Norovirus-glycan interactions - how strong are they really?
binding affinity
glycobiology
mass spectrometry
nmr spectroscopy
norovirus
Journal
Biochemical Society transactions
ISSN: 1470-8752
Titre abrégé: Biochem Soc Trans
Pays: England
ID NLM: 7506897
Informations de publication
Date de publication:
28 02 2022
28 02 2022
Historique:
received:
02
11
2021
revised:
01
12
2021
accepted:
06
12
2021
pubmed:
24
12
2021
medline:
20
4
2022
entrez:
23
12
2021
Statut:
ppublish
Résumé
Infection with human noroviruses requires attachment to histo blood group antigens (HBGAs) via the major capsid protein VP1 as a primary step. Several crystal structures of VP1 protruding domain dimers, so called P-dimers, complexed with different HBGAs have been solved to atomic resolution. Corresponding binding affinities have been determined for HBGAs and other glycans exploiting different biophysical techniques, with mass spectrometry (MS) and nuclear magnetic resonance (NMR) spectroscopy being most widely used. However, reported binding affinities are inconsistent. At the extreme, for the same system MS detects binding whereas NMR spectroscopy does not, suggesting a fundamental source of error. In this short essay, we will explain the reason for the observed differences and compile reliable and reproducible binding affinities. We will then highlight how a combination of MS techniques and NMR experiments affords unique insights into the process of HBGA binding by norovirus capsid proteins.
Identifiants
pubmed: 34940787
pii: 230564
doi: 10.1042/BST20210526
pmc: PMC9022987
doi:
Substances chimiques
Blood Group Antigens
0
Capsid Proteins
0
Polysaccharides
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
347-359Informations de copyright
© 2022 The Author(s).
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