Evidence map›Paper›PMID 35322502›Full record

ArticleThe Journal of eukaryotic microbiology2022

Localization and functional characterization of the alternative oxidase in Naegleria.

Diego Cantoni, Ashley Osborne, Najwa Taib, Gary Thompson, Rubén Martín-Escolano, Eleanna Kazana, Elizabeth Edrich, Ian R Brown, Simonetta Gribaldo, Campbell W Gourlay and 1 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of eukaryotic microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Copper Metabolism inFrontiers in cell and developmental biology · 2022
    Article
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 at 2 institutions in 2 countries.

Diego CantoniLaboratory of Molecular & Evolutionary Parasitology, RAPID Group, School of Biosciences, University of Kent, Canterbury, UK.ORCID 0000-0001-8527-7719
Ashley OsborneLaboratory of Molecular & Evolutionary Parasitology, RAPID Group, School of Biosciences, University of Kent, Canterbury, UK.ORCID 0000-0002-2804-8298
Najwa TaibUnit Evolutionary Biology of the Microbial Cell, Department of Microbiology, Institut Pasteur, UMR CNRS 2001, Paris, France.
Gary ThompsonNMR Facility, School of Biosciences, University of Kent, Canterbury, UK.
Rubén Martín-EscolanoLaboratory of Molecular & Evolutionary Parasitology, RAPID Group, School of Biosciences, University of Kent, Canterbury, UK.ORCID 0000-0002-6262-9344
Eleanna KazanaLaboratory of Molecular & Evolutionary Parasitology, RAPID Group, School of Biosciences, University of Kent, Canterbury, UK.
Elizabeth EdrichKent Fungal Group, RAPID Group, School of Biosciences, University of Kent, Canterbury, UK.
Ian R BrownBioimaging Facility, School of Biosciences, University of Kent, Canterbury, UK.
Simonetta GribaldoUnit Evolutionary Biology of the Microbial Cell, Department of Microbiology, Institut Pasteur, UMR CNRS 2001, Paris, France.ORCID 0000-0002-7662-021X
Campbell W GourlayKent Fungal Group, RAPID Group, School of Biosciences, University of Kent, Canterbury, UK.ORCID 0000-0002-2373-6788
Anastasios D TsaousisLaboratory of Molecular & Evolutionary Parasitology, RAPID Group, School of Biosciences, University of Kent, Canterbury, UK.ORCID 0000-0002-5424-1905
University of Kent · GBCentre National de la Recherche Scientifique · FR

Funding

Biotechnology and Biological Sciences Research Council BB/M009971/1
6 · The paper itself

Abstract

The alternative oxidase (AOX) is a protein involved in supporting enzymatic reactions of the Krebs cycle in instances when the canonical (cytochrome-mediated) respiratory chain has been inhibited, while allowing for the maintenance of cell growth and necessary metabolic processes for survival. Among eukaryotes, alternative oxidases have dispersed distribution and are found in plants, fungi, and protists, including Naegleria ssp. Naegleria species are free-living unicellular amoeboflagellates and include the pathogenic species of N. fowleri, the so-called "brain-eating amoeba." Using a multidisciplinary approach, we aimed to understand the evolution, localization, and function of AOX and the role that plays in Naegleria's biology. Our analyses suggest that AOX was present in last common ancestor of the genus and structure prediction showed that all functional residues are also present in Naegleria species. Using cellular and biochemical techniques, we also functionally characterize N. gruberi's AOX in its mitochondria, and we demonstrate that its inactivation affects its proliferation. Consequently, we discuss the benefits of the presence of this protein in Naegleria species, along with its potential pathogenicity role in N. fowleri. We predict that our findings will spearhead new explorations to understand the cell biology, metabolism, and evolution of Naegleria and other free-living relatives.

Indexed as

NaegleriaNaegleria fowleriAlternative OxidaseEukaryotaMitochondrial ProteinsOxidoreductasesPlant ProteinsAlternative OxidaseMitochondrial ProteinsOxidoreductasesPlant Proteinsadaptationconfocal microscopyevolutionmitochondriaNaegleriarespiration

Identifiers

PMID35322502
PMCPMC9540462
OpenAlexW4220918731

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.