<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Tomris I</submitter><funding>European Commission</funding><funding>NWO Rubicon Grant</funding><pagination>e4974</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10966353</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>33(4)</volume><pubmed_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.</pubmed_abstract><journal>Protein science : a publication of the Protein Society</journal><pubmed_title>Viral envelope proteins fused to multiple distinct fluorescent reporters to probe receptor binding.</pubmed_title><pmcid>PMC10966353</pmcid><funding_grant_id>45219118</funding_grant_id><funding_grant_id>802780</funding_grant_id><pubmed_authors>van der Woude R</pubmed_authors><pubmed_authors>de Paiva Froes Rocha R</pubmed_authors><pubmed_authors>de Vries RP</pubmed_authors><pubmed_authors>Tomris I</pubmed_authors><pubmed_authors>Torrents de la Pena A</pubmed_authors><pubmed_authors>Ward AB</pubmed_authors></additional><is_claimable>false</is_claimable><name>Viral envelope proteins fused to multiple distinct fluorescent reporters to probe receptor binding.</name><description>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.</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Apr</publication><modification>2026-06-03T06:52:11.159Z</modification><creation>2025-04-04T22:59:32.035Z</creation></dates><accession>S-EPMC10966353</accession><cross_references><pubmed>38533540</pubmed><doi>10.1002/pro.4974</doi></cross_references></HashMap>