Evidence map›Paper›PMID 28931913›Full record

ArticleScientific reports2017

Cell-free synthesis of functional antibodies using a coupled in vitro transcription-translation system based on CHO cell lysates.

M Stech, O Nikolaeva, L Thoring, W F M Stöcklein, D A Wüstenhagen, M Hust, S Dübel, S Kubick

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
5.6field-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

47 citing papers in PubMed, 75 citations in OpenAlex.

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  10. Optimizing Human Cell-Free System for Efficient Protein Production.Journal of microbiology and biotechnology · 2025
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  11. BeyondChemical reviews · 2025
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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

8 authors at 2 institutions in 1 country.

M StechFraunhofer Institute for Cell Therapy and Immunology (IZI), Branch Bioanalytics and Bioprocesses (IZI-BB), Am Mühlenberg 13, 14476, Potsdam, Germany.
O NikolaevaFraunhofer Institute for Cell Therapy and Immunology (IZI), Branch Bioanalytics and Bioprocesses (IZI-BB), Am Mühlenberg 13, 14476, Potsdam, Germany.
L ThoringFraunhofer Institute for Cell Therapy and Immunology (IZI), Branch Bioanalytics and Bioprocesses (IZI-BB), Am Mühlenberg 13, 14476, Potsdam, Germany.
W F M StöckleinFraunhofer Institute for Cell Therapy and Immunology (IZI), Branch Bioanalytics and Bioprocesses (IZI-BB), Am Mühlenberg 13, 14476, Potsdam, Germany.
D A WüstenhagenFraunhofer Institute for Cell Therapy and Immunology (IZI), Branch Bioanalytics and Bioprocesses (IZI-BB), Am Mühlenberg 13, 14476, Potsdam, Germany.
M HustTechnische Universität Braunschweig, Institute for Biochemistry, Biotechnology and Bioinformatics, Department of Biotechnology, Spielmannstr. 7, 38106, Braunschweig, Germany.
S DübelTechnische Universität Braunschweig, Institute for Biochemistry, Biotechnology and Bioinformatics, Department of Biotechnology, Spielmannstr. 7, 38106, Braunschweig, Germany.
S KubickFraunhofer Institute for Cell Therapy and Immunology (IZI), Branch Bioanalytics and Bioprocesses (IZI-BB), Am Mühlenberg 13, 14476, Potsdam, Germany. stefan.kubick@izi-bb.fraunhofer.de.
Fraunhofer Institute for Cell Therapy and Immunology · DETechnische Universität Braunschweig · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibodies are indispensable tools for basic research as well as diagnostic and therapeutic applications. Consequently, the development of alternative manufacturing strategies which circumvent the hurdles connected to conventional antibody production technologies is of enormous interest. To address this issue, we demonstrate the synthesis of complex antibody formats, in particular immunoglobulin G (IgG) and single-chain variable fragment Fc fusion (scFv-Fc), in a microsome-containing cell-free system based on translationally active chinese hamster ovary (CHO) cell lysates. To mimic the environment for antibody folding and assembly present in living cells, antibody genes were fused to an endoplasmic reticulum (ER)-specific signal sequence. Signal-peptide induced translocation of antibody polypeptide chains into the lumen of ER microsomes was found to be the prerequisite for antibody chain assembly and functionality. In this context, we show the rapid synthesis of antibody molecules in different reaction formats, including batch and continuous-exchange cell-free (CECF) reactions, depending on the amount of protein needed for further analysis. In addition, we demonstrate site-specific and residue-specific labeling of antibodies with fluorescent non-canonical amino acids. In summary, our study describes a novel antibody production platform which combines the highly efficient mammalian protein folding machinery of CHO cells with the benefits of cell-free protein synthesis.

Indexed as

Cell-Free SystemAnimalsAntibodiesBiotechnologyCHO CellsCricetinaeCricetulusEndoplasmic ReticulumHumansImmunoglobulin GMicrosomesProtein BiosynthesisProtein FoldingReproducibility of ResultsSingle-Chain AntibodiesTranscription, GeneticAntibodiesImmunoglobulin GSingle-Chain Antibodies

Identifiers

PMID28931913
PMCPMC5607253
OpenAlexW2754500770

What OpenQuestion holds

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LicenceCC BY
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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.