Evidence map›Paper›PMID 35137182›Full record

ArticleNucleic acids research2022

Sal-type ABC-F proteins: intrinsic and common mediators of pleuromutilin resistance by target protection in staphylococci.

Merianne Mohamad, David Nicholson, Chayan Kumar Saha, Vasili Hauryliuk, Thomas A Edwards, Gemma C Atkinson, Neil A Ranson, Alex J O'Neill

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
5.9field-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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026
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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

8 authors at 2 institutions in 2 countries.

Merianne MohamadAstbury Centre for Structural Molecular Biology and School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.
David NicholsonAstbury Centre for Structural Molecular Biology and School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.
Chayan Kumar SahaDepartment of Molecular Biology, Umeå University, 90187 Umeå, Sweden.
Vasili HauryliukDepartment of Molecular Biology, Umeå University, 90187 Umeå, Sweden.ORCID 0000-0003-2389-5057
Thomas A EdwardsAstbury Centre for Structural Molecular Biology and School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.
Gemma C AtkinsonDepartment of Molecular Biology, Umeå University, 90187 Umeå, Sweden.
Neil A RansonAstbury Centre for Structural Molecular Biology and School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.ORCID 0000-0002-3640-5275
Alex J O'NeillAstbury Centre for Structural Molecular Biology and School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.ORCID 0000-0003-3222-5493
University of Leeds · GBLund University · SE

Funding

Wellcome Trust 108466Wellcome Trust 108466/Z/15/ZWellcome Trust 203743/Z/16/Z
6 · The paper itself

Abstract

The first member of the pleuromutilin (PLM) class suitable for systemic antibacterial chemotherapy in humans recently entered clinical use, underscoring the need to better understand mechanisms of PLM resistance in disease-causing bacterial genera. Of the proteins reported to mediate PLM resistance in staphylococci, the least-well studied to date is Sal(A), a putative ABC-F NTPase that-by analogy to other proteins of this type-may act to protect the ribosome from PLMs. Here, we establish the importance of Sal proteins as a common source of PLM resistance across multiple species of staphylococci. Sal(A) is revealed as but one member of a larger group of Sal-type ABC-F proteins that vary considerably in their ability to mediate resistance to PLMs and other antibiotics. We find that specific sal genes are intrinsic to particular staphylococcal species, and show that this gene family is likely ancestral to the genus Staphylococcus. Finally, we solve the cryo-EM structure of a representative Sal-type protein (Sal(B)) in complex with the staphylococcal 70S ribosome, revealing that Sal-type proteins bind into the E site to mediate target protection, likely by displacing PLMs and other antibiotics via an allosteric mechanism.

Indexed as

DiterpenesPolycyclic CompoundsAnti-Bacterial AgentsBacterial ProteinsHumansPleuromutilinsStaphylococcusAnti-Bacterial AgentsBacterial ProteinsDiterpenesPleuromutilinsPolycyclic Compounds

Identifiers

PMID35137182
PMCPMC8887462
OpenAlexW4210361175

What OpenQuestion holds

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LicenceCC BY
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.