Evidence map›Paper›PMID 28238256›Full record

ArticleACS infectious diseases2017

Discovery of a Novel Nitric Oxide Binding Protein and Nitric-Oxide-Responsive Signaling Pathway in Pseudomonas aeruginosa.

Sajjad Hossain, Elizabeth M Boon

Open access · greenAbstract read
In one paragraph

Article in ACS infectious diseases, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

39 citing papers in PubMed, 78 citations in OpenAlex.

  1. Functional organization and regulatory logic of theApplied and environmental microbiology · 2026
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  16. Nitric oxide stimulates type IV MSHA pilus retraction inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Treatment ofFrontiers in microbiology · 2022
    Review
  18. Nitric oxide-secreting probiotics as sustainable bio-cleaners for reverse osmosis membrane systems.Environmental science and pollution research international · 2022
    Review
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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

2 authors at 1 institution in 1 country.

Sajjad HossainGraduate Program in Molecular and Cellular Biology, ‡Department of Chemistry, and §Institute of Chemical Biology & Drug Discovery, Stony Brook University , Stony Brook, New York 11794, United States.
Elizabeth M BoonGraduate Program in Molecular and Cellular Biology, ‡Department of Chemistry, and §Institute of Chemical Biology & Drug Discovery, Stony Brook University , Stony Brook, New York 11794, United States.ORCID 0000-0003-1891-839X
Stony Brook University · US

Funding

The role of NosP in Pseudomonas aeruginosa biofilm developmentR01GM118894 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI ELIZABETH M BOON · 2017 to 2026
$3.0M
NIGMS NIH HHS R01 GM118894
6 · The paper itself

Abstract

Nitric oxide (NO) is a radical diatomic gas molecule that, at low concentrations, plays important signaling roles in both eukaryotes and bacteria. In recent years, it has become evident that bacteria respond to low levels of NO in order to modulate their group behavior. Many bacteria respond via NO ligation to a well-established NO sensor called H-NOX (heme-nitric oxide/oxygen binding domain). Many others, such as Pseudomonas aeruginosa, lack an annotated hnoX gene in their genome yet are able to respond to low levels of NO to disperse their biofilms. This suggests the existence of a previously uncharacterized NO sensor. In this study, we describe the discovery of a novel nitric oxide binding protein (NosP; NO-sensing protein), which is much more widely conserved in bacteria than H-NOX, as well as a novel NO-responsive pathway in P. aeruginosa. We demonstrate that biofilms of a P. aeruginosa mutant lacking components of the NosP pathway lose the ability to disperse in response to NO. Upon cloning, expressing, and purifying NosP, we find it binds heme and ligates to NO with a dissociation rate constant that is comparable to that of other well-established NO-sensing proteins. Moreover, we show that NO-bound NosP is able to regulate the phosphorelay activity of a hybrid histidine kinase that is involved in biofilm regulation in P. aeruginosa. Thus, here, we present evidence of a novel NO-responsive pathway that regulates biofilm in P. aeruginosa.

Indexed as

Gene Expression Regulation, BacterialAdenosine TriphosphateBacterial ProteinsBinding SitesBiofilmsCloning, MolecularEscherichia coliGene ExpressionHemeHistidine KinaseKineticsNitric OxideOperonPlasmidsProtein BindingPseudomonas aeruginosaAdenosine TriphosphateBacterial ProteinsHemeHistidine KinaseNitric OxideRecombinant Proteinsbiofilmnitric oxidenitric oxide-responsive kinasenitric oxide sensornitric oxide signalingNosP

Identifiers

PMID28238256
PMCPMC5468770
OpenAlexW2592128814

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.