Evidence map›Paper›PMID 32710576›Full record

ArticleProtein science : a publication of the Protein Society2020

Drivers of recombinant soluble influenza A virus hemagglutinin and neuraminidase expression in mammalian cells.

Roosmarijn van der Woude, Hannah L Turner, Ilhan Tomris, Kim M Bouwman, Andrew B Ward, Robert P de Vries

Open access · hybridAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 28% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 18 citations in OpenAlex.

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  8. Design andInternational journal of molecular sciences · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Roosmarijn van der WoudeDepartment of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, Netherlands.
Hannah L TurnerDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA.
Ilhan TomrisDepartment of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, Netherlands.
Kim M BouwmanDepartment of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, Netherlands.
Andrew B WardDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA.
Robert P de VriesDepartment of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, Netherlands.ORCID 0000-0002-1586-4464
Utrecht University · NLScripps Research Institute · US

Funding

Bill & Melinda Gates Foundation OPP1170236European Research Council 802780
6 · The paper itself

Abstract

Recombinant soluble trimeric influenza A virus hemagglutinins (HA) and tetrameric neuraminidases (NAs) have proven to be excellent tools to decipher biological properties. Receptor binding and sialic acid cleavage by recombinant proteins correlate satisfactorily compared to whole viruses. Expression of HA and NA can be achieved in a plethora of different laboratory hosts. For immunological and receptor interaction studies however, insect and mammalian cell expressed proteins are preferred due to the presence of N-linked glycosylation and disulfide bond formation. Because mammalian-cell expression is widely applied, an increased expression yield is an important goal. Here we report that using codon-optimized genes and sfGFP fusions, the expression yield of HA can be significantly improved. sfGFP also significantly increased expression yields when fused to the N-terminus of NA. In this study, a suite of different hemagglutinin and neuraminidase constructs are described, which can be valuable tools to study a wide array of different HAs, NAs and their mutants.

Indexed as

Green Fluorescent ProteinsHemagglutinin Glycoproteins, Influenza VirusInfluenza A virusNeuraminidaseRecombinant Fusion ProteinsViral ProteinsHEK293 CellsHumansSolubilityGreen Fluorescent ProteinsHemagglutinin Glycoproteins, Influenza VirusNA protein, influenza A virusNeuraminidaseRecombinant Fusion ProteinsViral Proteinshemagglutinininfluenza A virusmultimerization domainneuraminidasesuper folder green fluorescent protein

Identifiers

PMID32710576
PMCPMC7454420
OpenAlexW3043899985

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.