Evidence map›Paper›PMID 28288571›Full record

ArticleBMC microbiology2017

In vivo characterization of an Hfq protein encoded by the Bacillus anthracis virulence plasmid pXO1.

Andrea B Keefer, Eugenia K Asare, Andrei P Pomerantsev, Mahtab Moayeri, Craig Martens, Stephen F Porcella, Susan Gottesman, Stephen H Leppla, Catherine E Vrentas

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. AtxA-Controlled Small RNAs ofFrontiers in microbiology · 2020
    Article
  4. 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

9 authors at 4 institutions in 1 country.

Andrea B KeeferNational Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Bethesda, MD, USA.
Eugenia K AsareNational Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Bethesda, MD, USA.
Andrei P PomerantsevNational Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Bethesda, MD, USA.
Mahtab MoayeriNational Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Bethesda, MD, USA.
Craig MartensGenomics Unit, Research Technologies Section, Rocky Mountain Laboratories, NIAID, NIH, Hamilton, MT, USA.
Stephen F PorcellaGenomics Unit, Research Technologies Section, Rocky Mountain Laboratories, NIAID, NIH, Hamilton, MT, USA.
Susan GottesmanNational Cancer Institute, NIH, Bethesda, MD, USA.
Stephen H LepplaNational Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Bethesda, MD, USA.
Catherine E VrentasNational Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Bethesda, MD, USA. catherine.vrentas@ars.usda.gov.
National Institute of Allergy and Infectious Diseases · USNational Institutes of Health · USAgricultural Research Service · USNational Cancer Institute · US

Funding

Bacterial Functions Involved in Cell Growth ControlZIABC008714 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI GOTTESMAN, SUSAN · 2009 to 2025
$20.3M
Molecular Genetics and Pathogenesis of AnthraxZIAAI001030 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI LEPPLA, STEPHEN · 2009 to 2025
$9.5M
6 · The paper itself

Abstract

backgroundBacterial Hfq proteins post-transcriptionally regulate gene expression, primarily by mediating the interaction between sRNAs (small RNAs) and their target mRNAs. The role of Hfq-based regulation has been well defined in Gram-negative bacteria, but comparatively less is known about the impact of Hfq proteins in Gram-positive species. The Gram-positive pathogen Bacillus anthracis (causative agent of anthrax) is distinct in that it expresses three homologs of Hfq: Hfq1 and Hfq2 from the chromosome, and Hfq3 from the pXO1 virulence plasmid.

resultsIn this study, we utilized overexpression as a strategy to examine the impact of Hfq3 on B. anthracis physiology. The increase in Hfq3 protein levels led to anomalous cell shape and chain formation, which manifested as a severe growth defect. This phenotype was specific to B. anthracis, as Hfq3 expression in B. subtilis at similar levels was not toxic. Toxicity was dependent on residues on the distal face of Hfq3 that are involved in mRNA binding in other bacterial species.

conclusionsThus, we hypothesize that Hfq3 interacts with RNA(s) involved in essential functions in the B. anthracis cell, leading to increased binding upon overexpression that either sequesters or accelerates degradation of RNAs important for growth. These results not only aid in elucidating the role of Hfq proteins in B. anthracis, but also contribute to our current understanding of Hfq in Gram-positive bacteria.

Indexed as

AnimalsAnthraxAutolysisBacillus anthracisBacillus subtilisEscherichia coliFemaleGene Expression Regulation, BacterialGenes, BacterialGenetic VectorsHost Factor 1 ProteinIntegration Host FactorsMice, Inbred BALB CMicrobial Sensitivity TestsMutagenesis, Site-DirectedPhenotypeHost Factor 1 ProteinIntegration Host FactorsRecombinant ProteinsRNA, BacterialRNA, MessengeranthraxBacillus anthracisgene expressionHfqmRNApXO1sRNA

Identifiers

PMID28288571
PMCPMC5348863
OpenAlexW2597386070

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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.