Viral envelope proteins fused to multiple distinct fluorescent reporters to probe receptor binding

Author:

Tomris Ilhan1,van der Woude Roosmarijn1,de Paiva Froes Rocha Rebeca2,Torrents de la Peña Alba2,Ward Andrew B.2,de Vries Robert P.1ORCID

Affiliation:

1. Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences Utrecht University The Netherlands

2. Department of Integrative Structural and Computational Biology The Scripps Research Institute La Jolla California USA

Abstract

AbstractEnveloped viruses carry one or multiple proteins with receptor‐binding functionalities. Functional receptors can be glycans, proteinaceous, or both; therefore, recombinant protein approaches are instrumental in attaining new insights regarding viral envelope protein receptor‐binding properties. Visualizing and measuring receptor binding typically entails antibody detection or direct labeling, whereas direct fluorescent fusions are attractive tools in molecular biology. Here, we report a suite of distinct fluorescent fusions, both N‐ and C‐terminal, for influenza A virus hemagglutinins and SARS‐CoV‐2 spike RBD. The proteins contained three or six fluorescent protein barrels and were applied directly to cells to assess receptor binding properties.

Funder

European Commission

Publisher

Wiley

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