Evidence map›Paper›PMID 32825605›Full record

ArticleVaccines2020

High-Yield Expression and Purification of Recombinant Influenza Virus Proteins from Stably-Transfected Mammalian Cell Lines.

Jeffrey W Ecker, Greg A Kirchenbaum, Spencer R Pierce, Amanda L Skarlupka, Rodrigo B Abreu, R Ethan Cooper, Dawn Taylor-Mulneix, Ted M Ross, Giuseppe A Sautto

Open access · goldAbstract read
In one paragraph

Article in Vaccines, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

65 citing papers in PubMed, 75 citations in OpenAlex.

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5 more citing papers are in PubMed but not listed here.

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

9 authors at 1 institution in 1 country.

Jeffrey W EckerCenter for Vaccines and Immunology, University of Georgia, Athens, GA 30602, USA.
Greg A KirchenbaumCenter for Vaccines and Immunology, University of Georgia, Athens, GA 30602, USA.ORCID 0000-0001-6463-7623
Spencer R PierceCenter for Vaccines and Immunology, University of Georgia, Athens, GA 30602, USA.ORCID 0000-0001-8913-6657
Amanda L SkarlupkaCenter for Vaccines and Immunology, University of Georgia, Athens, GA 30602, USA.
Rodrigo B AbreuCenter for Vaccines and Immunology, University of Georgia, Athens, GA 30602, USA.
R Ethan CooperCenter for Vaccines and Immunology, University of Georgia, Athens, GA 30602, USA.
Dawn Taylor-MulneixCenter for Vaccines and Immunology, University of Georgia, Athens, GA 30602, USA.
Ted M RossCenter for Vaccines and Immunology, University of Georgia, Athens, GA 30602, USA.
Giuseppe A SauttoCenter for Vaccines and Immunology, University of Georgia, Athens, GA 30602, USA.ORCID 0000-0002-0273-2235
University of Georgia · US

Funding

COVID Supplement - COMPONENT A OF THE COLLABORATIVE INFLUENZA VACCINE INNOVATION CENTERS (CIVICS) PROGRAM TO DESIGN AND EVALUATE INNOVATIVE INFLUENZA VACCINE APPROACHES,75N93019C00052 · NIAID · UNIVERSITY OF GEORGIA · PI ROSS, TED · 2019 to 2025
$74.6M
Georgia Research Alliance N/ANIAID NIH HHS 75N93019C00052NIH/NIAID Center of Excellence for Influenza Research and Surveillance (CEIRS) N/AUniversity of Georgia N/A
6 · The paper itself

Abstract

Influenza viruses infect millions of people each year, resulting in significant morbidity and mortality in the human population. Therefore, generation of a universal influenza virus vaccine is an urgent need and would greatly benefit public health. Recombinant protein technology is an established vaccine platform and has resulted in several commercially available vaccines. Herein, we describe the approach for developing stable transfected human cell lines for the expression of recombinant influenza virus hemagglutinin (HA) and recombinant influenza virus neuraminidase (NA) proteins for the purpose of in vitro and in vivo vaccine development. HA and NA are the main surface glycoproteins on influenza virions and the major antibody targets. The benefits for using recombinant proteins for in vitro and in vivo assays include the ease of use, high level of purity and the ability to scale-up production. This work provides guidelines on how to produce and purify recombinant proteins produced in mammalian cell lines through either transient transfection or generation of stable cell lines from plasmid creation through the isolation step via Immobilized Metal Affinity Chromatography (IMAC). Collectively, the establishment of this pipeline has facilitated large-scale production of recombinant HA and NA proteins to high purity and with consistent yields, including glycosylation patterns that are very similar to proteins produced in a human host.

Indexed as

cloningIMACinfluenzaplasmidprotein purificationrecombinant proteinstable cell linesvaccine

Identifiers

PMID32825605
PMCPMC7565037
OpenAlexW3080190993

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.