Evidence map›Paper›PMID 21873404›Full record

ArticleMicrobiology (Reading, England)2011

Structure-function analysis of HsiF, a gp25-like component of the type VI secretion system, in Pseudomonas aeruginosa.

Nadine S Lossi, Rana Dajani, Paul Freemont, Alain Filloux

Open access · greenAbstract read
In one paragraph

Article in Microbiology (Reading, England), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.2field-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

35 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. The Anti-Listeria Activity ofPathogens (Basel, Switzerland) · 2023
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  17. Review
  18. Type VI secretion system: secretion by a contractile nanomachine.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015
    Review
  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 at 1 institution in 1 country.

Nadine S LossiCentre for Molecular Microbiology and Infection (CMMI), Division of Cell and Molecular Biology, Imperial College London, London SW7 2AZ, UK.
Rana DajaniCentre for Molecular Microbiology and Infection (CMMI), Division of Cell and Molecular Biology, Imperial College London, London SW7 2AZ, UK.
Paul FreemontDivision of Molecular Biosciences, Imperial College London, London SW7 2AZ, UK.
Alain FillouxCentre for Molecular Microbiology and Infection (CMMI), Division of Cell and Molecular Biology, Imperial College London, London SW7 2AZ, UK.
Imperial College London · GB

Funding

Medical Research Council G0800171Medical Research Council G0800171/ID86344Wellcome TrustWellcome Trust WT091939
6 · The paper itself

Abstract

Bacterial pathogens use a range of protein secretion systems to colonize their host. One recent addition to this arsenal is the type VI secretion system (T6SS), which is found in many Gram-negative bacteria. The T6SS involves 12-15 components, including a ClpV-like AAA(+) ATPase. Moreover, the VgrG and Hcp components have been proposed to form a puncturing device, based on structural similarity to the tail spike components gp5/gp27 and the tail tube component gp19 of the T4 bacteriophage, respectively. Another T6SS component shows similarity to a T4 phage protein, namely gp25. The gp25 protein has been proposed to have lysozyme activity. Other T6SS components do not exhibit obvious similarity to characterized T4 phage components. The genome of Pseudomonas aeruginosa contains three T6SS gene clusters. In each cluster a gene encoding a putative member of the gp25-like protein family was identified, which we called HsiF. We confirmed this similarity by analysing the structure of the P. aeruginosa HsiF proteins using secondary and tertiary structure prediction tools. We demonstrated that HsiF1 is crucial for the T6SS-dependent secretion of Hcp and VgrG. Importantly, lysozyme activity of HsiF proteins was not detectable, and we related this observation to the demonstration that HsiF1 localizes to the cytoplasm of P. aeruginosa. Finally, our data showed that a conserved glutamate, predicted to be required for proper HsiF folding, is essential for its function. In conclusion, our data confirm the central role of HsiF in the T6SS mechanism, provide information on the predicted HsiF structure, and call for reconsideration of the function of gp25-like proteins.

Indexed as

DNA Mutational AnalysisAmino Acid SequenceMembrane Transport ProteinsModels, MolecularMolecular Sequence DataMultigene FamilyProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryPseudomonas aeruginosaSequence AlignmentVirulence FactorsMembrane Transport ProteinsVirulence Factors

Identifiers

PMID21873404
PMCPMC3352280
OpenAlexW2128755796

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.