Evidence map›Paper›PMID 23448318›Full record

ArticleMicrobial cell factories2013

New stable anchor protein and peptide linker suitable for successful spore surface display in B. subtilis.

Krzysztof Hinc, Adam Iwanicki, Michał Obuchowski

Abstract read
In one paragraph

Article in Microbial cell factories, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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

20 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Computational and structural biotechnology journal · 2023
    Article
  10. Surface Display ofFrontiers in immunology · 2022
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

3 authors.

Krzysztof HincLaboratory of Molecular Bacteriology, Intercollegiate Faculty of Biotechnology UG & MUG, Medical University of Gdańsk, Dębinki 1, Gdańsk 80-211, Poland.
Adam Iwanicki
Michał Obuchowski

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundIn last decade spores have been successfully used as a surface display platform. Various peptides or proteins were displayed this way as functional enzymes or antigens. Nearly all attempts involved use of three coat proteins: CotB, CotC or CotG. Increasing knowledge of the structure of the spore coat allowed us to propose the use of other proteins whose localization in the spore envelope has been determined. We also propose the application of a new linker suitable for building fusion proteins.

resultsWe show that a member of the outer coat, CotZ, is a good candidate as a new anchor protein useful in spore surface display. This protein allows use of relatively large passenger proteins and their efficient display on the spore surface. Analysis by Western- and dot-blotting, combined with immunofluorescence microscopy, allowed us to estimate the number of displayed fusion proteins molecules as 1.4 × 10(2) per spore. In addition, we present data indicating that the use of a peptide linker, which forms a stable α-helix, may greatly improve the display of anchored proteins on the spore surface.

conclusionCotZ can be used as an efficient anchor protein in the outer spore coat. Its localisation in the coat crust layer should guarantee surface display of passenger proteins. Moreover, a CotZ based fusion can tolerate relatively large passenger proteins for efficient spore surface display. In addition, to the properties of both the anchor and passenger proteins, an important issue is the nature of the linker. Here we present evidence that the linker, which forms a stable α-helix, may be crucial for successful display.

Indexed as

Bacillus subtilisBacterial ProteinsGenetic VectorsMicroscopy, FluorescencePeptidesRecombinant Fusion ProteinsSpores, BacterialBacterial ProteinsPeptidesRecombinant Fusion Proteins

Identifiers

PMID23448318
PMCPMC3599258

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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.