Human papillomavirus E1–E2 protein interaction

The **E1–E2 protein interaction** of human papillomavirus is critical for the initiation of viral DNA replication. E2 acts to recruit E1, the viral DNA helicase, to the viral origin of replication; their stable interaction is necessary to form the preinitiation complex that supports subsequent recruitment of cellular DNA replication machinery[1][2][3][6]. Both domains of E2—the transactivation and DNA-binding domains—can interact with E1. Disruption of this interaction abrogates HPV genome replication. Experimental small molecules have been developed to inhibit this protein-protein interaction, but these compounds are specific to certain HPV types and are not broadly effective due to sequence diversity in E1 and E2 among HPVs[2][3]. This interaction is a research tool and a proof-of-concept antiviral target but is not currently the basis of any approved therapeutic.[2][3] **Note on is_incorrect:** Although this is a validated protein-protein interaction of high biological importance, "Human papillomavirus E1–E2 protein interaction" is *not* a classical standalone molecular target such as a receptor, enzyme, ion channel, or transporter. Instead, it is a specific interaction interface between two viral proteins; thus, the concept as a "target" is valid for drug discovery in some experimental contexts but does not match standard naming conventions for molecular targets. If you require a classical target, "Human papillomavirus E1 protein" and/or "Human papillomavirus E2 protein" could be considered individually.

Other names

HPV E1–E2 interactionPapillomavirus E1–E2 complexE1-E2 interface

Inhibition of E1–E2 interaction blocks assembly of the replication complex and prevents viral DNA synthesis