FAB-MS characterization of sialyl Lewis x determinants on polylactosamine chains of human airway mucins secreted by patients suffering from cystic fibrosis or chronic bronchitis

Although a large body of structural data exists for bronchial mucins from cystic fibrosis (CF) and chronic bronchitis (CB) patients, little is known about terminal structures carried on poly-N-acetyllactosamine antennae. Such structures are of interest because they are potential ligands for bacterial adhesins and other lectins. In this study, we have used fast atom bombardment mass spectrometry (FAB-MS) to examine terminal sequences released by endo--galactosidase from O-glycans obtained by reductive elimination of bronchial mucins purified from the sputum of 8 CF and 8 CB patients. Our data show that, although the polylactosamine antennae of CF and CB mucins have several terminal sequences in common, they differ significantly in their sialyl Lewis^x (NeuAc2-3Gal1-4Fuc1-3]GlcNAc1-) content. Thus all examined mucins from CF patients carry sialyl Lewis^x on their polylactosamine antennae, whereas this type of epitope is present on only three out of the eight CB mucins examined, notably in the airways of one CB patient which were heavily infected by Pseudomonas aeruginosa as are the airways of all the CF patients. This suggests that, in airway mucins, the expression of sialyl Lewis^x on polylactosamine antennae is probably more related to inflammation and infection than to a direct effect of the CF defect.