Evidence map›Paper›PMID 36142753›Full record

ArticleInternational journal of molecular sciences2022

A Single

Sean Doyle, Daragh D Cuskelly, Niall Conlon, David A Fitzpatrick, Ciara B Gilmartin, Sophia H Dix, Gary W Jones

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. 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
1.2field-weighted citation impact, top 22% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Linker-mediated domain separation enhances cold adaptation in cellulases.Protein science : a publication of the Protein Society · 2025
    Article
  3. Article
  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

7 authors at 1 institution in 2 countries.

Sean DoyleDepartment of Biology, Maynooth University, Maynooth, Co., W23 F2K8 Kildare, Ireland.
Daragh D CuskellyDepartment of Biology, Maynooth University, Maynooth, Co., W23 F2K8 Kildare, Ireland.
Niall ConlonDepartment of Biology, Maynooth University, Maynooth, Co., W23 F2K8 Kildare, Ireland.ORCID 0000-0002-9534-1742
David A FitzpatrickDepartment of Biology, Maynooth University, Maynooth, Co., W23 F2K8 Kildare, Ireland.ORCID 0000-0001-7345-6998
Ciara B GilmartinDepartment of Biology, Maynooth University, Maynooth, Co., W23 F2K8 Kildare, Ireland.
Sophia H DixDepartment of Biology, Maynooth University, Maynooth, Co., W23 F2K8 Kildare, Ireland.
Gary W JonesDepartment of Biology, Maynooth University, Maynooth, Co., W23 F2K8 Kildare, Ireland.
National University of Ireland, Maynooth · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The naturally occurring sulphur-containing histidine derivative, ergothioneine (EGT), exhibits potent antioxidant properties and has been proposed to confer human health benefits. Although it is only produced by select fungi and prokaryotes, likely to protect against environmental stress, the GRAS organism Saccharomyces cerevisiae does not produce EGT naturally. Herein, it is demonstrated that the recombinant expression of a single gene, Aspergillus fumigatus egtA, in S. cerevisiae results in EgtA protein presence which unexpectedly confers complete EGT biosynthetic capacity. Both High Performance Liquid Chromatography (HPLC) and LC−mass spectrometry (MS) analysis were deployed to detect and confirm EGT production in S. cerevisiae. The localisation and quantification of the resultant EGT revealed a significantly (p < 0.0001) larger quantity of EGT was extracellularly present in culture supernatants than intracellularly accumulated in 96 h yeast cultures. Methionine addition to cultures improved EGT production. The additional expression of two candidate cysteine desulfurases from A. fumigatus was thought to be required to complete EGT biosynthesis, namely AFUA_2G13295 and AFUA_3G14240, termed egt2a and egt2b in this study. However, the co-expression of egtA and egt2a in S. cerevisiae resulted in a significant decrease in the observed EGT levels (p < 0.05). The AlphaFold prediction of A. fumigatus EgtA 3-Dimensional structure illuminates the bidomain structure of the enzyme and the opposing locations of both active sites. Overall, we clearly show that recombinant S. cerevisiae can biosynthesise and secrete EGT in an EgtA-dependent manner which presents a facile means of producing EGT for biotechnological and biomedical use.

Indexed as

ErgothioneineAntioxidantsAspergillus fumigatusCysteineEgtazic AcidHistidineHumansMethionineSaccharomyces cerevisiaeSulfurAntioxidantsCysteineEgtazic AcidErgothioneineHistidineMethionineSulfurAlphaFoldantioxidantcell factoryergothioneineredox stressROS

Identifiers

PMID36142753
PMCPMC9502471
OpenAlexW4296354713

What OpenQuestion holds

Textmetadata
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.