CD226, also known as DNAM-1, is a nectin receptor that contains two extracellular Ig-like domains (CD226-D1 and CD226-D2), and is widely expressed in monocytes, platelets, T cells, and most of the resting NK cells. The interactions between CD226and its nectin/Necl family ligands, CD155 (also known as Necl-5) and CD112 (nectin-2), play important roles in modulating NK cell adhesion and cytotoxicity, facilitating immunological synapse formation and promoting cytokine secretion during inflammation [, , ].
Transmembrane protein PVRIG, also known as CD112 receptor (CD112R), is the cell surface receptor for NECTIN2 (CD antigen CD112). CD112R functions as a coinhibitory receptor for T cells, competing with CD226 to bind to CD112 [].
