title: Structural Basis for Norovirus Inhibition by Human Milk Oligosaccharides.
abstract: Histo-blood group antigens (HBGAs) are important binding factors for norovirus infections. We show that two human milk oligosaccharides, 2'-fucosyllactose (2'FL) and 3-fucosyllactose (3FL), could block norovirus from binding to surrogate HBGA samples. We found that 2'FL and 3FL bound at the equivalent HBGA pockets on the norovirus capsid using X-ray crystallography. Our data revealed that 2'FL and 3FL structurally mimic HBGAs. These results suggest that 2'FL and 3FL might act as naturally occurring decoys in humans.
authors.affiliation: Pediatric Infectious Diseases Unit, University Children's Hospital Mannheim, University of Heidelberg, Mannheim, Germany.
authors.forename: Stefan
authors.initials: S
authors.lastname: Weichert
authors.affiliation: Schaller Research Group at the University of Heidelberg and the DKFZ, Heidelberg, Germany.|Department of Infectious Diseases, Virology, University of Heidelberg, Heidelberg, Germany.
authors.forename: Anna
authors.initials: A
authors.lastname: Koromyslova
authors.affiliation: Schaller Research Group at the University of Heidelberg and the DKFZ, Heidelberg, Germany.|Department of Infectious Diseases, Virology, University of Heidelberg, Heidelberg, Germany.
authors.forename: Bishal K
authors.initials: BK
authors.lastname: Singh
authors.affiliation: Pediatric Infectious Diseases Unit, University Children's Hospital Mannheim, University of Heidelberg, Mannheim, Germany.|Schaller Research Group at the University of Heidelberg and the DKFZ, Heidelberg, Germany.
authors.forename: Satoko
authors.initials: S
authors.lastname: Hansman
authors.affiliation: Jennewein Biotechnologie GmbH, Rheinbreitbach, Germany.
authors.forename: Stefan
authors.initials: S
authors.lastname: Jennewein
authors.affiliation: Pediatric Infectious Diseases Unit, University Children's Hospital Mannheim, University of Heidelberg, Mannheim, Germany.
authors.forename: Horst
authors.initials: H
authors.lastname: Schroten
authors.affiliation: Schaller Research Group at the University of Heidelberg and the DKFZ, Heidelberg, Germany g.hansman@dkfz.de.|Department of Infectious Diseases, Virology, University of Heidelberg, Heidelberg, Germany.
authors.forename: Grant S
authors.initials: GS
authors.lastname: Hansman
mesh_terms: D000998:Antiviral Agents / Q000737:chemistry* / Q000494:pharmacology; D001789:Blood Group Antigens / Q000737:chemistry / Q000378:metabolism; D018360:Crystallography, X-Ray; D006801:Humans; D008895:Milk, Human / Q000737:chemistry*; D008958:Models, Molecular; D008968:Molecular Conformation; D029322:Norovirus / Q000187:drug effects*; D009844:Oligosaccharides / Q000737:chemistry* / Q000494:pharmacology; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D013329:Structure-Activity Relationship; D014312:Trisaccharides / Q000737:chemistry / Q000494:pharmacology
chemical_list: D000998:Antiviral Agents; D001789:Blood Group Antigens; D009844:Oligosaccharides; D014312:Trisaccharides; C035714:3'-fucosyllactose; C031420:2'-fucosyllactose