Search

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...

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...

2013

Klassen, John S., Zhang, Yixuan, Deng, Lu, Kitova, Elena, N.

The results of collision-induced dissociation (CID) experiments performed on gaseous protonated and deprotonated ions of complexes of cholera toxin B subunit homopentamer (CTB5) with the pentasaccharide (β-D-Galp-(1→3)-β-D-GalpNAc-(1→4)[α-D-Neu5Ac-(2→3)]-β-D-Galp-(1→4)-β-D-Glcp (GM1)) and...

2012

Klassen, John S., Lin, Hong, Kitova, Elena N., Ng, Kenneth K., Johnson, M. A., Eugenio, Luiz

Electrospray ionization mass spectrometry (ESI-MS) measurements were performed under a variety of solution conditions on a highly acidic sub-fragment (B3C) of the C-terminal carbohydrate-binding repeat region of Clostridium difficile toxin B, and two mutants (B4A and B4B) containing fewer acidic...

2015

Zhong, Weiming, Quigley, Christina, Klassen, John S., Fang, Hao, Jiang, Xi, Wei, Chao, Tan, Ming, Xia, Ming, Huang, Pengwei, Fan, Qiang, Zhang, Xufu

The recent discovery that human noroviruses (huNoVs) recognize sialic acids (SAs) in addition to histo-blood group antigens (HBGAs) pointed to a new direction in studying virus-host interactions during calicivirus infection. HuNoVs remain difficult to study due to the lack of an effective cell...

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)...

2010

El-Hawiet, Amr, Liu, Lan, Klassen, John S., Kitova, Elena N.

A new electrospray ionization mass spectrometry (ES-MS) approach for quantifying protein—ligand complexes that are prone to in-source (gas-phase) dissociation is described. The method, referred to here as the reference ligand ES-MS method, is based on the direct ES-MS assay and competitive ligand...

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...

2013

Deng, Lu, Klassen, John S., Kitova, Elena N.

Dissociation rate constants (koff) for the model high affinity interaction between biotin (B) and the homotetramer of natural core streptavidin (S4) were measured at pH 7 and temperatures ranging from 15 to 45 °C using electrospray ionization mass spectrometry (ESI-MS). Two different approaches...

2014

Klassen, John S., Ng, Simon, Liu, Lan, Bailey, Justin, Derda, Ratmir, Baergen, Alyson, Jalili, Nobar

This paper reports on the first experimental study of the energies of noncovalent fluorine bonding in a protein-ligand complex in the absence of solvent. Arrhenius parameters were measured for the dissociation of gaseous deprotonated ions of complexes of bovine β-lactoglobulin (Lg), a model...