Studying the interaction of glycans with intact virions and virus-like particles by ligand-observed NMR spectroscopy

Bibliographische Detailangaben
Veröffentlicht in:	Magnetic resonance in chemistry : MRC. - 1985. - 62(2024), 5 vom: 03. Mai, Seite 337-344
1. Verfasser:	Haselhorst, Thomas (VerfasserIn)
Format:	Online-Aufsatz
Sprache:	English
Veröffentlicht:	2024
Zugriff auf das übergeordnete Werk:	Magnetic resonance in chemistry : MRC
Schlagworte:	Journal Article Review Research Support, Non-U.S. Gov't STD NMR spectroscopy structural glycoscience structural virology virus‐glycan interactions Ligands Polysaccharides Proteins

Beschreibung
Zusammenfassung:	© 2023 The Author. Magnetic Resonance in Chemistry published by John Wiley & Sons Ltd. Virus-glycan interactions play a crucial role in the infection process of many viruses. NMR spectroscopy has emerged as a powerful tool for studying these interactions at the molecular level. In this article, we review several published papers and reports that have highlighted the application of NMR spectroscopy in understanding the complex questions of how viruses engage with and bind to receptor glycans. The use of saturation transfer difference (STD) NMR spectroscopy has demonstrated itself as highly advantageous in investigating the interaction between glycans and intact virions or virus-like particles (VLPs). The broad NMR signal linewidth of virions and VLPs allows efficient saturation without affecting the glycan signals. The advantage of this approach is that the viral capsid environment in protein organization and function is not ignored and therefore provides a more biologically relevant model for exploring the interactions between the virus and the host cell glycans. We will review some examples of using NMR spectroscopy to study influenza cell tropism, rotaviruses, and noroviruses
Beschreibung:	Date Completed 09.04.2024 Date Revised 23.04.2024 published: Print-Electronic Citation Status MEDLINE
ISSN:	1097-458X
DOI:	10.1002/mrc.5399