Evidence map›Paper›PMID 32579107›Full record

ArticleeLife2020

Structural basis for capsid recruitment and coat formation during HSV-1 nuclear egress.

Elizabeth B Draganova, Jiayan Zhang, Z Hong Zhou, Ekaterina E Heldwein

Abstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

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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

4 authors.

Elizabeth B DraganovaDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, United States.ORCID 0000-0003-3697-4774
Jiayan ZhangDepartment of Microbiology, Immunology & Molecular Genetics, University of California, Los Angeles (UCLA), Los Angeles, United States.ORCID 0000-0003-3602-1199
Z Hong ZhouDepartment of Microbiology, Immunology & Molecular Genetics, University of California, Los Angeles (UCLA), Los Angeles, United States.ORCID 0000-0002-8373-4717
Ekaterina E HeldweinDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, United States.ORCID 0000-0003-3113-6958

Funding

Tufts IRACDAK12GM133314 · NIGMS · TUFTS UNIVERSITY BOSTON · PI CLAIRE L MOORE, Jamie Lynn Maguire · 2019 to 2026
$8.4M
West/Midwest Consortium for High-Resolution Cryo Electron MicroscopyU24GM116792 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI AGBANDJE-MCKENNA, MAVIS, DOKLAND, TERJE · 2016 to 2020
$3.0M
Biophysical and structural analysis of the herpesviral nuclear budding machineryR01AI147625 · NIAID · TUFTS UNIVERSITY BOSTON · PI HELDWEIN, EKATERINA · 2019 to 2023
$3.0M
Structural mechanism of membrane remodeling during herpesvirus nuclear egressR01GM111795 · NIGMS · TUFTS UNIVERSITY BOSTON · PI HELDWEIN, EKATERINA · 2014 to 2017
$1.3M
Direct Detection Device for atomic resolution cryoEM of macromolecular complexesS10OD018111 · OD · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI ZHOU, Z HONG · 2014 to 2014
$598k
Structural Dynamics and Regulation of the HSV-1 Nuclear Egress ComplexF32GM126760 · NIGMS · TUFTS UNIVERSITY BOSTON · PI DRAGANOVA, ELIZABETH BENNETT · 2017 to 2018
$116k
Howard Hughes Medical Institute 55108533National Science Foundation DBI-1338135National Science Foundation DMR-1548924NIAID NIH HHS R01 AI147625NIGMS NIH HHS F32 GM126760NIGMS NIH HHS K12 GM133314NIGMS NIH HHS R01 GM111795NIGMS NIH HHS U24 GM116792NIH HHS S10 OD018111
6 · The paper itself

Abstract

During herpesvirus infection, egress of nascent viral capsids from the nucleus is mediated by the viral nuclear egress complex (NEC). NEC deforms the inner nuclear membrane (INM) around the capsid by forming a hexagonal array. However, how the NEC coat interacts with the capsid and how curved coats are generated to enable budding is yet unclear. Here, by structure-guided truncations, confocal microscopy, and cryoelectron tomography, we show that binding of the capsid protein UL25 promotes the formation of NEC pentagons rather than hexagons. We hypothesize that during nuclear budding, binding of UL25 situated at the pentagonal capsid vertices to the NEC at the INM promotes formation of NEC pentagons that would anchor the NEC coat to the capsid. Incorporation of NEC pentagons at the points of contact with the vertices would also promote assembly of the curved hexagonal NEC coat around the capsid, leading to productive egress of UL25-decorated capsids.

Indexed as

Active Transport, Cell NucleusCapsid ProteinsCloning, MolecularCryoelectron MicroscopyEscherichia coliGene Expression Regulation, ViralHerpesvirus 1, HumanMicroscopy, ConfocalProtein TransportVirus ReplicationCapsid Proteinscapsid buddingherpes simplex virus type 1herpesvirusinfectious diseasemembrane buddingmicrobiologynuclear egressnuclear egress complexvirus

Identifiers

PMID32579107
PMCPMC7340501

What OpenQuestion holds

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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.