Swine
dysentery caused by Brachyspira hyodysenteriae is a disease present worldwide with an important economic impact on the farming business, resulting in an increased use of
antibiotics. In the present study, we investigated the binding of B. hyodysenteriae to
glycosphingolipids from porcine small intestinal epithelium in order to determine the
glycosphingolipids involved in B. hyodysenteriae adhesion. Specific interactions between B. hyodysenteriae and two non-
acid glycosphingolipids were obtained. These binding-active
glycosphingolipids, were characterized by mass spectrometry as
lactotetraosylceramide (Galβ3GlcNAcβ3Galβ4Glcβ1Cer) and the B5
glycosphingolipid (Galα3Galβ4GlcNAcβ3Galβ4Glcβ1Cer). Comparative binding studies using structurally related reference
glycosphingolipids showed that B. hyodysenteriae binding to
lactotetraosylceramide required an unsubstituted terminal Galβ3GlcNAc sequence, while for binding to the B5 pentaosylceramide the terminal Galα3Galβ4GlcNAc sequence is the minimum
element recognized by the bacteria. Binding of Griffonia simplicifolia IB4
lectin to pig colon tissue sections from healthy control pig and B. hyodysenteriae infected pigs showed that in the healthy pigs the Galα3Gal
epitope was mainly present in the lamina propria. In contrast, in four out of five pigs with swine
dysentery there was an increased expression of Galα3Gal in the goblet cells and in the colonic crypts, where B. hyodysenteriae also was present. The one pig that had recovered by the time of necropsy had the Galα3Gal
epitope only in the lamina propria. These data are consistent with a model where a transient increase in the carbohydrate sequence recognized by the bacteria occur in colonic
mucins during B. hyodysenteriae
infection, suggesting that the
mucins may act as decoys contributing to clearance of the
infection. These findings may lead to novel strategies for treatment of B. hyodysenteriae induced swine
dysentery.