Structural Basis for Norovirus Inhibition by Human Milk Oligosaccharides

Author:

Weichert Stefan1,Koromyslova Anna23,Singh Bishal K.23,Hansman Satoko12,Jennewein Stefan4,Schroten Horst1,Hansman Grant S.23

Affiliation:

1. Pediatric Infectious Diseases Unit, University Children's Hospital Mannheim, University of Heidelberg, Mannheim, Germany

2. Schaller Research Group at the University of Heidelberg and the DKFZ, Heidelberg, Germany

3. Department of Infectious Diseases, Virology, University of Heidelberg, Heidelberg, Germany

4. Jennewein Biotechnologie GmbH, Rheinbreitbach, Germany

Abstract

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.

Funder

Bundesministerium für Bildung und Forschung

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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