Evidence map›Paper›PMID 18362134›Full record

ArticleInfection and immunity2008

Moraxella catarrhalis expresses an unusual Hfq protein.

Ahmed S Attia, Jennifer L Sedillo, Wei Wang, Wei Liu, Chad A Brautigam, Wade Winkler, Eric J Hansen

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. RNA-binding proteins in bacteria.Nature reviews. Microbiology · 2018
    Review
  3. Article
  4. C-terminal domain of the RNA chaperone Hfq drives sRNA competition and release of target RNA.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Panel 5: Microbiology and immunology panel.Otolaryngology--head and neck surgery : official journal of American Academy of Otolaryngology-Head and Neck Surgery · 2013
    Review
  11. Article
  12. Hfq and its constellation of RNA.Nature reviews. Microbiology · 2011
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Molecular aspects of Moraxella catarrhalis pathogenesis.Microbiology and molecular biology reviews : MMBR · 2009
    Review
  18. Article
  19. 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

7 authors at 2 institutions in 2 countries.

Ahmed S AttiaDepartment of Microbiology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9048, USA.
Jennifer L Sedillo
Wei Wang
Wei Liu
Chad A Brautigam
Wade Winkler
Eric J Hansen
The University of Texas Southwestern Medical Center · USCairo University · EG

Funding

SURFACE PROTEINS OF MORAXELLA CATARRHALISR01AI036344 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI HANSEN, ERIC JOHN · 1996 to 2013
$3.6M
NIAID NIH HHS AI36344NIAID NIH HHS R01 AI036344
6 · The paper itself

Abstract

The Hfq protein is recognized as a global regulatory molecule that facilitates certain RNA-RNA interactions in bacteria. BLAST analysis identified a 630-nucleotide open reading frame in the genome of Moraxella catarrhalis ATCC 43617 that was highly conserved among M. catarrhalis strains and which encoded a predicted protein with significant homology to the Hfq protein of Escherichia coli. This protein, containing 210 amino acids, was more than twice as large as the Hfq proteins previously described for other bacteria. The C-terminal half of the M. catarrhalis Hfq protein was very hydrophilic and contained two different types of amino acid repeats. A mutation in the M. catarrhalis hfq gene affected both the growth rate of this organism and its sensitivity to at least two different types of stress in vitro. Provision of the wild-type M. catarrhalis hfq gene in trans eliminated these phenotypic differences in the hfq mutant. This M. catarrhalis hfq mutant exhibited altered expression of some cell envelope proteins relative to the wild-type parent strain and also had a growth advantage in a continuous flow biofilm system. The presence of the wild-type M. catarrhalis hfq gene in trans in an E. coli hfq mutant fully reversed the modest growth deficiency of this E. coli mutant and partially reversed the stress sensitivity of this E. coli mutant to methyl viologen. The use of an electrophoretic mobility shift assay showed that this M. catarrhalis Hfq protein could bind RNA derived from a gene whose expression was altered in the M. catarrhalis hfq mutant.

Indexed as

Amino Acid SequenceBiofilmsEscherichia coliGene Expression Regulation, BacterialGenetic Complementation TestHost Factor 1 ProteinMolecular Sequence DataMoraxella catarrhalisMutationProtein BindingRNAHost Factor 1 ProteinRNA

Identifiers

PMID18362134
PMCPMC2423088
OpenAlexW2152606930

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.