Competition for Membrane Receptors: Norovirus Detachment via Lectin Attachment | Sciact - CRIS-system of Boreskov Institute of Catalysis

Competition for Membrane Receptors: Norovirus Detachment via Lectin Attachment Full article

Journal

Journal of the American Chemical Society
ISSN: 0002-7863 , E-ISSN: 1520-5126

Output data

Year: 2019, Volume: 141, Number: 41, Pages: 16303-16311 Pages count : 9 DOI: 10.1021/jacs.9b06036

Tags

SUPPORTED LIPID-BILAYERS; SMALL-MOLECULE INHIBITOR; BLOOD-GROUP ANTIGENS; STRUCTURAL BASIS; VIRAL ENTRY; BINDING; VIRUS; PROTEIN; LIGAND; MODEL

Authors

Parveen Nagma ^1,6 , Rydell Gustaf E. ² , Larson Göran ³ , Hytönen Vesa P. ⁴ , Zhdanov Vladimir P. ^1,5 , Höök Fredrik ¹ , Block Stephan ^1,7

Affiliations

1	Department of Physics, Chalmers University of Technology, Gothenburg, Sweden
2	Department of Infectious Diseases, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden
3	Department of Laboratory Medicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden
4	Faculty of Medicine and Health Technology and BioMediTech, Tampere University, Tampere, Finland and Fimlab Laboratories, Tampere, Finland
5	Boreskov Institute of Catalysis, Russian Academy of Sciences, Novosibirsk, Russian Federation
6	Laboratory for Photochemistry and Spectroscopy, Department of Chemistry, KU Leuven, Leuven, Belgium
7	Department of Chemistry and Biochemistry, Freie Universität Berlin, Berlin, Germany

Funding (4)

1	Swedish Research Council	2017-00955
2	Swedish Research Council	2018-04900
3	German Research Foundation	BL1514/1
4	Academy of Finland	290506

Virus internalization into the host cells occurs via multivalent interactions, in which a single virus binds to multiple receptors in parallel. Because of analytical and experimental limitations this complex type of interaction is still poorly understood and quantified. Herein, the multivalent interaction of norovirus-like particles (noroVLPs) with H or B type 1 glycosphingolipids (GSLs), embedded in a supported phospholipid bilayer, is investigated by following the competition between noroVLPs and a lectin (from Ralstonia solanacearum) upon binding to these GSLs. Changes in noroVLP and lectin coverage, caused by competition, were monitored for both GSLs and at different GSL concentrations using quartz crystal microbalance with dissipation monitoring. The study yields information about the minimum GSL concentration needed for (i) noroVLPs to achieve firm attachment to the bilayer prior to competition and to (ii) remain firmly attached to the bilayer during competition. We show that these two concentrations are almost identical for the H type 1-noroVLP interaction but differ for B type 1, indicating an accumulation of B type 1 GSLs in the noroVLP-bilayer interaction area. Furthermore, the GSL concentration required for firm attachment is significantly larger for H type 1 than for B type 1, indicating a higher affinity of noroVLP toward B type 1. This finding is supported by extracting the energy of single noroVLP-H type 1 and noroVLP-B type 1 bonds from the competition kinetics, which were estimated to be 5 and 6 kcal/mol, respectively. This demonstrates the potential of utilizing competitive binding kinetics to analyze multivalent interactions, which has remained difficult to quantify using conventional approaches. Copyright © 2019 American Chemical Society.

Parveen N. , Rydell G.E. , Larson G. , Hytönen V.P. , Zhdanov V.P. , Höök F. , Block S.
Competition for Membrane Receptors: Norovirus Detachment via Lectin Attachment

Journal of the American Chemical Society. 2019. V.141. N41. P.16303-16311. DOI: 10.1021/jacs.9b06036 WOS Scopus РИНЦ ANCAN PMID OpenAlex

Full text from publisher

Submitted:	Jun 6, 2019
Published online:	Sep 18, 2019
Published print:	Oct 16, 2019

Web of science:	WOS:000491220300020
Scopus:	2-s2.0-85073111961
Elibrary:	41685915
Chemical Abstracts:	2019:1807110
Chemical Abstracts (print):	171:414994
PMID:	31533424
OpenAlex:	W2974811666

DB	Citing
Scopus	19
Web of science	18
Elibrary	18
OpenAlex	21