Evidence map›Paper›PMID 31263148›Full record

ArticleScientific reports2019

The type VI secretion system protein AsaA in Acinetobacter baumannii is a periplasmic protein physically interacting with TssM and required for T6SS assembly.

Lei Li, Yi-Nuo Wang, Hong-Bing Jia, Ping Wang, Jun-Fang Dong, Juan Deng, Feng-Min Lu, Qing-Hua Zou

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
0.8field-weighted citation impact, top 28% 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

13 citing papers in PubMed, 1 synthesis or guideline pooled it, 17 citations in OpenAlex.

  1. Drug-resistantClinical microbiology reviews · 2025
    Pooled it
  2. Review
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  10. Uncovering the Secretion Systems ofAntibiotics (Basel, Switzerland) · 2023
    Review
  11. Article
  12. Article
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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

8 authors at 2 institutions in 1 country.

Lei LiDepartment of Microbiology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, 100191, China.
Yi-Nuo WangNational Center for Health Professions Education Development, Beijing, 100191, China.
Hong-Bing JiaDepartment of clinical laboratory, China-Japan friendship hospital, Beijing, China.
Ping WangDepartment of Microbiology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, 100191, China.
Jun-Fang DongDepartment of Microbiology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, 100191, China.
Juan DengDepartment of Microbiology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, 100191, China.
Feng-Min LuDepartment of Microbiology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, 100191, China. fengmin.lu@hsc.pku.edu.cn.
Qing-Hua ZouDepartment of Microbiology, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, 100191, China. zouqinghua@bjmu.edu.cn.
Peking University · CNChina-Japan Friendship Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Type VI secretion system (T6SS) is described as a macromolecular secretion machine that is utilized for bacterial competition. The gene clusters encoding T6SS are composed of core tss genes and tag genes. However, the clusters differ greatly in different pathogens due to the great changes accumulated during the long-term evolution. In this work, we identified a novel hypothetical periplasmic protein designated as AsaA which is encoded by the first gene of the T6SS cluster in the genus Acinetobacter. By constructing asaA mutant, we delineated its relative contributions to bacterial competition and secretion of T6SS effector Hcp. Subsequently, we studied the localization of AsaA and potential proteins that may have interactions with AsaA. Our results showed that AsaA in Acinetobacter baumannii (A. baumannii) localized in the bacterial periplasmic space. Results based on bacterial two-hybrid system and protein pull-down assays indicated that it was most likely to affect the assembly or stability of T6SS by interacting with the T6SS core protein TssM. Collectively, our findings of AsaA is most likely a key step in understanding of the T6SS functions in A. baumannii.

Indexed as

Acinetobacter baumanniiBacterial ProteinsGene Knockout TechniquesMembrane ProteinsMultigene FamilyPeriplasmPeriplasmic ProteinsPlasmidsProtein BindingType VI Secretion SystemsBacterial ProteinsMembrane ProteinsPeriplasmic ProteinsType VI Secretion Systems

Identifiers

PMID31263148
PMCPMC6602968
OpenAlexW2956153130

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.