In vitro studies on the selective binding of IgG from different species to tissue sections of the bovine mammary gland.

Tissue sections of the mammary gland of cattle provide a sensitive and reproducible model for studying the initial events of the selective transport of bovine IgGs by the acinar epithelium (AE). Mammary tissue was reacted with purified antibody to horseradish peroxidase (HRP) and exposed to HRP. The sites of peroxidase activity were revealed cytochemically. The highly selective binding of IgGs by AE of the colostrum-forming gland but never of the lactating gland was most notable, whereas IgG1 and IgG2 subclasses and IgM and IgA lacked any binding capacity. An inhibition assay showed that the inhibitory capacity of IgGs was abolished by either alanylation or acetylation, whereas binding of IgGs was blocked by both Fab/c and isolated H-chains, but not by F(ab')2, Fab and Fc. The inhibitory pattern suggests that the region on the IgGs molecule involved in binding to the AE receptor may be located within the CH2 domain. In addition, IgG preparations of human, sheep and rabbit origin were found to be equally efficient in inhibiting the binding of IgGs to AE, whereas no inhibition was obtained with nonmammalian (turtle and chicken) IgG. Similarly, human myeloma proteins of the subclasses IgG1 and IgG3 caused complete inhibition, while IgG2 and IgG4 were inefficient. It is suggested that molecular evolution of IgG within mammalian species is accompanied by the conservation of structures fitting to receptors on the cell surface of different species.