Evidence map›Paper›PMID 20795687›Full record

ArticleBiochemistry2010

Escherichia coli mutants that synthesize dephosphorylated lipid A molecules.

Brian O Ingram, Ali Masoudi, Christian R H Raetz

Abstract read
In one paragraph

Article in Biochemistry, 2010. 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
1.5field-weighted citation impact, top 16% 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, 19 citations in OpenAlex.

  1. Dark Side ofJournal of the American Chemical Society · 2026
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  2. Delivery ofmSphere · 2024
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  6. Review
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  10. Article
  11. Modulating the innate immune response by combinatorial engineering of endotoxin.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  12. Article
  13. Article
  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

3 authors at 2 institutions in 1 country.

Brian O IngramDepartment of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA.
Ali Masoudi
Christian R H Raetz
Duke Medical Center · USDuke University Hospital · US

Funding

STEROL LIPIDSU54GM069338 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DENNIS, EDWARD A · 2003 to 2013
$72.2M
LIPID A MODIFICATION SYSTEMS IN GRAM-NEGATIVE BACTERIAR37GM051796 · NIGMS · DUKE UNIVERSITY · PI RAETZ, CHRISTIAN R · 1999 to 2008
$3.0M
Lipid A Modification Systems in Gram-Negative BacteriaR01GM051796 · NIGMS · DUKE UNIVERSITY · PI ZHOU, PEI · 1995 to 2012
$1.5M
NIGMS NIH HHS GM-069338NIGMS NIH HHS GM-51796NIGMS NIH HHS R01 GM051796NIGMS NIH HHS R37 GM051796NIGMS NIH HHS U54 GM069338
6 · The paper itself

Abstract

The lipid A moiety of Escherichia coli lipopolysaccharide is a hexaacylated disaccharide of glucosamine that is phosphorylated at the 1 and 4' positions. Expression of the Francisella novicida lipid A 1-phosphatase FnLpxE in E. coli results in dephosphorylation of the lipid A proximal unit. Coexpression of FnLpxE and the Rhizobium leguminosarum lipid A oxidase RlLpxQ in E. coli converts much of the proximal glucosamine to 2-amino-2-deoxygluconate. Expression of the F. novicida lipid A 4'-phosphatase FnLpxF in wild-type E. coli has no effect because FnLpxF cannot dephosphorylate hexaacylated lipid A. However, expression of FnLpxF in E. coli lpxM mutants, which synthesize pentaacylated lipid A lacking the secondary 3'-myristate chain, causes extensive 4'-dephosphorylation. Coexpression of FnLpxE and FnLpxF in lpxM mutants results in massive accumulation of lipid A species lacking both phosphate groups, and introduction of RlLpxQ generates phosphate-free lipid A variants containing 2-amino-2-deoxygluconate. The proposed lipid A structures were confirmed by electrospray ionization mass spectrometry. Strains with 4'-dephosphorylated lipid A display increased polymyxin resistance. Heptose-deficient mutants of E. coli lacking both the 1- and 4'-phosphate moieties are viable on plates but sensitive to CaCl(2). Our methods for reengineering lipid A structure may be useful for generating novel vaccines and adjuvants.

Indexed as

Escherichia coliEscherichia coli ProteinsFrancisellaIonsLipid ALipopolysaccharidesPhosphoric Monoester HydrolasesPolymyxinsRhizobium leguminosarumSpectrometry, Mass, Electrospray IonizationEscherichia coli ProteinsIonsLipid Alipid A 4'-phosphataseLipopolysaccharidesPhosphoric Monoester HydrolasesPolymyxins

Identifiers

PMID20795687
PMCPMC2943570
OpenAlexW2063672440

What OpenQuestion holds

Textmetadata
LicenceTDM
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.