a hydrophobic pocket on an adjacent pentamer, a process essential for protecting the viral genome and facilitating host cell entry (Cardone et al., 2014, J. Virol.). As a therapeutic target, this interface is highly attractive for the development of small-molecule antivirals designed to disrupt capsid assembly or promote premature disassembly. Unlike prophylactic vaccines that induce antibodies against the L1 surface, targeting the assembly interface offers a potential therapeutic strategy for treating existing HPV infections by preventing the production of infectious progeny. Research has identified several experimental small molecules and peptides that occupy these hydrophobic pockets, effectively neutralizing the virus by interfering with its structural integrity (Li et al., 2016, Structure).

Other names

HPV16 L1 pentamer-pentamer contact siteHPV16 L1 inter-pentameric interfaceHPV16 L1 capsomere-capsomere interfaceHPV16 L1 C-terminal arm docking site

Inhibition of viral capsid assembly and stabilization by blocking inter-pentameric protein-protein interactions, leading to the formation of non-infectious or malformed viral particles.