CD6 and its ligand activated leukocyte cell adhesion molecule (ALCAM,
CD166) have been detected on various immune cells and in the brain. CD
6-ligand interactions have been implicated in the regulation of T cell
function. ALCAM shares the same extracellular domain organization and
significant sequence homology with the chicken neural adhesion molecu
le BEN. Although ALCAM's CD6 binding site is only partially conserved
in BEN, CD6 specifically binds BEN, albeit with similar to 10-fold low
er avidity than ALCAM. Differences in binding avidity are not detected
when ALCAM and BEN fusion proteins containing the full-length extrace
llular regions are tested. Homotypic interactions between full-length
forms are likely to account for these observations. The identified cro
ss-species interaction between CD6 and BEN suggests that CD6-ligand in
teractions are highly conserved.