Evidence map›Paper›PMID 33188170›Full record

ArticleNature communications2020

S-nitrosylation-mediated activation of a histidine kinase represses the type 3 secretion system and promotes virulence of an enteric pathogen.

Dan Gu, Yibei Zhang, Qiyao Wang, Xiaohui Zhou

Abstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Direct sensing of host ferric iron by an archetype histidine kinase mediates virulence of an enteric pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Antimicrobial resistance ofApplied and environmental microbiology · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

4 authors.

Dan GuDepartment of Pathobiology and Veterinary Science, University of Connecticut, Storrs, 06269, CT, USA.
Yibei ZhangDepartment of Pathobiology and Veterinary Science, University of Connecticut, Storrs, 06269, CT, USA.
Qiyao WangState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237, Shanghai, China.
Xiaohui ZhouDepartment of Pathobiology and Veterinary Science, University of Connecticut, Storrs, 06269, CT, USA. xiaohui.zhou@uconn.edu.ORCID 0000-0003-3205-4743

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vibrio parahaemolyticus is the leading cause of seafood-borne diarrheal diseases. Experimental overproduction of a type 3 secretion system (T3SS1) in this pathogen leads to decreased intestinal colonization, which suggests that T3SS1 repression is required for maximal virulence. However, the mechanisms by which T3SS1 is repressed in vivo are unclear. Here, we show that host-derived nitrite modifies the activity of a bacterial histidine kinase and mediates T3SS1 repression. More specifically, nitrite activates histidine kinase sensor VbrK through S-nitrosylation on cysteine 86, which results in downregulation of the entire T3SS1 operon through repression of its positive regulator exsC. Replacement of cysteine 86 with a serine (VbrK C86S mutant) leads to increased expression of inflammatory cytokines in infected Caco-2 cells. In an infant rabbit model of infection, the VbrK C86S mutant induces a stronger inflammatory response at the early stage of infection, and displays reduced intestinal colonization and virulence at the later stage of infection, in comparison with the parent strain. Our results indicate that the pathogen V. parahaemolyticus perceives nitrite as a host-derived signal and responds by downregulating a proinflammatory factor (T3SS1), thus enhancing intestinal colonization and virulence.

Indexed as

AnaerobiosisAnimalsBacterial ProteinsBase SequenceBinding SitesCaco-2 CellsCytokinesDown-RegulationGene Expression Regulation, BacterialHistidine KinaseHost-Pathogen InteractionsHumansModels, BiologicalNitratesNitritesNitrosationBacterial ProteinsCytokinesHistidine KinaseNitratesNitritesType III Secretion Systems

Identifiers

PMID33188170
PMCPMC7666205

What OpenQuestion holds

Textmetadata
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.