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


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.

SUBMITTER: Tomris I 

PROVIDER: S-EPMC10966353 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature

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

Tomris Ilhan I   van der Woude Roosmarijn R   de Paiva Froes Rocha Rebeca R   Torrents de la Peña Alba A   Ward Andrew B AB   de Vries Robert P RP  

Protein science : a publication of the Protein Society 20240401 4


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  ...[more]

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