Were lectins primitive Fc receptors?

Co-operation between humoral and cellular pathways occurs by the interaction of antibody antigen complexes with effector cells. This interaction is mediated by receptors for the Fc region of antibody, Fc receptors (FcR). Molecular characterisation of low-affinity receptors for IgE revealed an 123-amino-acid domain homologous with the carbohydrate-binding domain of the C-type animal lectins. Although IgE is heavily glycosylated, the binding of FcϵRII to IgE was found to be independent of any “lectin-like” activity. The presence on lymphoid cells of a family of adhesion molecules containing a lectin-like domain, the ability of these lectin-like molecules and surface lectins to bind immunoglobulins, and subsequently the role of carbohydrates in the binding of immunoglobulins to such surface molecules imply that the ancestral carbohydrate recognition domain of lectins held together by conserved cystein residues has evolved as FcR to recognise the constant region of immunoglobulins.