Abstract
Secretory IgA immunoglobulins (sIgA) of human milk play an important role in the protection of infant against intestinal infection. In order to determine the biological role of the sIgAcarbohydrate moiety, particularly in the inhibition of bacterial adhesion on enterocytes in which are involved cell lectins (adhesins), we have undertaken the study of the primary structure of N-and O-glycosidically linked sIgA glycans. The results we obtained show an amazing heterogeneity of glycan structures, some of which are described.
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