Immunohistochemical identification and crossreactions of amyloid-A fibril protein in man and eleven other species.

Antisera were prepared in rabbits, sheep or chicken against purified amyloid fibril protein AA from man, mouse, stone marten, dog, cow and hamster. These antisera were tested by immunodiffusion against all purified antigens and applied to tissue sections containing amyloid from man, mouse, hamster, guinea pig, rabbit, cat, dog, mink, stone marten, pine marten, cow and horse. The binding of the antibodies to amyloid in tissue sections was assessed by the indirect immunoperoxidase method. The strongest reactions in the immunodiffusion and immunohistochemical methods were found between amyloid deposits of members of a given species and an antibody raised against protein AA from the same species. In contrast to the lack of cross-reactivity in immunodiffusion (except in the mouse-man relationship), extensive cross-reactions were observed immunohistochemically in phylogenetically related species, e.g. between stone marten, pine marten and mink, or between hamster and mouse. However, cross-reactions were also observed in combinations such as man-mouse, man-dog, man-cat, mouse-horse, and dog-cow. In addition, individual antisera showed variations in immunohistochemical reactivity with amyloid deposits of different members of one given species. Moreover, antisera prepared in rabbits reacted more restrictedly than those prepared in sheep, while rabbit antisera against any AA-protein did not react with rabbit amyloid. Finally, the widest degree of cross-reactivity including almost all mammalian species investigated was observed with a chicken antiserum to human amyloid AA protein.