Human papillomavirus type 11 regulatory protein E2 (HPV11 E2) (HPV11 E2)

The Human Papillomavirus type 11 (HPV11) regulatory protein E2 is a sequence-specific DNA-binding protein that plays a central role in the viral life cycle [UniProt: P04015]. Its N-terminal transactivation domain (TAD) is critical for viral DNA replication, as it facilitates the recruitment of the E1 helicase to the viral origin of replication through a specific protein-protein interaction (PPI) [PubMed: 10482316]. HPV11 is a low-risk HPV type primarily associated with the development of benign epithelial tumors, such as genital warts (condyloma acuminatum) and recurrent respiratory papillomatosis (RRP) [PubMed: 15140896]. The E1-E2 interaction interface within the TAD is a highly validated therapeutic target, as disrupting this complex prevents the initiation of viral genome replication [PubMed: 12857753]. Small-molecule inhibitors, including indandione and biphenylacetic acid derivatives, have been identified that bind to a deep hydrophobic pocket on the E2 TAD, effectively blocking E1 binding [PubMed: 16118251]. While no drugs targeting this interface are currently FDA-approved, they represent a promising class of antivirals for treating persistent low-risk HPV infections. These inhibitors offer a targeted approach to managing HPV-related diseases by directly interfering with the viral replication machinery rather than relying on non-specific ablative treatments.

Other names

HPV11 E2 transactivation domainHPV11 E2 TADE1-E2 protein-protein interaction interfaceHPV11 E2-E1 interface

Inhibition of the protein-protein interaction between the E1 helicase and the E2 transactivation domain, preventing viral DNA replication.