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Characterization of human norovirus binding to gut-associated bacterial ligands

Authors
  • Almand, Erin A.1, 2
  • Moore, Matthew D.3, 4
  • Jaykus, Lee-Ann1, 3
  • 1 North Carolina State University, Department of Plant and Microbial Biology, Raleigh, NC, 27695, USA , Raleigh (United States)
  • 2 Dean of Faculty, Department of Biology, United States Air Force Academy, CO, 80840, USA , United States Air Force Academy (United States)
  • 3 North Carolina State University, Department of Food, Bioprocessing and Nutrition Sciences, Raleigh, NC, 27695, USA , Raleigh (United States)
  • 4 University of Massachusetts, Department of Food Science, Amherst, MA, 01003, USA , Amherst (United States)
Type
Published Article
Journal
BMC Research Notes
Publisher
Springer (Biomed Central Ltd.)
Publication Date
Sep 23, 2019
Volume
12
Issue
1
Identifiers
DOI: 10.1186/s13104-019-4669-2
Source
Springer Nature
Keywords
License
Green

Abstract

ObjectiveResearch suggests human norovirus binding to histo-blood group antigen (HBGA)-like molecules on enteric bacteria may enhance viral pathogenesis; however, the properties of these bacterial ligands are not well known. Previous work identified, but did not characterize, seven norovirus-binding bacteria. To further examine this bacteria–virus binding interaction, enteric bacteria were analyzed via Western blot with anti-HBGA antibodies and lectins targeting HBGA-associated sugar components. Virus overlay assays using capsids from six different human norovirus strains further identified responsible ligands and strain dependent binding properties.ResultsEach bacterial species possessed varying degrees of HBGA-like activity, and lectin binding further elucidated potential sugar residues involved (N-acetyl-galactosamine, α-d-galactose or α-l-fucose). Both GI and GII norovirus capsids bound specific bacterial ligand sizes, and generally corresponded to anti-HBGA Western blot patterns. A 35-kDa band reacted with all HBGA antibodies, bound all six of the noroviruses tested, and had a high affinity for the lectins. Collectively, this work characterizes the varying carbohydrate residues potentially responsible for norovirus–bacteria interactions and provides a basis for future ligand identification.

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