Evidence map›Paper›PMID 17697396›Full record

ArticleParasitology2007

Type I and type II fatty acid biosynthesis in Eimeria tenella: enoyl reductase activity and structure.

J Z Lu, S P Muench, M Allary, S Campbell, C W Roberts, E Mui, R L McLeod, D W Rice, S T Prigge

Open access · greenAbstract read
In one paragraph

Article in Parasitology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. FromiScience · 2024
    Article
  2. Eimeria proteins: order amidst disorder.Parasites & vectors · 2022
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. 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

9 authors at 5 institutions in 2 countries.

J Z LuDepartment of Molecular Microbiology & Immunology, Johns Hopkins Bloomberg School of Public Health, Baltimore, MD 21205, USA.
S P Muench
M Allary
S Campbell
C W Roberts
E Mui
R L McLeod
D W Rice
S T Prigge
Johns Hopkins University · USUniversity of Chicago · USUniversity of Sheffield · GBEdinburgh Napier University · GBUniversity of Strathclyde · GB

Funding

XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 1985 to 2011
$17.6M
TREATMENT OF CONGENITAL TOXOPLASMOSISR01AI027530 · NIAID · UNIVERSITY OF CHICAGO · PI MCLEOD, RIMA L · 1989 to 2010
$2.8M
NOVEL APICOMPLEXAN METABOLISM AND ORGANELLE TRANSITR01AI043228 · NIAID · UNIVERSITY OF CHICAGO · PI MCLEOD, RIMA L · 1997 to 2005
$2.1M
Roles of Lipoate Pathways in Plasmodium SurvivalR01AI065853 · NIAID · JOHNS HOPKINS UNIVERSITY · PI PRIGGE, SEAN TAYLOR · 2006 to 2010
$2.0M
Roles of lipoate pathways in Plasmodium survivalR56AI065853 · NIAID · JOHNS HOPKINS UNIVERSITY · PI PRIGGE, SEAN TAYLOR · 2012 to 2012
$400k
NCRR NIH HHS P41 RR001081NCRR NIH HHS P41 RR-01081NIAID NIH HHS AI027530NIAID NIH HHS AI043228NIAID NIH HHS AI065853NIAID NIH HHS R01 AI027530NIAID NIH HHS R01 AI043228NIAID NIH HHS R01 AI065853NIAID NIH HHS R56 AI065853
6 · The paper itself

Abstract

Apicomplexan parasites of the genus Eimeria are the major causative agent of avian coccidiosis, leading to high economic losses in the poultry industry. Recent results show that Eimeria tenella harbours an apicoplast organelle, and that a key biosynthetic enzyme, enoyl reductase, is located in this organelle. In related parasites, enoyl reductase is one component of a type II fatty acid synthase (FAS) and has proven to be an attractive target for antimicrobial compounds. We cloned and expressed the mature form of E. tenella enoyl reductase (EtENR) for biochemical and structural studies. Recombinant EtENR exhibits NADH-dependent enoyl reductase activity and is inhibited by triclosan with an IC50 value of 60 nm. The crystal structure of EtENR reveals overall similarity with other ENR enzymes; however, the active site of EtENR is unoccupied, a state rarely observed in other ENR structures. Furthermore, the position of the central beta-sheet appears to block NADH binding and would require significant movement to allow NADH binding, a feature not previously seen in the ENR family. We analysed the E. tenella genomic database for orthologues of well-characterized bacterial and apicomplexan FAS enzymes and identified 6 additional genes, suggesting that E. tenella contains a type II FAS capable of synthesizing saturated, but not unsaturated, fatty acids. Interestingly, we also identified sequences that appear to encode multifunctional type I FAS enzymes, a feature also observed in Toxoplasma gondii, highlighting the similarity between these apicomplexan parasites.

Indexed as

Amino Acid SequenceAnimalsBinding SitesEimeria tenellaFatty Acid DesaturasesFatty AcidsFatty Acid Synthase, Type IFatty Acid Synthase, Type IIModels, MolecularMolecular Sequence DataProtein ConformationRecombinant ProteinsFatty Acid DesaturasesFatty AcidsFatty Acid Synthase, Type IFatty Acid Synthase, Type IIRecombinant Proteins

Identifiers

PMID17697396
PMCPMC2801558
OpenAlexW2115605595

What OpenQuestion holds

Textmetadata
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.