Evidence map›Paper›PMID 38773100›Full record

ArticleNature communications2024

Cell-free biosynthesis and engineering of ribosomally synthesized lanthipeptides.

Wan-Qiu Liu, Xiangyang Ji, Fang Ba, Yufei Zhang, Huiling Xu, Shuhui Huang, Xiao Zheng, Yifan Liu, Shengjie Ling, Michael C Jewett and 1 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. A ribosomally synthesized and posttranslationally modified peptide with ADP-ribosylation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. RadicalJournal of the American Chemical Society · 2026
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Reconstituting alternative life using the test-bed of cell-free systems.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  12. Article
  13. Breakthrough inActa biochimica et biophysica Sinica · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Substrate recognition by a peptide-aminoacyl-tRNA ligase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Article
  20. Cell-free protein synthesis platforms for accelerating drug discovery.Biotechnology notes (Amsterdam, Netherlands) · 2025
    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

11 authors.

Wan-Qiu Liu *School of Physical Science and Technology, ShanghaiTech University, Shanghai, China.
Xiangyang Ji *School of Physical Science and Technology, ShanghaiTech University, Shanghai, China.
Fang BaSchool of Physical Science and Technology, ShanghaiTech University, Shanghai, China.ORCID http://orcid.org/0000-0002-1458-1227
Yufei ZhangSchool of Physical Science and Technology, ShanghaiTech University, Shanghai, China.
Huiling XuSchool of Physical Science and Technology, ShanghaiTech University, Shanghai, China.
Shuhui HuangSchool of Physical Science and Technology, ShanghaiTech University, Shanghai, China.
Xiao ZhengSchool of Physical Science and Technology, ShanghaiTech University, Shanghai, China.
Yifan LiuSchool of Physical Science and Technology, ShanghaiTech University, Shanghai, China. liuyf6@shanghaitech.edu.cn.ORCID http://orcid.org/0000-0002-2989-6280
Shengjie LingSchool of Physical Science and Technology, ShanghaiTech University, Shanghai, China. lingshj@shanghaitech.edu.cn.ORCID http://orcid.org/0000-0003-1156-0479
Michael C JewettDepartment of Bioengineering, Stanford University, Stanford, CA, US. mjewett@stanford.edu.
Jian LiSchool of Physical Science and Technology, ShanghaiTech University, Shanghai, China. lijian@shanghaitech.edu.cn.ORCID http://orcid.org/0000-0003-2359-238X

Funding

Innovative technologies to transform antibiotic discovery. Project 4 Infection site-specific amplification of antimicrobial conjugatesU19AI142780 · NIAID · BROAD INSTITUTE, INC. · PI HUNG, DEBORAH T · 2019 to 2023
$33.9M
NIAID NIH HHS U19 AI142780
6 · The paper itself

Abstract

Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a major class of natural products with diverse chemical structures and potent biological activities. A vast majority of RiPP gene clusters remain unexplored in microbial genomes, which is partially due to the lack of rapid and efficient heterologous expression systems for RiPP characterization and biosynthesis. Here, we report a unified biocatalysis (UniBioCat) system based on cell-free gene expression for rapid biosynthesis and engineering of RiPPs. We demonstrate UniBioCat by reconstituting a full biosynthetic pathway for de novo biosynthesis of salivaricin B, a lanthipeptide RiPP. Next, we delete several protease/peptidase genes from the source strain to enhance the performance of UniBioCat, which then can synthesize and screen salivaricin B variants with enhanced antimicrobial activity. Finally, we show that UniBioCat is generalizable by synthesizing and evaluating the bioactivity of ten uncharacterized lanthipeptides. We expect UniBioCat to accelerate the discovery, characterization, and synthesis of RiPPs.

Indexed as

Cell-Free SystemProtein Processing, Post-TranslationalRibosomesBiocatalysisBiosynthetic PathwaysMultigene FamilyPeptidesPeptides

Identifiers

PMID38773100
PMCPMC11109155

What OpenQuestion holds

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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.