Evidence map›Paper›PMID 15775971›Full record

ArticleThe EMBO journal2005

Crosslinking renders bacteriophage HK97 capsid maturation irreversible and effects an essential stabilization.

Philip D Ross, Naiqian Cheng, James F Conway, Brian A Firek, Roger W Hendrix, Robert L Duda, Alasdair C Steven

Abstract readComparative Study
In one paragraph

Article in The EMBO journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026
    Review
  2. Article
  3. Review
  4. 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
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
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  15. Article
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  17. 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

7 authors.

Philip D RossLaboratory of Molecular Biology, National Institute of Diabetes, Digestive and Kidney Diseases, Bethesda, MD, USA.
Naiqian Cheng
James F Conway
Brian A Firek
Roger W Hendrix
Robert L Duda
Alasdair C Steven

Funding

Structural Biology Of Virus AssemblyZIAAR027002 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI WINGFIELD, PAUL T · 2009 to 2024
$19.2M
ASSEMBLY AND STRUCTURE OF BACTERIOPHAGE LAMBDAR01GM047795 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI DUDA, ROBERT LOUIS · 1991 to 2017
$7.8M
STRUCTURAL BIOLOGY OF VIRUS ASSEMBLYZ01AR027002 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI STEVEN, ALASDAIR C. · 1987 to 2008
$3.0M
NIGMS NIH HHS GM47795NIGMS NIH HHS R01 GM047795
6 · The paper itself

Abstract

In HK97 capsid maturation, structural change ('expansion') is accompanied by formation of covalent crosslinks, connecting residue K169 in the 'E-loop' of each subunit with N356 on another subunit. We show by complementation experiments with the K169Y mutant, which cannot crosslink, that crosslinking is an essential function. The precursor Prohead-II passes through three expansion intermediate (EI) states en route to the end state, Head-II. We investigated the effects of expansion and crosslinking on stability by differential scanning calorimetry of wild-type and K169Y capsids. After expansion, the denaturation temperature (Tp) of K169Y capsids is slightly reduced, indicating that their thermal stability is not enhanced, but crosslinking effects a major stabilization (deltaTp, +11 degrees C). EI-II is the earliest capsid to form crosslinks. Cryo-electron microscopy shows that for both wild-type and K169Y EI-II, most E-loops are in the 'up' position, 30 A from the nearest N356: thus, crosslinking in EI-II represents capture of mobile E-loops in 'down' positions. At pH 4, most K169Y capsids remain as EI-II, whereas wild-type capsids proceed to EI-III, suggesting that crosslink formation drives maturation by a Brownian ratchet mechanism.

Indexed as

Models, MolecularBacteriophagesCalorimetry, Differential ScanningCapsid ProteinsCryoelectron MicroscopyGenetic Complementation TestMutationProtein ConformationProtein SubunitsViral Core ProteinsVirus AssemblyCapsid ProteinsProtein SubunitsViral Core Proteins

Identifiers

PMID15775971
PMCPMC1142538

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.