Evidence map›Paper›PMID 24372821›Full record

ArticleMolecular microbiology2014

Identification of a broad family of lipid A late acyltransferases with non-canonical substrate specificity.

Erica J Rubin, John P O'Brien, Petko L Ivanov, Jennifer S Brodbelt, M Stephen Trent

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 21 citations in OpenAlex.

  1. Enteric-colonizedGut microbes · 2026
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  4. Review
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  7. Article
  8. Review
  9. AlmG, responsible for polymyxin resistance in pandemicThe Journal of biological chemistry · 2017
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Helicobacter pylori: expect the unexpected.Molecular microbiology · 2014
    Article
  16. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Erica J RubinInstitute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX, USA.
John P O'Brien
Petko L Ivanov
Jennifer S Brodbelt
M Stephen Trent
The University of Texas at Austin · US

Funding

MODIFICATION OF HELICOBACTER PYLORI LIPOPOLYSACCHARIDESR01AI064184 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI TRENT, MICHAEL STEPHEN · 2006 to 2015
$3.4M
UVPD-MS Characterization of LipopolysaccharidesR01GM103655 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2012 to 2019
$2.3M
NIAID NIH HHS AI064184NIAID NIH HHS R01 AI064184NIGMS NIH HHS GM103655NIGMS NIH HHS R01 GM103655
6 · The paper itself

Abstract

Most Gram-negative organisms produce lipopolysaccharide (LPS), a complex macromolecule anchored to the bacterial membrane by the lipid A moiety. Lipid A is synthesized via the Raetz pathway, a conserved nine-step enzymatic process first characterized in Escherichia coli. The Epsilonproteobacterium Helicobacter pylori uses the Raetz pathway to synthesize lipid A; however, only eight of nine enzymes in the pathway have been identified in this organism. Here, we identify the missing acyltransferase, Jhp0255, which transfers a secondary acyl chain to the 3'-linked primary acyl chain of lipid A, an activity similar to that of E. coli LpxM. This enzyme, reannotated as LpxJ due to limited sequence similarity with LpxM, catalyses addition of a C12:0 or C14:0 acyl chain to the 3'-linked primary acyl chain of lipid A, complementing an E. coli LpxM mutant. Enzymatic assays demonstrate that LpxJ and homologues in Campylobacter jejuni and Wolinella succinogenes can act before the 2' secondary acyltransferase, LpxL, as well as the 3-deoxy-d-manno-octulosonic acid (Kdo) transferase, KdtA. Ultimately, LpxJ is one member of a large class of acyltransferases found in a diverse range of organisms that lack an E. coli LpxM homologue, suggesting that LpxJ participates in lipid A biosynthesis in place of an LpxM homologue.

Indexed as

Multigene FamilyAcylationAcyltransferasesBacteriaBacterial ProteinsEpsilonproteobacteriaGenetic Complementation TestLipid AMutationPhenotypeSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSubstrate SpecificitySugar Acids2-keto-3-deoxyoctonateAcyltransferasesBacterial ProteinsLipid ASugar Acids

Identifiers

PMID24372821
PMCPMC3947442
OpenAlexW1492114039

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.