Evidence map›Paper›PMID 32182402›Full record

ArticleChembiochem : a European journal of chemical biology2020

Surface Display of Complex Enzymes by in Situ SpyCatcher-SpyTag Interaction.

Sabrina Gallus, Theo Peschke, Malte Paulsen, Teresa Burgahn, Christof M Niemeyer, Kersten S Rabe

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Engineering of Surface Display Systems inBiotech (Basel (Switzerland)) · 2026
    Article
  2. Review
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  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Living Bacteria: A New Vehicle for Vaccine Delivery in Cancer Immunotherapy.International journal of molecular sciences · 2025
    Review
  12. Article
  13. Genetically surface-modifiedBiotechnology reports (Amsterdam, Netherlands) · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Surface Display of Complex Enzymes by in Situ SpyCatcher-SpyTag Interaction.Chembiochem : a European journal of chemical biology · 2020
    Article
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.

Sabrina GallusKarlsruhe Institute of Technology (KIT), Institute for Biological Interfaces 1 (IBG 1), Hermann-von-Helmholtz-Platz 1, 76344, Eggenstein-Leopoldshafen, Germany.
Theo PeschkeKarlsruhe Institute of Technology (KIT), Institute for Biological Interfaces 1 (IBG 1), Hermann-von-Helmholtz-Platz 1, 76344, Eggenstein-Leopoldshafen, Germany.
Malte PaulsenEuropean Molecular Biology Laboratory (EMBL) Flow Cytometry Core Facility, Meyerhofstraße 1, 69117, Heidelberg, Germany).
Teresa BurgahnKarlsruhe Institute of Technology (KIT), Institute for Biological Interfaces 1 (IBG 1), Hermann-von-Helmholtz-Platz 1, 76344, Eggenstein-Leopoldshafen, Germany.
Christof M NiemeyerKarlsruhe Institute of Technology (KIT), Institute for Biological Interfaces 1 (IBG 1), Hermann-von-Helmholtz-Platz 1, 76344, Eggenstein-Leopoldshafen, Germany.
Kersten S RabeKarlsruhe Institute of Technology (KIT), Institute for Biological Interfaces 1 (IBG 1), Hermann-von-Helmholtz-Platz 1, 76344, Eggenstein-Leopoldshafen, Germany.ORCID 0000-0001-7909-8191

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The display of complex proteins on the surface of cells is of great importance for protein engineering and other fields of biotechnology. Herein, we describe a modular approach, in which the membrane anchor protein Lpp-OmpA and a protein of interest (passenger) are expressed independently as genetically fused SpyCatcher and SpyTag units and assembled in situ by post-translational coupling. Using fluorescent proteins, we first demonstrate that this strategy allows the construct to be installed on the surface of E. coli cells. The scope of our approach was then demonstrated by using three different functional enzymes, the stereoselective ketoreductase Gre2p, the homotetrameric glucose 1-dehydrogenase GDH, and the bulky heme- and diflavin-containing cytochrome P450 BM3 (BM3). In all cases, the SpyCatcher-SpyTag method enabled the generation of functional whole-cell biocatalysts, even for the bulky BM3, which could not be displayed by conventional fusion with Lpp-OmpA. Furthermore, by using a GDH variant carrying an internal SpyTag, the system could be used to display an enzyme with unmodified N- and C-termini.

Indexed as

Cell MembraneCell Surface Display TechniquesEnzymesEscherichia coliProtein Processing, Post-TranslationalRecombinant Fusion ProteinsEnzymesRecombinant Fusion ProteinsbiocatalysisLpp-OmpAmembrane proteinsself-assemblysurface display

Identifiers

PMID32182402
PMCPMC7497234

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.