Evidence map›Paper›PMID 24761813›Full record

ArticleParasites & vectors2014

Transsulfuration is an active pathway for cysteine biosynthesis in Trypanosoma rangeli.

Ibeth Romero, Jair Téllez, Lais Eiko Yamanaka, Mario Steindel, Alvaro José Romanha, Edmundo Carlos Grisard

Open access · goldAbstract read
In one paragraph

Article in Parasites & vectors, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

12 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Lupeol Acetate and α-Amyrin Terpenes Activity againstTropical medicine and infectious disease · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. A ComparativeEvolutionary bioinformatics online · 2016
    Article
  11. Article
  12. 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 1 institution in 1 country.

Ibeth RomeroLaboratórios de Protozoologia e de Bioinformática, Departamento de Microbiologia, Imunologia e Parasitologia, Centro de Ciências Biológicas, Universidade Federal de Santa Catarina, Florianópolis, SC 88040-970, Brasil. ibicris@gmail.com.
Jair Téllez
Lais Eiko Yamanaka
Mario Steindel
Alvaro José Romanha
Edmundo Carlos Grisard
Universidade Federal de Santa Catarina · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundCysteine, a sulfur-containing amino acid, plays an important role in a variety of cellular functions such as protein biosynthesis, methylation, and polyamine and glutathione syntheses. In trypanosomatids, glutathione is conjugated with spermidine to form the specific antioxidant thiol trypanothione (T[SH]2) that plays a central role in maintaining intracellular redox homeostasis and providing defence against oxidative stress.

methodsWe cloned and characterised genes coding for a cystathionine β-synthase (CβS) and cysteine synthase (CS), key enzymes of the transsulfuration and assimilatory pathways, respectively, from the hemoflagellate protozoan parasite Trypanosoma rangeli.

resultsOur results show that T. rangeli CβS (TrCβS), similar to its homologs in T. cruzi, contains the catalytic domain essential for enzymatic activity. Unlike the enzymes in bacteria, plants, and other parasites, T. rangeli CS lacks two of the four lysine residues (Lys26 and Lys184) required for activity. Enzymatic studies using T. rangeli extracts confirmed the absence of CS activity but confirmed the expression of an active CβS. Moreover, CβS biochemical assays revealed that the T. rangeli CβS enzyme also has serine sulfhydrylase activity.

conclusionThese findings demonstrate that the RTS pathway is active in T. rangeli, suggesting that this may be the only pathway for cysteine biosynthesis in this parasite. In this sense, the RTS pathway appears to have an important functional role during the insect stage of the life cycle of this protozoan parasite.

Indexed as

Amino Acid SequenceAnimalsCloning, MolecularCystathionine beta-SynthaseCysteineCysteine SynthaseGene Expression Regulation, EnzymologicMolecular Sequence DataOxidative StressPhosphatidylethanolaminesSpecies SpecificityTrypanosoma cruziTrypanosoma rangeli1,2-bis(decanoylthio)-1,2-dideoxyglycerol-3-phosphorylethanolamineCystathionine beta-SynthaseCysteineCysteine SynthasePhosphatidylethanolamines

Identifiers

PMID24761813
PMCPMC4005819
OpenAlexW2125735740

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.