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Permanent link (DOI): https://doi.org/10.7939/R3P84489X

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Affinities of recombinant norovirus P dimers for human blood group antigens Open Access

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Author or creator
Han, Ling
Kitov, Pavel I.
Kitova, Elena N.
Tan, Ming
Wang, Leyi
Xia, Ming
Jiang, Xi
Klassen, John S.
Additional contributors
Subject/Keyword
Norovirus
Electrospray ionization mass spectrometry
Affinity
Histo-blood group antigens
Receptor
Type of item
Journal Article (Published)
Language
English
Place
Time
Description
Noroviruses (NoVs), the major cause of viral acute gastroenteritis, recognize histo-blood group antigens (HBGAs) as receptors or attachment factors. To gain a deeper understanding of the interplay between NoVs and their hosts, the affinities of recombinant P dimers (P2's) of a GII.4 NoV (VA387) to a library of 41 soluble analogs of HBGAs were measured using the direct electrospray ionization mass spectrometry assay. The HBGAs contained the A, B, H and Lewis epitopes, with variable sizes (2–6 residues) and different types (1–6). The results reveal that the P2's exhibit a broad specificity for the HBGAs and bind to all of the oligosaccharides tested. Overall, the affinities are relatively low, ranging from 400 to 3000 M−1 and are influenced by the chain type: 3 > 1 ≈ 2 ≈ 4 ≈ 5 ≈ 6 for H antigens; 6 > 1 ≈ 3 ≈ 4 ≈ 5 > 2 for A antigens; 3 > 1 ≈ 4 ≈ 5 ≈ 6 > 2 for B antigens, but not by chain length. The highest-affinity ligands are B type 3 (3000 ± 300 M−1) and A type 6 (2350 ± 60 M−1). While the higher affinity to the type 3 H antigen was previously observed, preferential binding to the types 6 and 3 antigens with A and B epitopes, respectively, has not been previously reported. A truncated P domain dimer (lacking the C-terminal arginine cluster) exhibits similar binding. The central-binding motifs in the HBGAs were identified by molecular-docking simulations.
Date created
2013
DOI
doi:10.7939/R3P84489X
License information
© 2015 Han, L., Kitov, P. I., Kitova, E. N., Tan, M., Wang, L., Xia, M., Jiang, X., & 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., Kitov, P. I., Kitova, E. N., Tan, M., Wang, L., Xia, M., Jiang, X., & Klassen, J. S. (2013). Affinities of recombinant norovirus P dimers for human blood group antigens. Glycobiology, 23(3), 276-285.  http://doi.org/10.1093/glycob/cws141

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