Evidence map›Paper›PMID 24347545›Full record

ArticleeLife2013

A new topology of the HK97-like fold revealed in Bordetella bacteriophage by cryoEM at 3.5 A resolution.

Xing Zhang, Huatao Guo, Lei Jin, Elizabeth Czornyj, Asher Hodes, Wong H Hui, Angela W Nieh, Jeff F Miller, Z Hong Zhou

Erratum issuedAbstract read
In one paragraph

Article in eLife, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026
    Review
  2. Article
  3. Cryo-EM structure of cyanopodophage A4 reveals a pentameric pre-ejectosome in the double-stabilized capsid.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. A Capsid Structure ofViruses · 2022
    Article
  11. Predicting the capsid architecture of phages from metagenomic data.Computational and structural biotechnology journal · 2022
    Article
  12. Capsid Structure ofJournal of virology · 2021
    Article
  13. Article
  14. Cryo-EM structure ofProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. The Human Gut Phageome: Origins and Roles in the Human Gut Microbiome.Frontiers in cellular and infection microbiology · 2021
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Evolving a Peptide: Library Platforms and Diversification Strategies.International journal of molecular sciences · 2019
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Xing ZhangCalifornia NanoSystems Institute, University of California, Los Angeles, Los Angeles, United States.
Huatao Guo
Lei Jin
Elizabeth Czornyj
Asher Hodes
Wong H Hui
Angela W Nieh
Jeff F Miller
Z Hong Zhou

Funding

High-Resolution CryoEM Reconstruction of Large ComplexesR01GM071940 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI ZHOU, Z HONG · 2006 to 2025
$5.0M
Diversity-Generation and Variable Protein Displays in Pathogens and PhageR01AI096838 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI GHOSH, PARTHO, MILLER, JEFFERY F. · 2012 to 2016
$2.7M
HIGH-END CRYOEM INSTRUMENT FOR UCLA ELECTRON IMAGING CTR FOR NANOMACHINES: AIDSS10RR023057 · NCRR · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI ZHOU, Z HONG · 2006 to 2006
$1.6M
STRUCTURAL STUDIES OF HUMAN CYTOMEGALOVIRUSR01AI046420 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI ZHOU, Z HONG · 2000 to 2004
$1.1M
NCRR NIH HHS S10 RR023057NIAID NIH HHS AI046420NIAID NIH HHS AI069838NIAID NIH HHS R01 AI046420NIAID NIH HHS R01 AI096838NIGMS NIH HHS GM071940NIGMS NIH HHS R01 GM071940
6 · The paper itself

Abstract

Bacteriophage BPP-1 infects and kills Bordetella species that cause whooping cough. Its diversity-generating retroelement (DGR) provides a naturally occurring phage-display system, but engineering efforts are hampered without atomic structures. Here, we report a cryo electron microscopy structure of the BPP-1 head at 3.5 Å resolution. Our atomic model shows two of the three protein folds representing major viral lineages: jellyroll for its cement protein (CP) and HK97-like ('Johnson') for its major capsid protein (MCP). Strikingly, the fold topology of MCP is permuted non-circularly from the Johnson fold topology previously seen in viral and cellular proteins. We illustrate that the new topology is likely the only feasible alternative of the old topology. β-sheet augmentation and electrostatic interactions contribute to the formation of non-covalent chainmail in BPP-1, unlike covalent inter-protein linkages of the HK97 chainmail. Despite these complex interactions, the termini of both CP and MCP are ideally positioned for DGR-based phage-display engineering. DOI: http://dx.doi.org/10.7554/eLife.01299.001.

Indexed as

Amino Acid SequenceBacteriophagesBordetellaCryoelectron MicroscopyElectrophoresis, Polyacrylamide GelMass SpectrometryModels, MolecularMolecular Sequence DataProtein ConformationViral ProteinsViral Proteinsatomic resolutionCryoEMfold topologynon-covalent chainmailphage-display

Identifiers

PMID24347545
PMCPMC3863775

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.