The beta(1,2)-xylose- and/or alpha(1,3)-fucose-containing cross-reactive carbohydrate determinants (CCDs) are present in various plant and insect N-glycans, and have been attracted as potential antigens in IgE-mediated allergies and immunologically undesired post-translational products on some recombinant therapeutic proteins. By using ELISA and immunoblotting, CCDs-specific IgG and IgE antibodies from some, but not all, of mice and humans were found to fully retain their binding activity after a typical periodate-treatment to CCDs, which did cause the CCDs' antigenic activity to those from the other mice and rabbits to disappear almost completely. Furthermore, the mouse IgE recognizing the periodate-resistant CCDs induced the CCDs/IgE-dependent degranulation of rat basophilic RBL-2H3 cells. These findings indicate that in some cases CCDs include those dependent of the core trisaccharide more strongly than the terminal xylose and fucose, which might have been screened out in the CCDs analyses based on the loss of antibody-binding by the periodate-treatment.