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

Ilhan Tomris, Roosmarijn van der Woude, Rebeca de Paiva Froes Rocha, Alba Torrents de la Peña, Andrew B. Ward, Robert P. de Vries*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Enveloped 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.

Original languageEnglish
Article numbere4974
Pages (from-to)1-13
Number of pages13
JournalProtein science
Volume33
Issue number4
DOIs
Publication statusPublished - Apr 2024

Keywords

  • attachment protein
  • GFP
  • hemagglutinin
  • influenza a virus
  • multivalency
  • receptor-binding
  • SARS-CoV-2

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