Poliovirus receptor-related 1 (Nectin-1)

Poliovirus receptor-related 1 (Nectin-1, CD111, PVRL1) is a membrane protein and a member of the immunoglobulin superfamily of cell adhesion molecules, characterized by three extracellular immunoglobulin-like domains, a single transmembrane segment, and a cytoplasmic tail that binds the scaffolding protein afadin[6][2][7][8]. Nectin-1 localizes to adherens junctions in epithelial tissues and is crucial for the formation and maintenance of synapses in neural tissue[6][4][2][3]. It mediates both homophilic (Nectin-1/Nectin-1) and heterophilic (Nectin-1/Nectin-3) interactions, impacting tissue organization and signaling. Nectin-1 is the major entry receptor for Herpes simplex viruses and related alphaherpesviruses, as binding of viral glycoprotein D to Nectin-1 is essential for infection initiation[1][7][5]. Disruption or genetic variants in Nectin-1 are implicated in neurological and developmental disorders as well as serving as a potential cancer cell adhesion modulator. There are currently no approved drugs targeting Nectin-1 directly for therapeutic purposes.

Other names

Nectin-1CD111PVRL1Herpesvirus entry mediator C (HVEC)

Acts as a viral entry receptor: Herpes simplex virus glycoprotein D binds Nectin-1, facilitating viral entry into host cells[1][6][7]