Chapter 27: Epithelial mucins and bacterial adhesion
Published:20 Mar 2014
F. Colomb, C. Robbe-Masselot, S. Groux-Degroote, J. Bouckaert, P. Delannoy, and J. Michalski, in Carbohydrate Chemistry: Chemical and Biological Approaches, Volume 40, ed. A. Pilar Rauter, T. Lindhorst, and Y. Queneau, The Royal Society of Chemistry, 2014, vol. 40, ch. 27, pp. 596-623.
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Mucins are high molecular weight glycoproteins characterized by highly O-glycosylated tandem repeat domains. Mucin-type O-glycans exhibit a variety of terminal sequences including histo-blood group antigens that serve as counter receptors and participate in the adhesion and clearance of numerous bacteria including pathogens. In parallel, the pathological changes of mucin glycosylation modulate bacterial adhesion, often enhancing the adhesion of pathogenic bacteria. This review summarizes the current knowledge on the structure and biosynthesis of epithelial mucin O-glycans chains, the physio-pathological glycosylation repertoire of mucins and the role of mucin glycosylation in bacterial adhesion, focusing on the gastrointestinal tract and airway mucins.