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Article

Protein Secondary Structure Affects Glycan Clustering in Native Mass Spectrometry

1
Leibniz Institute for Experimental Virology (HPI), 20251 Hamburg, Germany
2
Organic Chemistry, Free University Berlin, 14195 Berlin, Germany
3
Fritz-Haber-Institut der Max-Planck-Gesellschaft, 14195 Berlin, Germany
4
Center of Structural and Cell Biology in Medicine (CSCM), Institute of Chemistry and Metabolomics, University of Lübeck, 23562 Lübeck, Germany
5
Institute of Virology, University of Lübeck, 23562 Lübeck, Germany
6
European XFEL GmbH, 22869 Schenefeld, Germany
7
Centre for Structural Systems Biology (CSSB), 22607 Hamburg, Germany
*
Author to whom correspondence should be addressed.
Authors contributed equally to this work.
Academic Editors: Adam Taylor and Marko Noerenberg
Life 2021, 11(6), 554; https://doi.org/10.3390/life11060554
Received: 2 May 2021 / Revised: 7 June 2021 / Accepted: 8 June 2021 / Published: 11 June 2021
(This article belongs to the Special Issue Capsid Protein)
Infection by the human noroviruses (hNoV), for the vast majority of strains, requires attachment of the viral capsid to histo blood group antigens (HBGAs). The HBGA-binding pocket is formed by dimers of the protruding domain (P dimers) of the capsid protein VP1. Several studies have focused on HBGA binding to P dimers, reporting binding affinities and stoichiometries. However, nuclear magnetic resonance spectroscopy (NMR) and native mass spectrometry (MS) analyses yielded incongruent dissociation constants (KD) for the binding of HBGAs to P dimers and, in some cases, disagreed on whether glycans bind at all. We hypothesized that glycan clustering during electrospray ionization in native MS critically depends on the physicochemical properties of the protein studied. It follows that the choice of a reference protein is crucial. We analysed carbohydrate clustering using various P dimers and eight non-glycan binding proteins serving as possible references. Data from native and ion mobility MS indicate that the mass fraction of β-sheets has a strong influence on the degree of glycan clustering. Therefore, the determination of specific glycan binding affinities from native MS must be interpreted cautiously. View Full-Text
Keywords: ion mobility; native MS; electrospray ionization; norovirus capsid protein; carbohydrate binding; HBGA ion mobility; native MS; electrospray ionization; norovirus capsid protein; carbohydrate binding; HBGA
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MDPI and ACS Style

Yan, H.; Lockhauserbäumer, J.; Szekeres, G.P.; Mallagaray, A.; Creutznacher, R.; Taube, S.; Peters, T.; Pagel, K.; Uetrecht, C. Protein Secondary Structure Affects Glycan Clustering in Native Mass Spectrometry. Life 2021, 11, 554. https://doi.org/10.3390/life11060554

AMA Style

Yan H, Lockhauserbäumer J, Szekeres GP, Mallagaray A, Creutznacher R, Taube S, Peters T, Pagel K, Uetrecht C. Protein Secondary Structure Affects Glycan Clustering in Native Mass Spectrometry. Life. 2021; 11(6):554. https://doi.org/10.3390/life11060554

Chicago/Turabian Style

Yan, Hao, Julia Lockhauserbäumer, Gergo Peter Szekeres, Alvaro Mallagaray, Robert Creutznacher, Stefan Taube, Thomas Peters, Kevin Pagel, and Charlotte Uetrecht. 2021. "Protein Secondary Structure Affects Glycan Clustering in Native Mass Spectrometry" Life 11, no. 6: 554. https://doi.org/10.3390/life11060554

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