Evidence map›Paper›PMID 36076042›Full record

ArticleBiotechnology letters2022

Efficient side-chain deacylation of polymyxin B1 in recombinant Streptomyces strains.

Xiaojing Wang, Kai Wu, Hanzhi Zhang, Jing Liu, Zhijun Yang, Jing Bai, Hao Liu, Lei Shao

Abstract read
PubMed Publisher
In one paragraph

Article in Biotechnology letters, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 69% of its field
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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

8 authors at 3 institutions in 1 country.

Xiaojing WangAffiliated Zhoupu Hospital, Shanghai University of Medicine and Health Sciences, Shanghai, China.
Kai WuMicrobial Pharmacology Laboratory, Shanghai University of Medicine and Health Sciences, Shanghai, China.
Hanzhi ZhangAbiochem Biotechnology Co., Ltd, Shanghai, China.
Jing LiuMicrobial Pharmacology Laboratory, Shanghai University of Medicine and Health Sciences, Shanghai, China.
Zhijun YangMicrobial Pharmacology Laboratory, Shanghai University of Medicine and Health Sciences, Shanghai, China.
Jing BaiSchool of Chemistry and Life Sciences, Suzhou University of Science and Technology, Suzhou, China.
Hao LiuDepartment of Antibiotics and Microorganisms, Shanghai Institute for Food and Drug Control, Shanghai, China. liuhao1968@hotmail.com.
Lei ShaoMicrobial Pharmacology Laboratory, Shanghai University of Medicine and Health Sciences, Shanghai, China. shaolei00@gmail.com.ORCID http://orcid.org/0000-0003-4130-2817
Shanghai University of Medicine and Health Sciences · CNSuzhou University of Science and Technology · CNZheJiang Institute For Food and Drug Control · CN

Funding

National Natural Science Foundation of China 81773616Natural Science Foundation of Shanghai 20ZR1424600Natural Science Research of Jiangsu Higher Education Institutions of China 20KJB180002Program of Shanghai Academic Research Leader 17XD1423200
6 · The paper itself

Abstract

objectivesPolymyxins are antibacterial polypeptides used as "last resort" therapy option for multidrug-resistant Gram-negative bacteria. The expansion of polymyxin-resistant infections has inspired development of novel polymyxin derivatives, and deacylation is one of the critical steps in generating those antibiotics. Deacylase from Actinoplanes utahensis hydrolyze the acyl moieties of echinocandins, and also efficiently deacylates daptomycin, ramoplanin and other important antibiotics. Here, deacylase was studied considering its potential usefulness in deacylating polymyxin B1.

resultsAll the six recombinant strains containing the deacylase gene catalyzed hydrolysis of polymyxin B1, yielding cyclic heptapeptides. The efficiency of recombinant S. albus (SAL701) was higher than that of the others, and deacylation was the most efficient at 40 °C in 0.2 M Tris buffer (pH 8.0) with 0.2 M Mg

conclusionsThese results show that SAL701 is effective in increasing the cyclic heptapeptide moiety of polymyxin B1. These properties of the biocatalyst may enable its development in the industrial production of polymyxins antibiotics.

Indexed as

StreptomycesAnti-Bacterial AgentsDrug Resistance, Multiple, BacterialPolymyxinsAnti-Bacterial Agentspolymyxin B(1)PolymyxinsAntibioticBioconversionDeacylasePolymyxin B1Streptomyces host

Identifiers

PMID36076042
OpenAlexW4294982632

What Socratic holds

Textmetadata
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 Socratic graph.