Evidence map›Paper›PMID 39038171›Full record

ArticleAnalytical chemistry2024

Investigating Lipid Transporter Protein and Lipid Interactions Using Variable Temperature Electrospray Ionization, Ultraviolet Photodissociation Mass Spectrometry, and Collision Cross Section Analysis.

Virginia K James, Bradley J Voss, Amanda Helms, M Stephen Trent, Jennifer S Brodbelt

Abstract read
In one paragraph

Article in Analytical chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Following phospholipid transfer through the OmpFProceedings of the National Academy of Sciences of the United States of America · 2025
    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

5 authors.

Virginia K JamesDepartment of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.
Bradley J VossDepartment of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, Georgia 30602, United States.
Amanda HelmsDepartment of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.ORCID 0009-0001-7194-096X
M Stephen TrentDepartment of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, Georgia 30602, United States.ORCID 0000-0001-6134-1800
Jennifer S BrodbeltDepartment of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States.ORCID 0000-0003-3207-0217

Funding

The Cell Envelope of the Multi-Drug Resistant Pathogen Acinetobacter baumanniiR01AI150098 · NIAID · UNIVERSITY OF GEORGIA · PI Michael Stephen Trent · 2020 to 2026
$3.9M
Ultraviolet Photodissociation Mass Spectrometry for Characterization of Biological MoleculesR35GM139658 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2021 to 2025
$2.9M
Synthesis and transport of outer membrane components across the Gram-negative cell envelopeR01AI176776 · NIAID · UNIVERSITY OF GEORGIA · PI Michael Stephen Trent · 2023 to 2026
$2.5M
The role of cardiolipin in the biogenesis of the Gram-negative bacterial cell envelopeR01AI174416 · NIAID · UNIVERSITY OF GEORGIA · PI Michael Stephen Trent · 2023 to 2026
$2.4M
Molecular mechanisms required for the maintenance of the gram-negative outer membraneR01AI138576 · NIAID · UNIVERSITY OF GEORGIA · PI TRENT, MICHAEL STEPHEN · 2018 to 2022
$2.0M
NIAID NIH HHS R01 AI138576NIAID NIH HHS R01 AI150098NIAID NIH HHS R01 AI174416NIAID NIH HHS R01 AI176776NIGMS NIH HHS R35 GM139658NIH HHS R35 GM13965
6 · The paper itself

Abstract

Gram-negative bacteria develop and exhibit resistance to antibiotics, owing to their highly asymmetric outer membrane maintained by a group of six proteins comprising the Mla (maintenance of lipid asymmetry) pathway. Here, we investigate the lipid binding preferences of one Mla protein, MlaC, which transports lipids through the periplasm. We used ultraviolet photodissociation (UVPD) to identify and characterize modifications of lipids endogenously bound to MlaC expressed in three different bacteria strains. UVPD was also used to localize lipid binding to MlaC residues 130-140, consistent with the crystal structure reported for lipid-bound MlaC. The impact of removing the bound lipid from MlaC on its structure was monitored based on collision cross section measurements, revealing that the protein unfolded prior to release of the lipid. The lipid selectivity of MlaC was evaluated based on titrimetric experiments, indicating that MlaC-bound lipids in various classes (sphingolipids, glycerophospholipids, and fatty acids) as long as they possessed no more than two acyl chains.

Indexed as

Spectrometry, Mass, Electrospray IonizationUltraviolet RaysBacterial ProteinsCarrier ProteinsLipidsPhotochemical ProcessesTemperatureBacterial ProteinsCarrier ProteinsLipids

Identifiers

PMID39038171
PMCPMC11533218

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Registered trials

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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.