Glycan-protein interactions are highly specific yet transient, rendering glycans ideal recognition signals in a variety of biological processes. In human norovirus (HuNoV) infection, histo-blood group antigens (HBGAs) play an essential but poorly understood role. For murine norovirus infection (MNV), sialylated glycolipids or glycoproteins appear to be important. It has also been suggested that HuNoV capsid proteins bind to sialylated ganglioside head groups. Here, we study the binding of HBGAs...
[NMR paper] Automated glycan assembly of 19F labelled glycan probes enables high-throughput NMR studies of protein-glycan interactions
Automated glycan assembly of 19F labelled glycan probes enables high-throughput NMR studies of protein-glycan interactions
Protein-glycan interactions mediate important biological processes, including pathogen host invasion and cellular communication. Major challenges to monitoring these low affinity interactions are the required high sensitivity of a biophysical assay and to cover a breath of synthetic well-defined structures. Here, we showcase an expedite approach that integrates automated glycan assembly (AGA) of 19 F labelled probes and high-throughput NMR methods, enabling the study...
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03-30-2021 11:12 PM
Structural investigation of glycan recognition by the ERAD quality control lectin Yos9
Structural investigation of glycan recognition by the ERAD quality control lectin Yos9
Abstract
Yos9 is an essential component of the endoplasmic reticulum associated protein degradation (ERAD) system that is responsible for removing terminally misfolded proteins from the ER lumen and mediating proteasomal degradation in the cytosol. Glycoproteins that fail to attain their native conformation in the ER expose a distinct oligosaccharide structure, a terminal α1,6-linked mannose residue, that is specifically recognized by the mannose 6-phoshate...
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11-25-2018 06:02 AM
[NMR paper] Breaking the limits in analyzing carbohydrate recognition by NMR: Resolving Branch-Selective Interaction of a Tetraantennary N-Glycan with lectins
Breaking the limits in analyzing carbohydrate recognition by NMR: Resolving Branch-Selective Interaction of a Tetraantennary N-Glycan with lectins
Abstract: The biological recognition of complex-type N-glycans is part of many key physiological and pathological events. Despite their importance, the structural characterization of these events remains an unsolved task. The inherent flexibility of N-glycans hampers crystallization and the chemical equivalence of individual branches precludes their NMR characterization. By using a chemoenzymatically synthesized tetraantennary N-glycan...
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10-09-2017 04:12 PM
[NMR paper] Epitope mapping of histo blood group antigens bound to norovirus VLPs using STD NMR experiments reveals fine details of molecular recognition.
Epitope mapping of histo blood group antigens bound to norovirus VLPs using STD NMR experiments reveals fine details of molecular recognition.
Epitope mapping of histo blood group antigens bound to norovirus VLPs using STD NMR experiments reveals fine details of molecular recognition.
Glycoconj J. 2017 Aug 19;:
Authors: Fiege B, Leuthold M, Parra F, Dalton KP, Meloncelli PJ, Lowary TL, Peters T
Abstract
Attachment of human noroviruses to histo blood group antigens (HBGAs) is thought to be critical for the infection process....
Study finding could shed light on molecular mechanisms underlying Huntington's disease - News-Medical.net
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Study finding could shed light on molecular mechanisms underlying Huntington's disease
News-Medical.net
... the process," he said. "Using advanced nuclear magnetic resonance spectroscopy, we were able to provide an unprecedented view of the internal structure of the protein clumps that form in the disease, which we hope will one day lead to new therapies ...
Researchers Describe Brain Plaques Involved In...
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02-04-2016 11:46 AM
[NMR paper] A rigid lanthanide binding tag to aid NMR studies of a 70 kDa homodimeric coat protein of human norovirus.
A rigid lanthanide binding tag to aid NMR studies of a 70 kDa homodimeric coat protein of human norovirus.
Related Articles A rigid lanthanide binding tag to aid NMR studies of a 70 kDa homodimeric coat protein of human norovirus.
Chem Commun (Camb). 2015 Nov 10;
Authors: Mallagaray A, Domínguez G, Peters T, Pérez-Castells J
Abstract
Attachment of human noroviruses to histo blood group antigens is thought to be essential for infection of host cells. Molecular details of the attachment process can be studied in vitro using a...
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11-11-2015 02:40 PM
[NMR paper] Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments.
Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments.
Related Articles Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments.
J Biol Chem. 2013 Jun 20;
Authors: Probert F, Whittaker SB, Crispin M, Mitchell DA, Dixon AM
Abstract
The C-type lectin DC-SIGNR (Dendritic Cell-Specific ICAM-3-Grabbing...
NMR Experiments Shed New Light on Glycan Recognition by Human and Murine Norovirus Capsid Proteins
Linear Mode
