Evidence map›Paper›PMID 25068415›Full record

ArticleACS chemical biology2014

Antimicrobial peptide resistance of Vibrio cholerae results from an LPS modification pathway related to nonribosomal peptide synthetases.

Jeremy C Henderson, Christopher D Fage, Joe R Cannon, Jennifer S Brodbelt, Adrian T Keatinge-Clay, M Stephen Trent

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

36 citing papers in PubMed, 56 citations in OpenAlex.

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  16. Functional and structural characterization of IdnL7, an adenylation enzyme involved in incednine biosynthesis.Acta crystallographica. Section F, Structural biology communications · 2019
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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

6 authors at 1 institution in 1 country.

Jeremy C HendersonDepartment of Molecular Biosciences, ‡Department of Chemistry, §Institute of Cellular and Molecular Biology, The University of Texas at Austin , Austin, Texas 78712, United States.
Christopher D Fage
Joe R Cannon
Jennifer S Brodbelt
Adrian T Keatinge-Clay
M Stephen Trent
The University of Texas at Austin · US

Funding

Determining the Architectures and Activities of Polyketide Synthase ModulesR01GM106112 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI KEATINGE-CLAY, ADRIAN TRISTAN · 2013 to 2025
$3.9M
MODIFICATION OF HELICOBACTER PYLORI LIPOPOLYSACCHARIDESR01AI064184 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI TRENT, MICHAEL STEPHEN · 2006 to 2015
$3.4M
The Outer Surface of Vibrio CholeraeR01AI076322 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI TRENT, MICHAEL STEPHEN · 2008 to 2017
$3.2M
UVPD-MS Characterization of LipopolysaccharidesR01GM103655 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2012 to 2019
$2.3M
The Outer Surface of Vibrio choleraeR56AI076322 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI TRENT, MICHAEL STEPHEN · 2013 to 2013
$384k
NIAID NIH HHS AI064184NIAID NIH HHS AI76322NIAID NIH HHS R01 AI076322NIAID NIH HHS R56 AI076322NIGMS NIH HHS GM103655NIGMS NIH HHS GM106112NIGMS NIH HHS R01 GM103655NIGMS NIH HHS R01 GM106112
6 · The paper itself

Abstract

The current pandemic El Tor biotype of O1 Vibrio cholerae is resistant to polymyxins, whereas the previous pandemic strain of the classical biotype is polymyxin sensitive. The almEFG operon found in El Tor V. cholerae confers >100-fold resistance to polymyxins through the glycylation of lipopolysaccharide. Here, we present the mechanistic determination of initial steps in the AlmEFG pathway. We verify that AlmF is an aminoacyl carrier protein and identify AlmE as the enzyme required to activate AlmF as a functional carrier protein. A combination of structural information and activity assays was used to identify a pair of active site residues that are important for mediating AlmE glycine specificity. Overall, the structure of AlmE in complex with its glycyl-adenylate intermediate reveals that AlmE is related to Gram-positive d-alanine/d-alanyl carrier protein ligase, while the trio of proteins in the AlmEFG system forms a chemical pathway that resembles the division of labor in nonribosomal peptide synthetases.

Indexed as

Anti-Infective AgentsBacterial ProteinsCholeraCrystallography, X-RayDrug Resistance, BacterialGene Expression Regulation, BacterialLipopolysaccharidesPeptide FragmentsPeptide SynthasesPolymyxin BProtein ConformationSignal TransductionSubstrate SpecificityTandem Mass SpectrometryVibrio cholerae O1Anti-Infective AgentsBacterial ProteinsLipopolysaccharidesnon-ribosomal peptide synthasePeptide FragmentsPeptide SynthasesPolymyxin B

Identifiers

PMID25068415
PMCPMC4520716
OpenAlexW2325469930

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.