Evidence map›Paper›PMID 25053840›Full record

ArticleNucleic acids research2014

Major capsid reinforcement by a minor protein in herpesviruses and phage.

Udom Sae-Ueng, Ting Liu, Carlos Enrique Catalano, Jamie B Huffman, Fred L Homa, Alex Evilevitch

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

30 citing papers in PubMed, 52 citations in OpenAlex.

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  8. Intranuclear HSV-1 DNA ejection induces major mechanical transformations suggesting mechanoprotection of nucleus integrity.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

6 authors at 3 institutions in 2 countries.

Udom Sae-UengDepartment of Physics, Carnegie Mellon University, Pittsburgh, PA 15213, USA.
Ting LiuDepartment of Physics, Carnegie Mellon University, Pittsburgh, PA 15213, USA.
Carlos Enrique CatalanoDepartment of Medicinal Chemistry, University of Washington School of Pharmacy, H172 Health Sciences Building, Box 357610, Seattle, WA 98195, USA.
Jamie B HuffmanDepartment of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.
Fred L HomaDepartment of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.
Alex EvilevitchDepartment of Physics, Carnegie Mellon University, Pittsburgh, PA 15213, USA Department of Biochemistry and Structural Biology, Lund University, Box 124, Lund, Sweden alexe@cmu.edu.
Carnegie Mellon University · USUniversity of Pittsburgh · USUniversity of Washington · US

Funding

Structure and Function of the Herpesvirus Capsid and its DNA-Packaging MachineryR01AI089803 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CONWAY, JAMES F., HOMA, FREDERICK L · 2011 to 2019
$4.0M
Herpes Simplex Virus Capsid Assembly and DNA PackagingR01AI060836 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HOMA, FREDERICK L · 2006 to 2010
$1.6M
Herpes Simples Virus Capsid Assembly and DNA PackagingR56AI060836 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HOMA, FREDERICK L · 2011 to 2011
$379k
NIAID NIH HHS AI060836NIAID NIH HHS R01 AI089803
6 · The paper itself

Abstract

Herpes simplex type 1 virus (HSV-1) and bacteriophage λ capsids undergo considerable structural changes during self-assembly and DNA packaging. The initial steps of viral capsid self-assembly require weak, non-covalent interactions between the capsid subunits to ensure free energy minimization and error-free assembly. In the final stages of DNA packaging, however, the internal genome pressure dramatically increases, requiring significant capsid strength to withstand high internal genome pressures of tens of atmospheres. Our data reveal that the loosely formed capsid structure is reinforced post-assembly by the minor capsid protein UL25 in HSV-1 and gpD in bacteriophage λ. Using atomic force microscopy nano-indentation analysis, we show that the capsid becomes stiffer upon binding of UL25 and gpD due to increased structural stability. At the same time the force required to break the capsid increases by ∼70% for both herpes and phage. This demonstrates a universal and evolutionarily conserved function of the minor capsid protein: facilitating the retention of the pressurized viral genome in the capsid. Since all eight human herpesviruses have UL25 orthologs, this discovery offers new opportunities to interfere with herpes replication by disrupting the precise force balance between the encapsidated DNA and the capsid proteins crucial for viral replication.

Indexed as

Virus AssemblyAnimalsBacteriophage lambdaCapsidCapsid ProteinsChlorocebus aethiopsGlycoproteinsHerpesvirus 1, HumanVero CellsViral ProteinsCapsid ProteinsDNA cleavage and packaging proteins, HerpesvirusGlycoproteinsgpD protein, lambda phageViral Proteins

Identifiers

PMID25053840
PMCPMC4132744
OpenAlexW2166560113

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.