Evidence map›Paper›PMID 34342709›Full record

ArticleApplied microbiology and biotechnology2021

Homogenous overexpression of the extracellular matrix protein Netrin-1 in a hollow fiber bioreactor.

Aniel Moya-Torres, Monika Gupta, Fabian Heide, Natalie Krahn, Scott Legare, Denise Nikodemus, Thomas Imhof, Markus Meier, Manuel Koch, Jörg Stetefeld

Open access · hybridAbstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
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    Article
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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

10 authors at 4 institutions in 4 countries.

Aniel Moya-TorresDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.
Monika GuptaDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.
Fabian HeideDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada. heidef@myumanitoba.ca.ORCID http://orcid.org/0000-0002-6849-3177
Natalie KrahnDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.
Scott LegareDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.
Denise NikodemusBiotech Research and Innovation Centre, University of Copenhagen, Copenhagen, Denmark.
Thomas ImhofInstitute for Dental Research and Oral Musculoskeletal Biology, Center for Biochemistry, Medical Faculty, University of Cologne, Cologne, Germany.
Markus MeierDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.
Manuel KochInstitute for Dental Research and Oral Musculoskeletal Biology, Center for Biochemistry, Center for Molecular Medicine, Medical Faculty, University of Cologne, Cologne, Germany.
Jörg StetefeldDepartment of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada. jorg.stetefeld@umanitoba.ca.
University of Manitoba · CAUniversity of Cologne · DEUniversity of Copenhagen · DKYale University · US

Funding

Canadian Institutes of Health Research (CIHR) 201610PJT-152935Deutsche Forschungsgemeinschaft FOR 2722Deutsche Forschungsgemeinschaft NI 1895/1-1
6 · The paper itself

Abstract

The production of recombinant proteins for functional and biophysical studies, especially in the field of structural determination, still represents a challenge as high quality and quantities are needed to adequately perform experiments. This is in part solved by optimizing protein constructs and expression conditions to maximize the yields in regular flask expression systems. Still, work flow and effort can be substantial with no guarantee to obtain improvements. This study presents a combination of workflows that can be used to dramatically increase protein production and improve processing results, specifically for the extracellular matrix protein Netrin-1. This proteoglycan is an axon guidance cue which interacts with various receptors to initiate downstream signaling cascades affecting cell differentiation, proliferation, metabolism, and survival. We were able to produce large glycoprotein quantities in mammalian cells, which were engineered for protein overexpression and secretion into the media using the controlled environment provided by a hollow fiber bioreactor. Close monitoring of the internal bioreactor conditions allowed for stable production over an extended period of time. In addition to this, Netrin-1 concentrations were monitored in expression media through biolayer interferometry which allowed us to increase Netrin-1 media concentrations tenfold over our current flask systems while preserving excellent protein quality and in solution behavior. Our particular combination of genetic engineering, cell culture system, protein purification, and biophysical characterization permitted us to establish an efficient and continuous production of high-quality protein suitable for structural biology studies that can be translated to various biological systems. KEY POINTS: • Hollow fiber bioreactor produces substantial yields of homogenous Netrin-1 • Biolayer interferometry allows target protein quantitation in expression media • High production yields in the bioreactor do not impair Netrin-1 proteoglycan quality.

Indexed as

BioreactorsAnimalsCell DifferentiationCulture MediaNetrin-1NetrinsCulture MediaNetrin-1NetrinsBiophysical quality controlBioreactorExtracellular matrix protein productionNetrin-1Sleeping beauty

Identifiers

PMID34342709
PMCPMC8390410
OpenAlexW3189585901

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.