Evidence map›Paper›PMID 33144547›Full record

ArticleJournal of microbiology and biotechnology2021

Engineered Recombinant PON1-OPH Fusion Hybrids: Potentially Effective Catalytic Bioscavengers against Organophosphorus Nerve Agent Analogs.

Nari Lee, Hyeongseok Yun, Chan Lee, Yikjae Lee, Euna Kim, Sumi Kim, Hyoeun Jeon, Chiho Yu, Jaerang Rho

Abstract read
In one paragraph

Article in Journal of microbiology and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. 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

9 authors.

Nari LeeDepartment of Microbiology and Molecular Biology, Chungnam National University, Daejeon 34134, Republic of Korea.
Hyeongseok YunDepartment of Microbiology and Molecular Biology, Chungnam National University, Daejeon 34134, Republic of Korea.
Chan LeeDepartment of Microbiology and Molecular Biology, Chungnam National University, Daejeon 34134, Republic of Korea.
Yikjae LeeDepartment of Microbiology and Molecular Biology, Chungnam National University, Daejeon 34134, Republic of Korea.
Euna KimDepartment of Microbiology and Molecular Biology, Chungnam National University, Daejeon 34134, Republic of Korea.
Sumi KimDepartment of Microbiology and Molecular Biology, Chungnam National University, Daejeon 34134, Republic of Korea.
Hyoeun JeonDepartment of Microbiology and Molecular Biology, Chungnam National University, Daejeon 34134, Republic of Korea.
Chiho YuAgency for Defense Development, P.O. Box 35, Yuseong, Daejeon 34186, Republic of Korea.
Jaerang RhoDepartment of Microbiology and Molecular Biology, Chungnam National University, Daejeon 34134, Republic of Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Organophosphorus nerve agents (OPNAs), including both G- and V-type nerve agents such as sarin, soman, tabun and VX, are extremely neurotoxic organophosphorus compounds. Catalytic bioscavengers capable of hydrolyzing OPNAs are under development because of the low protective effects and adverse side effects of chemical antidotes to OPNA poisoning. However, these bioscavengers have certain limitations for practical application, including low catalytic activity and narrow specificity. In this study, we generated a fusion-hybrid form of engineered recombinant human paraoxonase 1 (rePON1) and bacterial organophosphorus hydrolase (OPH), referred to as GV-hybrids, using a flexible linker to develop more promising catalytic bioscavengers against a broad range of OPNAs. These GV-hybrids were able to synergistically hydrolyze both G-type OPNA analogs (paraoxon: 1.7 ~ 193.7-fold,

Indexed as

AntidotesAryldialkylphosphataseCatalysisGenetic EngineeringHumansHydrolysisNerve AgentsOrganophosphatesOrganophosphorus CompoundsPhosphoric Triester HydrolasesRecombinant Fusion ProteinsSubstrate SpecificityAntidotesAryldialkylphosphataseNerve AgentsOrganophosphatesOrganophosphorus CompoundsPhosphoric Triester HydrolasesPON1 protein, humanRecombinant Fusion ProteinstabunBioscavengernerve agentorganophosphorus compoundorganophosphorus hydrolaseparaoxonase 1phosphotriesterase

Identifiers

PMID33144547
PMCPMC9705692

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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.