Nectin-2, also known as CD112, is a cell adhesion molecule that belongs to the Nectin family. Nectin is highly homologous to human poliovirus receptors and also known as a poliovirus receptor-associated protein. The Nectin family consists of four members: Nectin-1, Nectin-2, Nectin-3, and Nectin-4. Nectin protein had three consecutive immunoglobulin-like domains outside the cell, namely, the Ig-V domain at the N terminal and two Ig-C2 domains at the C terminal. Nectin-2 is found in neurons, endothelial cells, epithelial cells, and fibroblasts. Nectin-2 can bind pseudorabies virus and herpes simplex virus-2 (HSV-2) and participate in the intercellular transmission of these viruses, but cannot bind HSV-1 and has a low binding affinity with TIGIT. Nectin-2 was identified as a ligand for DNAM-1 (CD226), whose CD226/CD112 interaction mediates cytotoxicity and cytokine secretion in T and NK cells.
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