Evidence map›Paper›PMID 40479047›Full record

ArticleScience advances2025

RBPseg: Toward a complete phage tail fiber structure atlas.

Victor Klein-Sousa, Aritz Roa-Eguiara, Claudia S Kielkopf, Nicholas Sofos, Nicholas M I Taylor

Abstract read
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 1 pooled it
–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

14 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Review
  6. Auxin (Indole-3-acetic acid) modulation of quorum sensing enhances phage susceptibility in Klebsiella pneumoniae.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026
    Article
  7. Article
  8. Review
  9. Computational and structural biotechnology journal · 2026
    Article
  10. Identification of candidate nucleomodulins in ESKAPE bacteria -Frontiers in cellular and infection microbiology · 2026
    Article
  11. Review
  12. Review
  13. Review
  14. 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

5 authors.

Victor Klein-SousaStructural Biology of Molecular Machines Group, Protein Structure & Function Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.ORCID 0000-0002-0430-4330
Aritz Roa-EguiaraStructural Biology of Molecular Machines Group, Protein Structure & Function Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.ORCID 0000-0003-3962-7583
Claudia S KielkopfStructural Biology of Molecular Machines Group, Protein Structure & Function Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.ORCID 0000-0003-1360-4260
Nicholas SofosStructural Biology of Molecular Machines Group, Protein Structure & Function Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.ORCID 0000-0002-7224-3330
Nicholas M I TaylorStructural Biology of Molecular Machines Group, Protein Structure & Function Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.ORCID 0000-0003-0761-4921

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteriophages use receptor-binding proteins (RBPs) to adhere to bacterial hosts, yet their sequence and structural diversity remain poorly understood. Tail fibers, a major class of RBPs, are elongated and flexible trimeric proteins, making their full-length structures difficult to resolve experimentally. Advances in deep learning-based protein structure prediction, such as AlphaFold2-multimer (AF2M) and ESMFold, provide opportunities for studying these challenging proteins. Here, we introduce RBPseg, a method that combines monomeric ESMFold predictions with a structural-based domain identification approach, to divide tail fiber sequences into manageable fractions for high-confidence modeling with AF2M. Using this approach, we generated complete tail fiber models, validated by single-particle cryo-electron microscopy of five fibers from three phages. A structural classification of 67 fibers identified 16 distinct classes and 89 domains, revealing patterns of modularity, convergence, divergence, and domain swapping. Our findings suggest that these structural classes represent at least 24% of the known tail fiber universe, providing key insights into their evolution and functionality.

Indexed as

BacteriophagesViral Tail ProteinsCryoelectron MicroscopyModels, MolecularProtein ConformationViral Tail Proteins

Identifiers

PMID40479047
PMCPMC12143355

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.