Journal Article

PUBDB-2022-00779

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Norovirus–glycan interactions — how strong are they really?

Peters, T. ; Creutznacher, R. ; Maass, T. ; Mallagaray, A. ; Ogrissek, P. ; Taube, S.Extern* ; Thiede, L.CSSB* ; Uetrecht, C. (Corresponding author)CSSB*XFEL.EU*DESY*

2022
Biochemical Society London

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Please use a persistent id in citations: doi:10.1042/BST20210526  doi:10.3204/PUBDB-2022-00779

Abstract: 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.

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Contributing Institute(s):

1. Strukturelle Mikrobiologie CSSB (FS-CS)
2. Universität zu Lübeck (U Lübeck)
3. CSSB - Leibniz-Institut für Experimentelle Virologie (LIV) / DESY - Charlotte Uetrecht (CSSB-LIV/DESY-CU)

Research Program(s):

1. 633 - Life Sciences – Building Blocks of Life: Structure and Function (POF4-633) (POF4-633)

Experiment(s):

1. No specific instrument

Appears in the scientific report 2022

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Database coverage:
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