Evidence map›Paper›PMID 33243226›Full record

ArticleBMC biology2020

Speciation and adaptive evolution reshape antioxidant enzymatic system diversity across the phylum Nematoda.

Lian Xu, Jian Yang, Meng Xu, Dai Shan, Zhongdao Wu, Dongjuan Yuan

Open access · goldAbstract read
In one paragraph

Article in BMC biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

13 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. High-quality genome ofiScience · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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

6 authors at 5 institutions in 1 country.

Lian XuKey Laboratory of Neuroregeneration, Ministry of Education and Jiangsu Province, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, 226001, China.
Jian YangKey Laboratory of Neuroregeneration, Ministry of Education and Jiangsu Province, Co-innovation Center of Neuroregeneration, Nantong University, Nantong, 226001, China.
Meng XuDepartment of Ecology, Jinan University, Guangzhou, 510632, China.
Dai ShanBGI Genomics, BGI-Shenzhen, Shenzhen, 518083, China.
Zhongdao WuDepartment of Parasitology, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou, 510080, China. wuzhd@mail.sysu.edu.cn.
Dongjuan YuanCollege of Veterinary Medicine, South China Agricultural University, Guangzhou, 510642, China. yuandj@scau.edu.cn.
Sun Yat-sen University · CNBGI Group (China) · CNJinan University · CNNantong University · CNSouth China Agricultural University · CN

Funding

Innovation Team Project of Guangdong University, China 2019KCXTD001National Natural Science Foundation of China 32072881National Research and Development Plan of China 2016YFC1200500Natural Science Foundation of Guangdong Province, China 2020A1515010294Science and Technology Program of Guangzhou 201804010006
6 · The paper itself

Abstract

backgroundNematodes have evolved to survive in diverse ecological niches and can be a serious burden on agricultural economy, veterinary medicine, and public health. Antioxidant enzymes in parasitic nematodes play a critical role in defending against host oxidative stress. However, the features of the evolution of antioxidant enzymes in the phylum Nematoda remain elusive.

resultsHere, we systematically investigated the evolution and gene expression of antioxidant enzymes in the genomes of 59 nematodes and transcriptomes of 20 nematodes. Catalase has been independently lost in several orders, suggesting that it is unnecessary for some nematodes. Unlike in mammals, phospholipid hydroperoxide glutathione peroxidase is widely distributed in nematodes, among which it has evolved independently. We found that superoxide dismutase (SOD) has been present throughout nematode evolutionary process, and the extracellular isoform (SOD3) is diverged from the corresponding enzyme in mammals and has undergone duplication and differentiation in several nematodes. Moreover, the evolution of intracellular and extracellular SOD isoforms in filaria strongly indicates that extracellular SOD3 originated from intracellular SOD1 and underwent rapid evolution to form the diversity of extracellular SOD3. We identify a novel putative metal-independent extracellular SOD presenting independently in Steinernema and Strongyloididae lineage that featured a high expression level in Strongyloides larvae. Sequence divergence of SOD3 between parasitic nematodes and their closest free-living nematode, the specifically high expression in the parasitic female stage, and presence in excretory-secretory proteome of Strongyloides suggest that SOD3 may be related with parasitism.

conclusionsThis study advances our understanding of the complex evolution of antioxidant enzymes across Nematoda and provides targets for controlling parasitic nematode diseases.

Indexed as

Biological EvolutionGenetic SpeciationAdaptation, BiologicalAnimalsAntioxidantsEnzymesNematodaAntioxidantsEnzymesAntioxidant enzymeExtracellular superoxide dismutaseGene family evolutionNematodaTranscriptome

Identifiers

PMID33243226
PMCPMC7694339
OpenAlexW3110442380

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.