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Polymer-stabilized sialylated nanoparticles : synthesis, optimization, and differential binding to influenza hemagglutinins
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Richards, Sarah-Jane, Baker, Alexander, Walker, Marc and Gibson, Matthew I. (2020) Polymer-stabilized sialylated nanoparticles : synthesis, optimization, and differential binding to influenza hemagglutinins. Biomacromolecules, 21 (4). pp. 1604-1612. doi:10.1021/acs.biomac.0c00179 ISSN 1525-7797.
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WRAP-Polymer-stabilized-sialylated-nanoparticles-synthesis-Gibson-2020.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution Non-commercial No Derivatives 4.0. Download (2901Kb) | Preview |
Official URL: https://doi.org/10.1021/acs.biomac.0c00179
Abstract
During influenza infection, hemagglutinins (HAs) on the viral surface bind to sialic acids on the host cell's surface. While all HAs bind sialic acids, human influenza targets terminal α2,6 sialic acids and avian influenza targets α2,3 sialic acids. For interspecies transmission (zoonosis), HA must mutate to adapt to these differences. Here, multivalent gold nanoparticles bearing either α2,6- or α2,3-sialyllactosamine have been developed to interrogate a panel of HAs from pathogenic human, low pathogenic avian, and other species' influenza. This method exploits the benefits of multivalent glycan presentation compared to monovalent presentation to increase affinity and investigate how multivalency affects selectivity. Using a library-orientated approach, parameters including polymer coating and core diameter were optimized for maximal binding and specificity were probed using galactosylated particles and a panel of biophysical techniques [ultraviolet-visible spectroscopy, dynamic light scattering, and biolayer interferometry]. The optimized particles were then functionalized with sialyllactosamine and their binding analyzed against a panel of HAs derived from pathogenic influenza strains including low pathogenic avian strains. This showed significant specificity crossover, which is not observed in monovalent formats, with binding of avian HAs to human sialic acids and in agreement with alternate assay formats. These results demonstrate that precise multivalent presentation is essential to dissect the interactions of HAs and may aid the discovery of tools for disease and zoonosis transmission.
| Item Type: | Journal Article | ||||||||||||||||||
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| Subjects: | Q Science > QP Physiology Q Science > QR Microbiology R Medicine > RA Public aspects of medicine R Medicine > RC Internal medicine R Medicine > RS Pharmacy and materia medica |
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| Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Science > Physics |
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| SWORD Depositor: | Library Publications Router | ||||||||||||||||||
| Library of Congress Subject Headings (LCSH): | Influenza, Hemagglutinin, Multivalent molecules, Binding sites (Biochemistry) | ||||||||||||||||||
| Journal or Publication Title: | Biomacromolecules | ||||||||||||||||||
| Publisher: | American Chemical Society | ||||||||||||||||||
| ISSN: | 1525-7797 | ||||||||||||||||||
| Official Date: | 31 March 2020 | ||||||||||||||||||
| Dates: |
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| Volume: | 21 | ||||||||||||||||||
| Number: | 4 | ||||||||||||||||||
| Page Range: | pp. 1604-1612 | ||||||||||||||||||
| DOI: | 10.1021/acs.biomac.0c00179 | ||||||||||||||||||
| Status: | Peer Reviewed | ||||||||||||||||||
| Publication Status: | Published | ||||||||||||||||||
| Access rights to Published version: | Open Access (Creative Commons) | ||||||||||||||||||
| Copyright Holders: | Copyright © 2020 American Chemical Society | ||||||||||||||||||
| Date of first compliant deposit: | 29 April 2020 | ||||||||||||||||||
| Date of first compliant Open Access: | 29 April 2020 | ||||||||||||||||||
| RIOXX Funder/Project Grant: |
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