Evidence map›Paper›PMID 25991684›Full record

ArticlemBio2015

Reinforcing Lipid A Acylation on the Cell Surface of Acinetobacter baumannii Promotes Cationic Antimicrobial Peptide Resistance and Desiccation Survival.

Joseph M Boll, Ashley T Tucker, Dustin R Klein, Alexander M Beltran, Jennifer S Brodbelt, Bryan W Davies, M Stephen Trent

Open access · goldAbstract read
In one paragraph

Article in mBio, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed
5.0field-weighted citation impact, top 3% 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

126 citing papers in PubMed, 192 citations in OpenAlex.

  1. Loss of CsrA inProceedings of the National Academy of Sciences of the United States of America · 2026
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  2. Review
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  4. Membrane-Focused Strategies AgainstAntibiotics (Basel, Switzerland) · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Lipid landscaping of the bacterial cell surface.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  9. A surface-exposed cardiolipin synthase provides an unexpected paradigm for maintaining the Gram-negative outer membrane.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. Exogenous KFrontiers in microbiology · 2026
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  11. Phenylacetic acid mediatesMicrobiology (Reading, England) · 2026
    Article
  12. The glutathione pathway is required for biofilm formation inCurrent research in microbial sciences · 2026
    Article
  13. Review
  14. Article
  15. Article
  16. Resurfacing promotes antibacterial activity of a lipid A-binding nanobody.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Carbapenem-ResistantMicroorganisms · 2025
    Review
  18. A critical role forProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Article
  20. Article

66 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 1 country.

Joseph M BollDepartment of Molecular Biosciences, University of Texas at Austin, Austin, Texas, USA.
Ashley T TuckerDepartment of Molecular Biosciences, University of Texas at Austin, Austin, Texas, USA.
Dustin R KleinDepartment of Chemistry, University of Texas at Austin, Austin, Texas, USA.
Alexander M BeltranDepartment of Molecular Biosciences, University of Texas at Austin, Austin, Texas, USA.
Jennifer S BrodbeltDepartment of Chemistry, University of Texas at Austin, Austin, Texas, USA.
Bryan W Davies
M Stephen TrentDepartment of Infectious Diseases, University of Georgia, College of Veterinary Medicine, Athens, Georgia, USA strent@uga.edu.
The University of Texas at Austin · USUniversity of Georgia · US

Funding

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
Preventing Persistence and Spread of Acinetobacter baumannii in HospitalsF32GM116523 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI TUCKER, ASHLEY T · 2015 to 2017
$109k
Solving a Novel Multidrug Resistance Puzzle: Complete Loss of LipooligosaccharideF32GM113488 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BOLL, JOSEPH MICHAEL · 2015 to 2016
$109k
NIAID NIH HHS AI064184NIAID NIH HHS AI076322NIAID NIH HHS R01 AI064184NIAID NIH HHS R01 AI076322NIAID NIH HHS R56 AI076322NIGMS NIH HHS F32 GM113488NIGMS NIH HHS F32GM113488NIGMS NIH HHS F32 GM116523NIGMS NIH HHS GM103655NIGMS NIH HHS R01 GM103655
6 · The paper itself

Abstract

unlabelledAcinetobacter baumannii is an emerging Gram-negative pathogen found in hospitals and intensive care units. In order to persist in hospital environments, A. baumannii withstands desiccative conditions and can rapidly develop multidrug resistance to conventional antibiotics. Cationic antimicrobial peptides (CAMPs) have served as therapeutic alternatives because they target the conserved lipid A component of the Gram-negative outer membrane to lyse the bacterial cell. However, many Gram-negative pathogenic bacteria, including A. baumannii, fortify their outer membrane with hepta-acylated lipid A to protect the cell from CAMP-dependent cell lysis. Whereas in Escherichia coli and Salmonella, increased production of the outer membrane acyltransferase PagP results in formation of protective hepta-acylated lipid A, which reinforces the lipopolysaccharide portion of the outer membrane barrier, A. baumannii does not carry a gene that encodes a PagP homolog. Instead, A. baumannii has evolved a PagP-independent mechanism to synthesize protective hepta-acylated lipid A. Taking advantage of a recently adapted A. baumannii genetic recombineering system, we characterized two putative acyltransferases in A. baumannii designated LpxLAb (A. baumannii LpxL) and LpxMAb (A. baumannii LpxM), which transfer one and two lauroyl (C12:0) acyl chains, respectively, during lipid A biosynthesis. Hepta-acylation of A. baumannii lipid A promoted resistance to vertebrate and polymyxin CAMPs, which are prescribed as last-resort treatment options. Intriguingly, our analysis also showed that LpxMAb-dependent acylation of lipid A is essential for A. baumannii desiccation survival, a key resistance mechanism for survival in hospital environments. Compounds that inhibit LpxMAb-dependent hepta-acylation of lipid A could act synergistically with CAMPs to provide innovative transmission prevention strategies and treat multidrug-resistant infections. IMPORTANCE: Acinetobacter baumannii infections can be life threatening, and disease can progress in a variety of host tissues. Current antibiotic regimen and disinfectant strategies have failed to limit nosocomial A. baumannii infections. Instead, the rate of A. baumannii infection among health care communities has skyrocketed due to the bacterium's adaptability. Its aptitude for survival over extended periods on inanimate objects, such as catheters, respirators, and surfaces in intensive care units, or on the hands of health care workers and its ability to rapidly develop antibiotic resistance make A. baumannii a threat to health care communities. Emergence of multidrug- and extremely drug-resistant A. baumannii illustrates the ineffectiveness of current prevention and treatment options. Our analysis to understand how A. baumannii resists cationic antimicrobial peptide (CAMP)-mediated and desiccative killing revealed two lipid A acyltransferases that produce protective hepta-acylated lipid A. Our work suggests that inhibiting lipid A biosynthesis by targeting the acyltransferase LpxMAb (A. baumannii LpxM) could provide a novel target to combat this pathogen.

Indexed as

Acinetobacter baumanniiAcylationAcyltransferasesAntimicrobial Cationic PeptidesBacterial ProteinsCell MembraneDesiccationDrug Resistance, BacterialHumansLipid AMicrobial ViabilityPolymyxinsAcyltransferasesAntimicrobial Cationic PeptidesBacterial ProteinsLipid ALpxL protein, bacteriaPolymyxins

Identifiers

PMID25991684
PMCPMC4442142
OpenAlexW1888541961

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.