Nectin cell adhesion molecule 1 (NECTIN1) (Nectin-1)

Nectin cell adhesion molecule 1 (NECTIN1), also known as PVRL1 or CD111, is a calcium-independent cell-cell adhesion molecule belonging to the immunoglobulin superfamily, primarily located at adherens junctions in epithelial and neuronal tissues [12, 24]. It serves as the principal host cell receptor for the entry of Herpes Simplex Virus types 1 and 2 (HSV-1 and HSV-2) by binding with high affinity to the viral envelope protein Glycoprotein D (gD) [1, 18]. This interaction is a critical step in the viral life cycle, as it triggers the conformational changes in gD necessary to activate the core fusion machinery (gB and gH/gL), facilitating membrane fusion and viral entry [10, 11, 18]. Beyond its role as a viral portal, Nectin-1 is essential for normal tissue architecture and development; mutations in the NECTIN1 gene are linked to cleft lip and palate syndromes, and its dysregulation is associated with the progression and metastasis of various cancers, including hepatocellular carcinoma [21, 24]. Therapeutic efforts targeting the gD/Nectin-1 axis include the development of subunit and mRNA vaccines (e.g., gD2t-AS04, BNT163), neutralizing monoclonal antibodies, and peptidomimetics designed to block viral attachment and spread [2, 3, 6, 7].

Other names

CD111PVRL1HveCHIgRPRR1Poliovirus receptor-related protein 1Herpesvirus entry mediator CNectin-2 (PVRL2)CD112

Inhibition of viral entry by blocking the interaction between Herpes Simplex Virus Glycoprotein D and host Nectin receptors.