Evidence map›Paper›PMID 26079269›Full record

ArticlePloS one2015

Crystal Structure of Hcp from Acinetobacter baumannii: A Component of the Type VI Secretion System.

Federico M Ruiz, Elena Santillana, Mercedes Spínola-Amilibia, Eva Torreira, Esther Culebras, Antonio Romero

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 27 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed, 1 pooled it
3.6field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 1 synthesis or guideline pooled it, 40 citations in OpenAlex.

  1. Drug-resistantClinical microbiology reviews · 2025
    Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. The role of type VI secretion system genes in antibiotic resistance and virulence inFrontiers in cellular and infection microbiology · 2024
    Article
  7. Deciphering the virulence factors, regulation, and immune response toFrontiers in cellular and infection microbiology · 2023
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Phosphorylation of Extracellular Proteins inFrontiers in microbiology · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Crystal structure of the putative cytoplasmic protein STM0279 (Hcp2) from Salmonella typhimurium.Acta crystallographica. Section F, Structural biology communications · 2017
    Article
  20. The Secrets of Acinetobacter Secretion.Trends in microbiology · 2017
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Federico M RuizDepartment of Chemical and Physical Biology, Centro de Investigaciones Biológicas-CSIC, Madrid, Spain.
Elena SantillanaDepartment of Chemical and Physical Biology, Centro de Investigaciones Biológicas-CSIC, Madrid, Spain.
Mercedes Spínola-AmilibiaDepartment of Chemical and Physical Biology, Centro de Investigaciones Biológicas-CSIC, Madrid, Spain.
Eva TorreiraDepartment of Chemical and Physical Biology, Centro de Investigaciones Biológicas-CSIC, Madrid, Spain.
Esther CulebrasDepartment of Clinical Microbiology, Hospital Clínico San Carlos, Madrid, Spain.
Antonio RomeroDepartment of Chemical and Physical Biology, Centro de Investigaciones Biológicas-CSIC, Madrid, Spain.
Centro de Investigaciones Biológicas Margarita Salas · ESHospital Clínico San Carlos · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The type VI secretion system (T6SS) is a bacterial macromolecular machine widely distributed in Gram-negative bacteria, which transports effector proteins into eukaryotic host cells or other bacteria. Membrane complexes and a central tubular structure, which resembles the tail of contractile bacteriophages, compose the T6SS. One of the proteins forming this tube is the hemolysin co-regulated protein (Hcp), which acts as virulence factor, as transporter of effectors and as a chaperone. In this study, we present the structure of Hcp from Acinetobacter baumannii, together with functional and oligomerization studies. The structure of this protein exhibits a tight β barrel formed by two β sheets and flanked at one side by a short α-helix. Six Hcp molecules associate to form a donut-shaped hexamer, as observed in both the crystal structure and solution. These results emphasize the importance of this oligomerization state in this family of proteins, despite the low similarity of sequence among them. The structure presented in this study is the first one for a protein forming part of a functional T6SS from A. baumannii. These results will help us to understand the mechanism and function of this secretion system in this opportunistic nosocomial pathogen.

Indexed as

Acinetobacter baumanniiBacterial ProteinsCrystallography, X-RayModels, MolecularProtein MultimerizationProtein Structure, QuaternaryProtein Structure, SecondaryType VI Secretion SystemsBacterial ProteinsType VI Secretion Systems

Identifiers

PMID26079269
PMCPMC4469607
OpenAlexW1558208010

What OpenQuestion holds

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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.