Evidence map›Paper›PMID 31075115›Full record

ArticlePloS one2019

Environmental factors influence the Haloferax volcanii S-layer protein structure.

Thiago Rodrigues-Oliveira, Amanda Araújo Souza, Ricardo Kruger, Bernhard Schuster, Sonia Maria de Freitas, Cynthia Maria Kyaw

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. DPANN symbiont ofiScience · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Electrochemical Biosensors Based on S-Layer Proteins.Sensors (Basel, Switzerland) · 2020
    Review
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

6 authors at 2 institutions in 2 countries.

Thiago Rodrigues-OliveiraDepartment of Cell Biology, Institute of Biological Sciences, University of Brasília, Brasília, Brazil.
Amanda Araújo SouzaDepartment of Cell Biology, Institute of Biological Sciences, University of Brasília, Brasília, Brazil.
Ricardo KrugerDepartment of Cell Biology, Institute of Biological Sciences, University of Brasília, Brasília, Brazil.
Bernhard SchusterDepartment of NanoBiotechnology, Institute for Synthetic Bioarchitectures, University of Natural Resources and Life Sciences, Vienna, Austria.
Sonia Maria de FreitasDepartment of Cell Biology, Institute of Biological Sciences, University of Brasília, Brasília, Brazil.
Cynthia Maria KyawDepartment of Cell Biology, Institute of Biological Sciences, University of Brasília, Brasília, Brazil.ORCID 0000-0002-0876-9717
Universidade de Brasília · BRBOKU University · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

S-layers commonly cover archaeal cell envelopes and are composed of proteins that self-assemble into a paracrystalline surface structure. Despite their detection in almost all archaea, there are few reports investigating the structural properties of these proteins, with no reports exploring this topic for halophilic S-layers. The objective of the present study was to investigate the secondary and tertiary organization of the Haloferax volcanii S-layer protein. Such investigations were performed using circular dichroism, fluorescence spectroscopy, dynamic light scattering and transmission electron microscopy. The protein secondary structure is centered on β-sheets and is affected by environmental pH, with higher disorder in more alkaline conditions. The pH can also affect the protein's tertiary structure, with higher tryptophan side-chain exposure to the medium under the same conditions. The concentrations of Na, Mg and Ca ions in the environment also affect the protein structures, with small changes in α-helix and β-sheet content, as well as changes in tryptophan side chain exposure. These changes in turn influence the protein's functional properties, with cell envelope preparations revealing striking differences when in different salt conditions. Thermal denaturation assays revealed that the protein is stable. It has been reported that the S-layer protein N-glycosylation process is affected by external factors and the present study indicates for the first time changes in the protein structure.

Indexed as

Hot TemperatureSalinityHaloferax volcaniiHydrogen-Ion ConcentrationMembrane GlycoproteinsMetalsProtein DenaturationProtein Structure, SecondaryMembrane GlycoproteinsMetalsS-layer proteins

Identifiers

PMID31075115
PMCPMC6607943
OpenAlexW2944537229

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.