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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...

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...

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)...

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)...

2011

Dingle, Tanis C., Szpacenko, Adam, Ng, Kenneth K.S., Kitov, Pavel, Klassen, John S., El-Hawiet, Amr, Kitova,Elena N., Mulvey, George L., Eugenio, Luiz, Armstrong, Glen D.

The binding of recombinant fragments of the C-terminal cell-binding domains of the two large exotoxins, toxin A (TcdA) and toxin B (TcdB), expressed by Clostridium difficile and a library consisting of the most abundant neutral and acidic human milk oligosaccharides (HMOs) was examined...

2011

El-Hawiet, Amr, Klassen, John S., Armstrong, Glen D., Dingle, Tanis C., Eugenio, Luiz, Mulvey, George L., Szpacenko, Adam, Ng, Kenneth K.S., Kitova,Elena N., Kitov, Pavel

The binding of recombinant fragments of the C-terminal cell-binding domains of the two large exotoxins, toxin A (TcdA) and toxin B (TcdB), expressed by Clostridium difficile and a library consisting of the most abundant neutral and acidic human milk oligosaccharides (HMOs) was examined...

2012

Sun, Nian, Klassen, John S., Bai, Yu, Liu, Lan, Xia, Li, Lowary, Todd L.

The interactions between 3-O-methyl-mannose polysaccharides (MMPs), extracted from Mycobacterium smegmatis (consisting of a mixture of MMP-10, -11, -12 and -13) or obtained by chemical synthesis (MMP-5s, -8s, -11s and -14s), and linear saturated and unsaturated fatty acids (FAs), and a commercial...

2012

Xia, Li, Sun, Nian, Klassen, John S., Liu, Lan, Bai, Yu, Lowary, Todd L.

The interactions between 3-O-methyl-mannose polysaccharides (MMPs), extracted from Mycobacterium smegmatis (consisting of a mixture of MMP-10, -11, -12 and -13) or obtained by chemical synthesis (MMP-5s, -8s, -11s and -14s), and linear saturated and unsaturated fatty acids (FAs), and a commercial...

2016

Klassen, John S., Han, Ling, Kitova, Elena N.

This study reports on the use of the catch-and-release electrospray ionization mass spectrometry (CaR-ESI-MS) assay, combined with glycomicelles, as a method for detecting specific interactions between water-soluble proteins and glycolipids (GLs) in aqueous solution. The B subunit homopentamers...

2016

Han, Ling, Klassen, John S., Kitova, Elena N.

This study reports on the use of the catch-and-release electrospray ionization mass spectrometry (CaR-ESI-MS) assay, combined with glycomicelles, as a method for detecting specific interactions between water-soluble proteins and glycolipids (GLs) in aqueous solution. The B subunit homopentamers...