Viral envelope proteins fused to multiple distinct fluorescent reporters to probe receptor binding
Ilhan TomrisiD, Roosmarijn van der WoudeiD, Rebeca de Paiva Fróes RochaiD, Alba Torrents de la PeñaiD, Andrew B. WardiD, Robert P. de VriesiD
Abstract
Enveloped viruses carry one or multiple proteins with receptor binding functionalities. Functional receptors can either be glycans, proteinaceous or both, recombinant protein approaches are instrumental to gain more insight into these binding properties. Visualizing and measuring receptor binding normally entails antibody detection or direct labelling, whereas direct fluorescent fusions are attractive tools in molecular biology. Here we report a suite of different fluorescent fusions, both N- and/or C-terminal, for influenza A virus hemagglutinins and SARS-CoV-2 spike RBD. The proteins contained a total of three or six fluorescent protein barrels and were applied directly to cells to determine receptor binding properties.
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