期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 136, 期 36, 页码 12631-12637出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja505272n
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资金
- Alberta Glycomics Centre
- National Institutes of Health of the Unites States of America
- Alberta Innovates Graduate Student Scholarship
Human noroviruses (NoVs) are known to recognize histo-blood group antigens (HBGAs) as attachment factors. We report the first experimental evidence that sialic acid-containing glycosphingolipids (gangliosides) are also ligands for human NoVs. Electrospray ionization mass spectrometry-based carbohydrate binding measurements performed on assemblies (P dimer, P particle, and virus-like particle) of recombinant viral capsid proteins of two NoV strains, VA387 (GII.4) and VA115 (GI.3), identified binding to the oligosaccharides of mono-, di-, and trisialylated gangliosides. The intrinsic (per binding site) affinities measured for these ligands are similar in magnitude (10(2)103 M1) to those of human HBGAs. Binding of NoV VLPs, P particles, and glutathione S-transferase (GST)-P domain fusion proteins to sialic acid-containing glycoconjugates, observed in enzyme-linked immunosorbent assays, provided additional confirmation of the NoVganglioside interactions.
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