Evidence map›Paper›PMID 30254227›Full record

ArticleNature communications2018

Vibrio parahaemolyticus RhsP represents a widespread group of pro-effectors for type VI secretion systems.

Nan Jiang, Le Tang, Ruiqiang Xie, Zhi Li, Brianne Burkinshaw, Xiaoye Liang, Dylan Sosa, L Aravind, Tao Dong, Dapeng Zhang and 1 more

RetractedAbstract readRetracted Publication
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Two DsbA Proteins Are Important forFrontiers in microbiology · 2019
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors.

Nan JiangFaculty of Health Sciences, University of Macau, Macau SAR, China.
Le TangDepartment of Ecosystem and Public Health, University of Calgary, Calgary, AB, T2N 4Z6, Canada.
Ruiqiang XieFaculty of Health Sciences, University of Macau, Macau SAR, China.
Zhi LiFaculty of Health Sciences, University of Macau, Macau SAR, China.
Brianne BurkinshawDepartment of Ecosystem and Public Health, University of Calgary, Calgary, AB, T2N 4Z6, Canada.
Xiaoye LiangState Key Laboratory of Microbial Metabolism, Joint International Laboratory on Metabolic and Developmental Sciences, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, 200240, China.
Dylan SosaProgram of Bioinformatics and Computational Biology, College of Arts and Sciences, Saint Louis University, Saint Louis, MO, 63103, USA.
L AravindNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD, 20894, USA.
Tao DongDepartment of Ecosystem and Public Health, University of Calgary, Calgary, AB, T2N 4Z6, Canada. tdong@ucalgary.ca.ORCID http://orcid.org/0000-0003-3557-1850
Dapeng ZhangProgram of Bioinformatics and Computational Biology, College of Arts and Sciences, Saint Louis University, Saint Louis, MO, 63103, USA. dapeng.zhang@slu.edu.
Jun ZhengFaculty of Health Sciences, University of Macau, Macau SAR, China. junzheng@umac.mo.ORCID http://orcid.org/0000-0001-6329-4518

Funding

Fundo para o Desenvolvimento das Ciências e da Tecnologia (Science and Technology Development Fund) FDCT/0058/2018/A2Fundo para o Desenvolvimento das Ciências e da Tecnologia (Science and Technology Development Fund) FDCT/066/2015/A2Universidade de Macau (University of Macau) MYRG2016-00073-FHSUniversidade de Macau (University of Macau) MYRG2016-00199-FHS
6 · The paper itself

Abstract

Type VI secretion systems (T6SSs) translocate effector proteins, such as Rhs toxins, to eukaryotic cells or prokaryotic competitors. All T6SS Rhs-type effectors characterized thus far contain a PAAR motif or a similar structure. Here, we describe a T6SS-dependent delivery mechanism for a subset of Rhs proteins that lack a PAAR motif. We show that the N-terminal Rhs domain of protein RhsP (or VP1517) from Vibrio parahaemolyticus inhibits the activity of the C-terminal DNase domain. Upon auto-proteolysis, the Rhs fragment remains inside the cells, and the C-terminal region interacts with PAAR2 and is secreted by T6SS2; therefore, RhsP acts as a pro-effector. Furthermore, we show that RhsP contributes to the control of certain "social cheaters" (opaR mutants). Genes encoding proteins with similar Rhs and PAAR-interacting domains, but diverse C-terminal regions, are widely distributed among Vibrio species.

Indexed as

Amino Acid MotifsAmino Acid SequenceBacterial ProteinsBacterial ToxinsBinding SitesMutagenesis, Site-DirectedProtein BindingProtein DomainsSequence Homology, Amino AcidType VI Secretion SystemsVibrio parahaemolyticusBacterial ProteinsBacterial ToxinsType VI Secretion Systems

Identifiers

PMID30254227
PMCPMC6156420

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.