Evidence map›Paper›PMID 35620472›Full record

ArticleFrontiers in bioengineering and biotechnology2022

Streamlining the Transition From Yeast Surface Display of Antibody Fragment Immune Libraries to the Production as IgG Format in Mammalian Cells.

David Fiebig, Jan P Bogen, Stefania C Carrara, Lukas Deweid, Stefan Zielonka, Julius Grzeschik, Björn Hock, Harald Kolmar

Open access · goldAbstract read
In one paragraph

Article in Frontiers in bioengineering and biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

8 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Frontiers in bioengineering and biotechnology · 2023
    Article
  7. Article
  8. Frontiers in bioengineering and biotechnology · 2022
    Review
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 2 countries.

David FiebigInstitute for Organic Chemistry and Biochemistry, Technical University of Darmstadt, Darmstadt, Germany.
Jan P BogenInstitute for Organic Chemistry and Biochemistry, Technical University of Darmstadt, Darmstadt, Germany.
Stefania C CarraraInstitute for Organic Chemistry and Biochemistry, Technical University of Darmstadt, Darmstadt, Germany.
Lukas DeweidInstitute for Organic Chemistry and Biochemistry, Technical University of Darmstadt, Darmstadt, Germany.
Stefan ZielonkaInstitute for Organic Chemistry and Biochemistry, Technical University of Darmstadt, Darmstadt, Germany.
Julius GrzeschikFerring Biologics Innovation Centre, Epalinges, Switzerland.
Björn HockFerring Biologics Innovation Centre, Epalinges, Switzerland.
Harald KolmarInstitute for Organic Chemistry and Biochemistry, Technical University of Darmstadt, Darmstadt, Germany.
Technical University of Darmstadt · DEFerring Pharmaceuticals (Switzerland) · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Yeast-surface display (YSD) is commonly applied to screen Fab immune or naïve libraries for binders of predefined target molecules. However, reformatting of isolated variants represents a time-intensive bottleneck. Herein, we present a novel approach to facilitate a lean transition from antibody screening using YSD Fab libraries to the production of full-length IgG antibodies in Expi293-F cells. In this study, utilizing Golden Gate Cloning (GGC) and a bidirectional promoter system, an exemplary Fab-displaying YSD library was generated based on immunised transgene rats. After subsequent screening for antigen-specific antibody candidates by fluorescence-activated cell sorting (FACS), the Fab-encoding genes were subcloned into a bidirectional mammalian expression vector, exhibiting CH2-CH3 encoding genes, in a GGC-mediated, PCR-free manner. This novel, straightforward and time-saving workflow allows the VH/VL pairing to be preserved. This study resulted in antibody variants exhibiting suitable biophysical properties and covered a broad VH diversity after two rounds of FACS screening, as revealed by NGS analysis. Ultimately, we demonstrate that the implication of such a gene transfer system streamlines antibody hit discovery efforts, allowing the faster characterisation of antibodies against a plethora of targets that may lead to new therapeutic agents.

Indexed as

antibody hit discoverybidirectional promotergolden gate cloningmonoclonal antibodiesreformattingyeast surface display

Identifiers

PMID35620472
PMCPMC9127228
OpenAlexW4229449396

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.