Evidence map›Paper›PMID 12869541›Full record

ArticleThe Journal of biological chemistry2003

Expression cloning and biochemical characterization of a Rhizobium leguminosarum lipid A 1-phosphatase.

Mark J Karbarz, Suzanne R Kalb, Robert J Cotter, Christian R H Raetz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
9.6field-weighted citation impact, top 2% 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

35 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. TheMicroorganisms · 2021
    Article
  6. Article
  7. Aminosugar-based immunomodulator lipid A: synthetic approaches.Beilstein journal of organic chemistry · 2018
    Review
  8. Identification ofFrontiers in microbiology · 2017
    Article
  9. Bacterial strategies of resistance to antimicrobial peptides.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016
    Review
  10. Kdo2 -lipid A: structural diversity and impact on immunopharmacology.Biological reviews of the Cambridge Philosophical Society · 2015
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
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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

4 authors at 4 institutions in 1 country.

Mark J KarbarzDepartment of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA.
Suzanne R Kalb
Robert J Cotter
Christian R H Raetz
Duke Medical Center · USDuke University · USJohns Hopkins Medicine · USJohns Hopkins University · US

Funding

LIPID A MODIFICATION SYSTEMS IN GRAM-NEGATIVE BACTERIAR37GM051796 · NIGMS · DUKE UNIVERSITY · PI RAETZ, CHRISTIAN R · 1999 to 2008
$3.0M
CHEMISTRY-BIOLOGY INTERFACE TRAINING PROGRAMT32GM008558 · NIGMS · DUKE UNIVERSITY · PI PIRRUNG, MICHAEL C · 1994 to 2003
$1.2M
NIGMS NIH HHS GM-08558NIGMS NIH HHS R37 GM051796
6 · The paper itself

Abstract

Lipid A of Rhizobium leguminosarum, a nitrogen-fixing plant endosymbiont, displays several significant structural differences when compared with Escherichia coli. An especially striking feature of R. leguminosarum lipid A is that it lacks both the 1- and 4'-phosphate groups. Distinct lipid A phosphatases that attack either the 1 or the 4' positions have previously been identified in extracts of R. leguminosarum and Rhizobium etli but not Sinorhizobium meliloti or E. coli. Here we describe the identification of a hybrid cosmid (pMJK-1) containing a 25-kb R. leguminosarum 3841 DNA insert that directs the overexpression of the lipid A 1-phosphatase. Transfer of pMJK-1 into S. meliloti 1021 results in heterologous expression of 1-phosphatase activity, which is normally absent in extracts of strain 1021, and confers resistance to polymyxin. Sequencing of a 7-kb DNA fragment derived from the insert of pMJK-1 revealed the presence of a lipid phosphatase ortholog (designated LpxE). Expression of lpxE in E. coli behind the T7lac promoter results in the appearance of robust 1-phosphatase activity, which is normally absent in E. coli membranes. Matrix-assisted laser-desorption/time of flight and radiochemical analysis of the product generated in vitro from the model substrate lipid IVA confirms the selective removal of the 1-phosphate group. These findings show that lpxE is the structural gene for the 1-phosphatase. The availability of lpxE may facilitate the re-engineering of lipid A structures in diverse Gram-negative bacteria and allow assessment of the role of the 1-phosphatase in R. leguminosarum symbiosis with plants. Possible orthologs of LpxE are present in some intracellular human pathogens, including Francisella tularensis, Brucella melitensis, and Legionella pneumophila.

Indexed as

Amino Acid SequenceBase SequenceCarbohydrate SequenceCloning, MolecularCosmidsDNA, BacterialGenes, BacterialLipid AMolecular Sequence DataMolecular StructurePhosphoric Monoester HydrolasesRecombinant ProteinsRhizobium leguminosarumSinorhizobium melilotiSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationDNA, BacterialLipid Alipid A 1-phosphatase, Rhizobium leguminosarumPhosphoric Monoester HydrolasesRecombinant Proteins

Identifiers

PMID12869541
PMCPMC2553562
OpenAlexW1975141356

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.