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Molecules 2018, 23(5), 1151; https://doi.org/10.3390/molecules23051151

The Double Face of Mucin-Type O-Glycans in Lectin-Mediated Infection and Immunity

1
University Children’s Hospital, Mannheim, Heidelberg University, Theodor-Kutzer-Ufer 1-3, 68167 Mannheim, Germany
2
Schaller Research Group at the University of Heidelberg and the DKFZ, 69120 Heidelberg, Germany
3
Institute of Biochemistry II, Medical Faculty, University of Cologne, Joseph-Stelzmann-Str. 52, 50931 Köln, Germany
These authors contributed equally to the paper.
*
Author to whom correspondence should be addressed.
Received: 26 April 2018 / Revised: 3 May 2018 / Accepted: 7 May 2018 / Published: 11 May 2018
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Abstract

Epithelial human blood group antigens (HBGAs) on O-glycans play roles in pathogen binding and the initiation of infection, while similar structures on secretory mucins exert protective functions. These double-faced features of O-glycans in infection and innate immunity are reviewed based on two instructive examples of bacterial and viral pathogens. Helicobacter pylori represents a class 1 carcinogen in the human stomach. By expressing blood group antigen-binding adhesin (BabA) and LabA adhesins that bind to Lewis-b and LacdiNAc, respectively, H. pylori colocalizes with the mucin MUC5AC in gastric surface epithelia, but not with MUC6, which is cosecreted with trefoil factor family 2 (TFF2) by deep gastric glands. Both components of the glandular secretome are concertedly up-regulated upon infection. While MUC6 expresses GlcNAc-capped glycans as natural antibiotics for H. pylori growth control, TFF2 may function as a probiotic lectin. In viral infection human noroviruses of the GII genogroup interact with HBGAs via their major capsid protein, VP1. HBGAs on human milk oligosaccharides (HMOs) may exert protective functions by binding to the P2 domain pocket on the capsid. We discuss structural details of the P2 carbohydrate-binding pocket in interaction with blood group H/Lewis-b HMOs and fucoidan-derived oligofucoses as effective interactors for the most prevalent norovirus strains, GII.4 and GII.17. View Full-Text
Keywords: human blood group antigens; lectins; adhesins; mucin; MUC6; trefoil factor family 2 (TFF2); norovirus; human milk oligosaccharides; fucoidan human blood group antigens; lectins; adhesins; mucin; MUC6; trefoil factor family 2 (TFF2); norovirus; human milk oligosaccharides; fucoidan
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
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Morozov, V.; Borkowski, J.; Hanisch, F.-G. The Double Face of Mucin-Type O-Glycans in Lectin-Mediated Infection and Immunity. Molecules 2018, 23, 1151.

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