Evidence map›Paper›PMID 27658030›Full record

ArticlePloS one

SpyTag/SpyCatcher Cyclization Enhances the Thermostability of Firefly Luciferase.

Meng Si, Qing Xu, Ling Jiang, He Huang

Abstract read
In one paragraph

Article in PloS one. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Luciferase complementation for cellular assays beyond protein-protein interactions.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025
    Review
  5. Article
  6. Enhancement of the Thermostability ofMolecules (Basel, Switzerland) · 2024
    Article
  7. Article
  8. Improved Thermal Stability of a Novel Acidophilic Phytase.Journal of microbiology and biotechnology · 2024
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Review
  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

4 authors.

Meng SiCollege of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, 211816, China.
Qing XuCollege of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, 211816, China.
Ling JiangCollege of Food Sciences and Light Industry, Nanjing Tech University, Nanjing, 211816, China.
He HuangCollege of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, 211816, China.ORCID http://orcid.org/0000-0003-4670-9018

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SpyTag can spontaneously form a covalent isopeptide bond with its protein partner SpyCatcher. Firefly luciferase from Photinus pyralis was cyclized in vivo by fusing SpyCatcher at the N terminus and SpyTag at the C terminus. Circular LUC was more thermostable and alkali-tolerant than the wild type, without compromising the specific activity. Structural analysis indicated that the cyclized LUC increased the thermodynamic stability of the structure and remained more properly folded at high temperatures when compared with the wild type. We also prepared an N-terminally and C-terminally shortened form of the SpyCatcher protein and cyclization using this truncated form led to even more thermostability than the original form. Our findings suggest that cyclization with SpyTag and SpyCatcher is a promising and effective strategy to enhance thermostability of enzymes.

Identifiers

PMID27658030
PMCPMC5033358

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Registered trials

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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.