Evidence map›Paper›PMID 34074781›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Periscope Proteins are variable-length regulators of bacterial cell surface interactions.

Fiona Whelan, Aleix Lafita, James Gilburt, Clément Dégut, Samuel C Griffiths, Huw T Jenkins, Alexander N St John, Emanuele Paci, James W B Moir, Michael J Plevin and 3 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

  1. Structure of theProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. The long and the short of Periscope Proteins.Biochemical Society transactions · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. 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

13 authors.

Fiona WhelanDepartment of Biology, The University of York, YO10 5DD York, United Kingdom.ORCID 0000-0002-0791-6850
Aleix LafitaEuropean Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Genome Campus, CB10 1SD, United Kingdom.ORCID 0000-0003-1549-3162
James GilburtDepartment of Biology, The University of York, YO10 5DD York, United Kingdom.
Clément DégutDepartment of Biology, The University of York, YO10 5DD York, United Kingdom.ORCID 0000-0003-1644-7432
Samuel C GriffithsDepartment of Biology, The University of York, YO10 5DD York, United Kingdom.ORCID 0000-0002-9257-7354
Huw T JenkinsDepartment of Chemistry, The University of York, YO10 5DD York, United Kingdom.ORCID 0000-0002-3302-6966
Alexander N St JohnAstbury Centre for Structural Molecular Biology, The University of Leeds, LS2 9JT Leeds, United Kingdom.
Emanuele PaciAstbury Centre for Structural Molecular Biology, The University of Leeds, LS2 9JT Leeds, United Kingdom.ORCID 0000-0002-4891-2768
James W B MoirDepartment of Biology, The University of York, YO10 5DD York, United Kingdom.ORCID 0000-0003-2972-5235
Michael J PlevinDepartment of Biology, The University of York, YO10 5DD York, United Kingdom.ORCID 0000-0003-2057-8291
Christoph G BaumannDepartment of Biology, The University of York, YO10 5DD York, United Kingdom.ORCID 0000-0002-8818-972X
Alex BatemanEuropean Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Genome Campus, CB10 1SD, United Kingdom; agb@ebi.ac.uk jennifer.potts@sydney.edu.au.
Jennifer R PottsDepartment of Biology, The University of York, YO10 5DD York, United Kingdom; agb@ebi.ac.uk jennifer.potts@sydney.edu.au.ORCID 0000-0002-1734-6425

Funding

British Heart Foundation FS/07/034/22969British Heart Foundation FS/09/023/27460British Heart Foundation FS/12/36/29588British Heart Foundation PG/17/19/32862Medical Research Council G1001063Medical Research Council MC_PC_15073
6 · The paper itself

Abstract

Changes at the cell surface enable bacteria to survive in dynamic environments, such as diverse niches of the human host. Here, we reveal "Periscope Proteins" as a widespread mechanism of bacterial surface alteration mediated through protein length variation. Tandem arrays of highly similar folded domains can form an elongated rod-like structure; thus, variation in the number of domains determines how far an N-terminal host ligand binding domain projects from the cell surface. Supported by newly available long-read genome sequencing data, we propose that this class could contain over 50 distinct proteins, including those implicated in host colonization and biofilm formation by human pathogens. In large multidomain proteins, sequence divergence between adjacent domains appears to reduce interdomain misfolding. Periscope Proteins break this "rule," suggesting that their length variability plays an important role in regulating bacterial interactions with host surfaces, other bacteria, and the immune system.

Indexed as

Bacterial ProteinsMembrane ProteinsStreptococcus gordoniiBacterial ProteinsMembrane Proteinsbacterial surface proteinsmultidomain proteinsprotein structure

Identifiers

PMID34074781
PMCPMC8201768

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.