Evidence map›Paper›PMID 32467158›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Dynamic competition for hexon binding between core protein VII and lytic protein VI promotes adenovirus maturation and entry.

Mercedes Hernando-Pérez, Natalia Martín-González, Marta Pérez-Illana, Maarit Suomalainen, Gabriela N Condezo, Philomena Ostapchuk, José Gallardo, Margarita Menéndez, Urs F Greber, Patrick Hearing and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

25 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Mysteries of adenovirus packaging.Journal of virology · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Label-free microscopy for virus infections.Microscopy (Oxford, England) · 2023
    Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review
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

12 authors at 4 institutions in 3 countries.

Mercedes Hernando-PérezDepartment of Macromolecular Structures, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, 28049 Madrid, Spain.ORCID 0000-0002-5875-5620
Natalia Martín-GonzálezDepartment of Condensed Matter Physics, Universidad Autónoma de Madrid, 28049 Madrid, Spain.
Marta Pérez-IllanaDepartment of Macromolecular Structures, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, 28049 Madrid, Spain.ORCID 0000-0003-3659-478X
Maarit SuomalainenDepartment of Molecular Life Sciences, University of Zurich, CH-8057 Zurich, Switzerland.ORCID 0000-0002-3276-3008
Gabriela N CondezoDepartment of Macromolecular Structures, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, 28049 Madrid, Spain.ORCID 0000-0003-2884-0661
Philomena OstapchukDepartment of Microbiology and Immunology, Renaissance School of Medicine, Stony Brook University, Stony Brook, NY 11794-5222.
José GallardoDepartment of Macromolecular Structures, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, 28049 Madrid, Spain.
Margarita MenéndezInstituto de Química Física Rocasolano, Consejo Superior de Investigaciones Cientificas, 28006 Madrid, Spain.ORCID 0000-0002-5258-9959
Urs F GreberDepartment of Molecular Life Sciences, University of Zurich, CH-8057 Zurich, Switzerland.ORCID 0000-0003-2278-120X
Patrick HearingDepartment of Microbiology and Immunology, Renaissance School of Medicine, Stony Brook University, Stony Brook, NY 11794-5222.
Pedro J de PabloDepartment of Condensed Matter Physics, Universidad Autónoma de Madrid, 28049 Madrid, Spain.ORCID 0000-0003-2386-3186
Carmen San MartínDepartment of Macromolecular Structures, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, 28049 Madrid, Spain; carmen@cnb.csic.es.ORCID 0000-0001-9799-175X
Consejo Superior de Investigaciones Científicas · ESStony Brook School · USUniversidad Autónoma de Madrid · ESUniversity of Zurich · CH

Funding

Regulation of Nuclear Signaling Pathways by the Adenovirus E4-ORF3 ProteinR01CA122677 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI HEARING, PATRICK · 2007 to 2022
$5.2M
Role of Adenovirus Core Proteins in Innate Signaling and Viral Genome PackagingR21AI102577 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI HEARING, PATRICK · 2012 to 2013
$418k
NCI NIH HHS R01 CA122677NIAID NIH HHS R21 AI102577
6 · The paper itself

Abstract

Adenovirus minor coat protein VI contains a membrane-disrupting peptide that is inactive when VI is bound to hexon trimers. Protein VI must be released during entry to ensure endosome escape. Hexon:VI stoichiometry has been uncertain, and only fragments of VI have been identified in the virion structure. Recent findings suggest an unexpected relationship between VI and the major core protein, VII. According to the high-resolution structure of the mature virion, VI and VII may compete for the same binding site in hexon; and noninfectious human adenovirus type 5 particles assembled in the absence of VII (Ad5-VII-) are deficient in proteolytic maturation of protein VI and endosome escape. Here we show that Ad5-VII- particles are trapped in the endosome because they fail to increase VI exposure during entry. This failure was not due to increased particle stability, because capsid disruption happened at lower thermal or mechanical stress in Ad5-VII- compared to wild-type (Ad5-wt) particles. Cryoelectron microscopy difference maps indicated that VII can occupy the same binding pocket as VI in all hexon monomers, strongly arguing for binding competition. In the Ad5-VII- map, density corresponding to the immature amino-terminal region of VI indicates that in the absence of VII the lytic peptide is trapped inside the hexon cavity, and clarifies the hexon:VI stoichiometry conundrum. We propose a model where dynamic competition between proteins VI and VII for hexon binding facilitates the complete maturation of VI, and is responsible for releasing the lytic protein from the hexon cavity during entry and stepwise uncoating.

Indexed as

Virus AssemblyVirus InternalizationAdenoviruses, HumanCryoelectron MicroscopyHumansNucleocapsid ProteinsProtein BindingProtein DomainsNucleocapsid ProteinsadenovirusDNA virusvirus assemblyvirus entryvirus maturation

Identifiers

PMID32467158
PMCPMC7306765
OpenAlexW3032063331

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.