Evidence map›Paper›PMID 41618851›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026

Systematic Engineering of Proteases in Saccharopolyspora Spinosa Reveals Synergistic Enhancement of Spinosad Biosynthesis via Substrate Flux Optimization.

Duo Jin, Wangqiong Chen, Danlu Yang, Qing Liu, Baolong Bai, Zirui Dai, Xirong Liu, Zirong Zhu, Jie Rang, Liqiu Xia

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

10 authors.

Duo JinHunan Provincial Key Laboratory of Microbial Molecular Biology, College of Life Science, Hunan Normal University, Changsha, China.
Wangqiong ChenHunan Provincial Key Laboratory of Microbial Molecular Biology, College of Life Science, Hunan Normal University, Changsha, China.
Danlu YangHunan Provincial Key Laboratory of Microbial Molecular Biology, College of Life Science, Hunan Normal University, Changsha, China.
Qing LiuHunan Provincial Key Laboratory of Microbial Molecular Biology, College of Life Science, Hunan Normal University, Changsha, China.
Baolong BaiHunan Provincial Key Laboratory of Microbial Molecular Biology, College of Life Science, Hunan Normal University, Changsha, China.
Zirui DaiHunan Provincial Key Laboratory of Microbial Molecular Biology, College of Life Science, Hunan Normal University, Changsha, China.
Xirong LiuHunan Norchem Pharmaceutical Co., Ltd, Changsha, Hunan, China.
Zirong ZhuHunan Provincial Key Laboratory of Microbial Molecular Biology, College of Life Science, Hunan Normal University, Changsha, China.
Jie RangHunan Provincial Key Laboratory of Microbial Molecular Biology, College of Life Science, Hunan Normal University, Changsha, China.
Liqiu XiaHunan Provincial Key Laboratory of Microbial Molecular Biology, College of Life Science, Hunan Normal University, Changsha, China.ORCID https://orcid.org/0000-0001-8443-2916

Funding

National Basic Research Program (973) of China 2012CB722301National Natural Science Foundation of China 32200062,31770106Natural Science Foundation of Hunan Province 2024JJ5258
6 · The paper itself

Abstract

Natural product biosynthesis is tightly coupled to nitrogen allocation. However, scalable strategies to amplify pathway outputs remain limited. Here, atmospheric and room temperature plasma (ARTP) mutagenesis of Saccharopolyspora spinosa yielded a high-performing strain, D184, which showed improved utilization of extracellular nitrogen sources together with enhanced spinosad production. To identify novel regulatory mechanisms linking nitrogen utilization with natural product biosynthetic efficiency, we established a combinatorial engineering workflow that integrates systematic protease genetic manipulation, multi-omics analysis, and rational design. Using this workflow, the functional contributions of eight overexpressed high-titer protease-related targets were examined from a set of 21 protease-related genes related to nitrogen utilization, which were categorized into three modules: membrane proteostasis (htpX), adenosine triphosphate (ATP)-dependent proteolysis (clpP), and amino acid supply (dap, pepP, metAP, alp). Synergy modeling, coupled with cross-module coordination, highlighted a representative triangular combination, pepP-clpP-htpX. Overexpressing this combination in D184 increased spinosad titer to 2318.87 mg/L in a nitrogen-rich 50L bioreactor, corresponding to a 9.81 fold improvement over the wild type. Crucially, this study provided causal evidence that dynamic inter-modular crosstalk governs nitrogen-dependent metabolic flux in D184. These findings establish fundamental mechanistic insights into protease-mediated regulation in S. spinosa and offer guidance for protease-informed optimization of natural product biosynthesis.

Indexed as

MacrolidesMetabolic EngineeringPeptide HydrolasesSaccharopolysporaBacterial ProteinsDrug CombinationsNitrogenBacterial ProteinsDrug CombinationsMacrolidesNitrogenPeptide Hydrolasesspinosadmetabolic regulationproteases engineeringsaccharopolyspora spinosaspinosadsynergism

Identifiers

PMID41618851
PMCPMC13067860

What OpenQuestion holds

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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.