Bovine papillomavirus type 1 E6 protein (BPV-1 E6)

The Bovine papillomavirus type 1 (BPV-1) E6 protein is a small, zinc-binding oncoprotein that plays a critical role in the induction of cellular transformation and the maintenance of the viral episome. It is characterized by two zinc-binding domains (CXXC motifs) and functions primarily through protein-protein interactions with host cellular factors. A hallmark of BPV-1 E6 is its high-affinity binding to the focal adhesion protein paxillin, which distinguishes it from high-risk human papillomavirus (HPV) E6 proteins that prioritize p53 degradation (UniProt P03119; PubMed: 9154831). This interaction with paxillin leads to the reorganization of the actin cytoskeleton and contributes to the invasive phenotype of transformed cells. Additionally, BPV-1 E6 interacts with transcriptional co-activators like CBP/p300 to alter host gene expression patterns (PubMed: 10823895). In veterinary medicine, BPV-1 E6 is the primary driver of bovine fibropapillomas and equine sarcoids, making it a significant target for therapeutic intervention (PubMed: 23102587). Current research into targeting BPV-1 E6 involves the development of therapeutic vaccines, siRNA-mediated gene silencing, and peptide-based inhibitors designed to block its interaction with host proteins (PubMed: 15105531).

Other names

BPV1 E6Early protein E6VE6_BPV1

Disruption of E6-paxillin protein-protein interaction and inhibition of viral oncogene expression.