Evidence map›Paper›PMID 26109065›Full record

ArticleThe Journal of biological chemistry2015

The Tubular Sheaths Encasing Methanosaeta thermophila Filaments Are Functional Amyloids.

Morten S Dueholm, Poul Larsen, Kai Finster, Marcel R Stenvang, Gunna Christiansen, Brian S Vad, Andreas Bøggild, Daniel E Otzen, Per Halkjær Nielsen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

26 citing papers in PubMed, 45 citations in OpenAlex.

  1. The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  2. Review
  3. Mechanisms of microbial co-aggregation in mixed anaerobic cultures.Applied microbiology and biotechnology · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Symbiosis betweenmBio · 2022
    Article
  8. Article
  9. Review
  10. Review
  11. The biofilm adhesion protein Aap fromThe Journal of biological chemistry · 2020
    Article
  12. Article
  13. Functional Amyloids.Cold Spring Harbor perspectives in biology · 2019
    Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Review
  19. The Sheaths ofFrontiers in microbiology · 2018
    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

9 authors at 2 institutions in 5 countries.

Morten S DueholmFrom the Center for Microbial Communities, Department of Chemistry and Biosciences, Aalborg University, 9220 Aalborg, Denmark.ORCID http://orcid.org/0000-0003-4135-2670
Poul LarsenFrom the Center for Microbial Communities, Department of Chemistry and Biosciences, Aalborg University, 9220 Aalborg, Denmark.
Kai Finsterthe Department of Biosciences.
Marcel R Stenvangthe Interdisciplinary Nanoscience Center (iNANO) and Center for Insoluble Protein Structures (inSPIN), the Department of Molecular Biology and Genetics, and.
Gunna Christiansenthe Department of Biomedicine, Aarhus University, 8000 Aarhus, Denmark.
Brian S Vadthe Interdisciplinary Nanoscience Center (iNANO) and Center for Insoluble Protein Structures (inSPIN), the Department of Molecular Biology and Genetics, and.
Andreas Bøggildthe Department of Molecular Biology and Genetics, and.
Daniel E Otzenthe Interdisciplinary Nanoscience Center (iNANO) and Center for Insoluble Protein Structures (inSPIN), the Department of Molecular Biology and Genetics, and.
Per Halkjær NielsenFrom the Center for Microbial Communities, Department of Chemistry and Biosciences, Aalborg University, 9220 Aalborg, Denmark, phn@bio.aau.dk.
Aarhus University · DKAalborg University · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Archaea are renowned for their ability to thrive in extreme environments, although they can be found in virtually all habitats. Their adaptive success is linked to their unique cell envelopes that are extremely resistant to chemical and thermal denaturation and that resist proteolysis by common proteases. Here we employ amyloid-specific conformation antibodies and biophysical techniques to show that the extracellular cell wall sheaths encasing the methanogenic archaea Methanosaeta thermophila PT are functional amyloids. Depolymerization of sheaths and subsequent MS/MS analyses revealed that the sheaths are composed of a single major sheath protein (MspA). The amyloidogenic nature of MspA was confirmed by in vitro amyloid formation of recombinant MspA under a wide range of environmental conditions. This is the first report of a functional amyloid from the archaeal domain of life. The amyloid nature explains the extreme resistance of the sheath, the elastic properties that allow diffusible substrates to penetrate through expandable hoop boundaries, and how the sheaths are able to split and elongate outside the cell. The archaeal sheath amyloids do not share homology with any of the currently known functional amyloids and clearly represent a new function of the amyloid protein fold.

Indexed as

AmyloidMethanosarcinalesMicroscopy, Electron, TransmissionTandem Mass SpectrometryAmyloidamyloidarchaeacell wallfunctional amyloidmethanogenprotein foldingsheathstructure-function

Identifiers

PMID26109065
PMCPMC4536462
OpenAlexW1911999476

What OpenQuestion holds

Textmetadata
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.