Nectin-1 is involved in cell adhesion and synaptogegesis [, , ]. The molecule also serves as a functional receptor for Herpes simplex virus []and other alphaherpesviruses [].Nectins are single-pass type I membrane glycoproteins belonging to the immunoglobulin superfamily. They are characterised by three Ig-like domains (a distal IgV domain and two IgC domains) in the ectodomain, followed by a transmembrane region and a cytoplasmic tail []. Unlike cadherins, nectins are Ca2+-independent cell adhesion molecules that mediate not only homotypic but also heterotypic cell-cell adhesion []. The cytoplasmic tail of nectins possesses a conserved afadin-binding motif, except for nectin-4 which binds the PDZ domain of afadin at its carboxyl terminus. Afadin connects nectins to F-actin and the actin cytoskeleton [, , ].
