Evidence map›Paper›PMID 31110358›Full record

ArticleNature microbiology2019

An extensively glycosylated archaeal pilus survives extreme conditions.

Fengbin Wang, Virginija Cvirkaite-Krupovic, Mark A B Kreutzberger, Zhangli Su, Guilherme A P de Oliveira, Tomasz Osinski, Nicholas Sherman, Frank DiMaio, Joseph S Wall, David Prangishvili and 2 more

Abstract read
In one paragraph

Article in Nature microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.0field-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

39 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Cytochrome nanowires under electron microscopy.Emerging topics in life sciences · 2026
    Review
  3. Article
  4. Article
  5. Tat-dependent bundling pilus of a halophilic archaeon assembles by a strand donation mechanism and facilitates biofilm formation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
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  8. Article
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  11. A Collagen Triple Helix without the Super Helical Twist.bioRxiv : the preprint server for biology · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The evolution of archaeal flagellar filaments.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Article
  18. Article
  19. 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

12 authors at 4 institutions in 2 countries.

Fengbin WangDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA, USA.ORCID http://orcid.org/0000-0003-1008-663X
Virginija Cvirkaite-KrupovicUnité de Biologie Moléculaire du Gène chez les Extrêmophiles, Institut Pasteur, Paris, France.
Mark A B KreutzbergerDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA, USA.
Zhangli SuDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA, USA.
Guilherme A P de OliveiraDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA, USA.ORCID http://orcid.org/0000-0002-0063-5888
Tomasz OsinskiDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA, USA.
Nicholas ShermanDepartment of Microbiology, Immunology and Cancer Biology, University of Virginia, Charlottesville, VA, USA.
Frank DiMaioDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
Joseph S WallBrookhaven National Laboratory, Upton, NY, USA.
David PrangishviliUnité de Biologie Moléculaire du Gène chez les Extrêmophiles, Institut Pasteur, Paris, France.
Mart KrupovicUnité de Biologie Moléculaire du Gène chez les Extrêmophiles, Institut Pasteur, Paris, France. krupovic@pasteur.fr.ORCID http://orcid.org/0000-0001-5486-0098
Edward H EgelmanDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA, USA. egelman@virginia.edu.ORCID http://orcid.org/0000-0003-4844-5212
University of Virginia · USInstitut Pasteur · FRBrookhaven National Laboratory · USUniversity of Washington · US

Funding

Women's Oncology Program - WONP30CA044579 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI Thomas P. Loughran · 1987 to 2026
$72.1M
Cryo-EM of Helical Protein and Nucleoprotein Polymers at Near Atomic ResolutionR35GM122510 · NIGMS · UNIVERSITY OF VIRGINIA · PI EDWARD H. EGELMAN · 2017 to 2026
$7.3M
Protein structure determination from low-resolution experimental dataR01GM123089 · NIGMS · UNIVERSITY OF WASHINGTON · PI DIMAIO, FRANK P · 2017 to 2025
$2.6M
Molecular Electron Microscopy Core Facility ImprovementsG20RR031199 · NCRR · UNIVERSITY OF VIRGINIA · PI SHUPNIK, MARGARET A · 2010 to 2010
$2.0M
300 keV Liquid Helium Robotic MicroscopeS10RR025067 · NCRR · UNIVERSITY OF VIRGINIA · PI EGELMAN, EDWARD H. · 2009 to 2009
$2.0M
Training in Molecular BiophysicsT32GM080186 · NIGMS · UNIVERSITY OF VIRGINIA · PI NAKAMOTO, ROBERT K. · 2008 to 2019
$1.5M
Direct Electron Detector for a Titan Krios Robotic Electron Cryo-MicroscopeS10OD018149 · OD · UNIVERSITY OF VIRGINIA · PI EGELMAN, EDWARD H., YEAGER, MARK JAY · 2014 to 2014
$500k
NCI NIH HHS P30 CA044579NCRR NIH HHS G20 RR031199NCRR NIH HHS S10 RR025067NIGMS NIH HHS R01 GM123089NIGMS NIH HHS R35 GM122510NIGMS NIH HHS T32 GM080186NIH HHS S10 OD018149
6 · The paper itself

Abstract

Pili on the surface of Sulfolobus islandicus are used for many functions, and serve as receptors for certain archaeal viruses. The cells grow optimally at pH 3 and ~80 °C, exposing these extracellular appendages to a very harsh environment. The pili, when removed from cells, resist digestion by trypsin or pepsin, and survive boiling in sodium dodecyl sulfate or 5 M guanidine hydrochloride. We used electron cryo-microscopy to determine the structure of these filaments at 4.1 Å resolution. An atomic model was built by combining the electron density map with bioinformatics without previous knowledge of the pilin sequence-an approach that should prove useful for assemblies where all of the components are not known. The atomic structure of the pilus was unusual, with almost one-third of the residues being either threonine or serine, and with many hydrophobic surface residues. While the map showed extra density consistent with glycosylation for only three residues, mass measurements suggested extensive glycosylation. We propose that this extensive glycosylation renders these filaments soluble and provides the remarkable structural stability. We also show that the overall fold of the archaeal pilin is remarkably similar to that of archaeal flagellin, establishing common evolutionary origins.

Indexed as

ArchaeaArchaeal ProteinsCryoelectron MicroscopyFimbriae ProteinsGlycosylationHydrophobic and Hydrophilic InteractionsModels, MolecularPepsin AProtein ConformationProtein StabilitySequence Analysis, ProteinSulfolobusTrypsinArchaeal ProteinsFimbriae ProteinsPepsin ATrypsin

Identifiers

PMID31110358
PMCPMC6656605
OpenAlexW2946313727

What OpenQuestion holds

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Registered trials

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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.