TY  - JOUR
AU  - Peters, Thomas
AU  - Creutznacher, Robert
AU  - Maass, Thorben
AU  - Mallagaray, Alvaro
AU  - Ogrissek, Patrick
AU  - Taube, Stefan
AU  - Thiede, Lars
AU  - Uetrecht, Charlotte
TI  - Norovirus–glycan interactions — how strong are they really?
JO  - Biochemical Society transactions
VL  - 50
IS  - 1
SN  - 0300-5127
CY  - London
PB  - Biochemical Society
M1  - PUBDB-2022-00779
SP  - 347 – 359
PY  - 2022
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:34940787
UR  - <Go to ISI:>//WOS:000736185200001
DO  - DOI:10.1042/BST20210526
UR  - https://bib-pubdb1.desy.de/record/474421
ER  -