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Permanent link (DOI): https://doi.org/10.7939/R3T14V339

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Affinities of human histo-blood group antigens for norovirus capsid protein complexes Open Access

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Author or creator
Han, Ling
Kitova, Elena N.
Tan, Ming
Jiang, Xi
Pluvinage, Benjamin
Boraston, Alisdair, B.
Klassen, John S.
Additional contributors
Subject/Keyword
Antigen
Electrospray ionization mass spectrometry
Norovirus
Affinities
Type of item
Journal Article (Published)
Language
English
Place
Time
Description
The binding profiles of many human noroviruses (huNoVs) for human histo-blood group antigens have been characterized. However, quantitative-binding data for these important virus–host interactions are lacking. Here, we report on the intrinsic (per binding site) affinities of HBGA oligosaccharides for the huNoV VA387 virus-like particles (VLPs) and the associated subviral P particles measured using electrospray ionization mass spectrometry. The affinities of 13 HBGA oligosaccharides, containing A, B and H epitopes, with variable sizes (disaccharide to tetrasaccharide) and different precursor chain types (types 1, 2, 3, 5 and 6), were measured for the P particle, while the affinities of the A and B trisaccharides and A and B type 6 tetrasaccharides for the VLP were determined. The intrinsic affinities of the HBGA oligosaccharides for the P particle range from 500 to 2300 M−1, while those of the A and B trisaccharides and the A and B type 6 tetrasaccharides for the VLP range from 1000 to 4000 M−1. Comparison of these binding data with those measured previously for the corresponding P dimer reveals that the HBGA oligosaccharides tested exhibit similar intrinsic affinities for the P dimer and P particle. The intrinsic affinities for the VLP are consistently higher than those measured for the P particle, but within a factor of three. While the cause of the subtle differences in HBGA oligosaccharide affinities for the P dimer and P particle and those for the VLP remains unknown, the present data support the use of P dimers or P particles as surrogates to the VLP for huNoV-receptor-binding studies.
Date created
2015
DOI
doi:10.7939/R3T14V339
License information
© 2015 Han, L., Kitova, E. N., Tan, M., Jiang, X., Pluvinage, B., Boraston, A. B., & Klassen, J. S. This version of this article is open access and can be downloaded and shared. The original author(s) and source must be cited.
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Citation for previous publication
Han, L., Kitova, E. N., Tan, M., Jiang, X., Pluvinage, B., Boraston, A. B., & Klassen, J. S. (2015). Affinities of human histo-blood group antigens for norovirus capsid protein complexes. Glycobiology, 25(2), 170-180.  http://doi.org/10.1093/glycob/cwu100

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