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Skip to Search Results- 7Norovirus
- 6Carbohydrates
- 6Electrospray ionization mass spectrometry
- 3Mass-spectrometry
- 2Affinities
- 2Affinity
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2015
Boraston, Alisdair, B., Kitova, Elena N., Klassen, John S., Tan, Ming, Pluvinage, Benjamin, Han, Ling, Jiang, Xi
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...
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2015
Tan, Ming, Jiang, Xi, Han, Ling, Kitova, Elena N., Klassen, John S., Boraston, Alisdair, B., Pluvinage, Benjamin
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...
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2013
Klassen, John S., Xia, Ming, Tan, Ming, Wang, Leyi, Han, Ling, Kitova, Elena N., Jiang, Xi, Kitov, Pavel I.
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)...
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2013
Jiang, Xi, Klassen, John S., Kitova, Elena N., Wang, Leyi, Han, Ling, Kitov, Pavel I., Xia, Ming, Tan, Ming
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)...
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Identifying carbohydrate ligands of a norovirus P particle using a catch and release electrospray ionization mass spectrometry assay
Download2014
Jiang, Xi, Kitova, Elena N., Klassen, John S., Tan, Ming, Han, Ling
Noroviruses (NoVs), the major cause of epidemic acute gastroenteritis, recognize human histo-blood group antigens (HBGAs), which are present as free oligosaccharides in bodily fluid or glycolipids and glycoproteins on the surfaces of cells. The subviral P particle formed by the protruding (P)...
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Identifying carbohydrate ligands of a norovirus P particle using a catch and release electrospray ionization mass spectrometry assay
Download2014
Jiang, Xi, Kitova, Elena N., Klassen, John S., Tan, Ming, Han, Ling
Noroviruses (NoVs), the major cause of epidemic acute gastroenteritis, recognize human histo-blood group antigens (HBGAs), which are present as free oligosaccharides in bodily fluid or glycolipids and glycoproteins on the surfaces of cells. The subviral P particle formed by the protruding (P)...
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Quantitative Characterization of Noncovalent Protein-Carbohydrate Interactions using Electrospray Ionization Mass Spectrometry
DownloadFall 2015
The interactions between water-soluble proteins and carbohydrates found on the surfaces of cells play important roles in many physiological and pathological cellular processes. Carbohydrates function as receptors for signaling, cellular recognition and adhesion, and pathogen infections. This...
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Screening carbohydrate libraries for protein interactions using the direct ESI-MS assay: Applications to libraries of unknown concentration
Download2014
El-Hawiet, Amr, Klassen, John S., Kitova, Elena N.
A semiquantitative electrospray ionization mass spectrometry (ESI-MS) binding assay suitable for analyzing mixtures of oligosaccharides, at unknown concentrations, for interactions with target proteins is described. The assay relies on the differences in the ratio of the relative abundances of...
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Screening carbohydrate libraries for protein interactions using the direct ESI-MS assay: Applications to libraries of unknown concentration
Download2014
El-Hawiet, Amr, Klassen, John S., Kitova, Elena N.
A semiquantitative electrospray ionization mass spectrometry (ESI-MS) binding assay suitable for analyzing mixtures of oligosaccharides, at unknown concentrations, for interactions with target proteins is described. The assay relies on the differences in the ratio of the relative abundances of...
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Structure and stability of carbohydrate-lipid interactions: Methylmannose polysaccharide-fatty acid complexes
Download2016
Klassen, John S., Siuda, Iwona, Renaud, Justin, Tieleman, D. Peter, Kitova, Elena N., Liu, Lan, Mayer, Paul M., Richards, Michele R., Lowary, Todd L.
We report a detailed study of the structure and stability of carbohydrate–lipid interactions. Complexes of a methylmannose polysaccharide (MMP) derivative and fatty acids (FAs) served as model systems. The dependence of solution affinities and gas-phase dissociation activation energies (Ea) on FA...