Evidence map›Paper›PMID 33009400›Full record

ArticleNature communications2020

Identification of a pocket factor that is critical to Zika virus assembly.

Nadia M DiNunno, Daniel J Goetschius, Anoop Narayanan, Sydney A Majowicz, Ibrahim Moustafa, Carol M Bator, Susan L Hafenstein, Joyce Jose

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

29 citing papers in PubMed, 42 citations in OpenAlex.

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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

8 authors at 1 institution in 1 country.

Nadia M DiNunnoDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, 16802, USA.
Daniel J GoetschiusDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, 16802, USA.ORCID http://orcid.org/0000-0002-6052-7141
Anoop NarayananDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, 16802, USA.
Sydney A MajowiczDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, 16802, USA.
Ibrahim MoustafaDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, 16802, USA.
Carol M BatorThe Huck Institutes of the Life Sciences, The Pennsylvania State University, University Park, PA, 16802, USA.
Susan L HafensteinDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, 16802, USA.
Joyce JoseDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, 16802, USA. jxj321@psu.edu.ORCID http://orcid.org/0000-0003-1261-6921
Pennsylvania State University · US

Funding

Mechanisms of Enterovirus EntryR01AI107121 · NIAID · UNIVERSITY OF MINNESOTA · PI HAFENSTEIN, SUSAN · 2015 to 2024
$3.9M
HEI: Acquisition of a Talos Arctica G2S10OD026822 · OD · PENNSYLVANIA STATE UNIVERSITY, THE · PI HAFENSTEIN, SUSAN · 2019 to 2019
$2.0M
NIAID NIH HHS R01 AI107121NIH HHS S10 OD026822
6 · The paper itself

Abstract

Zika virus (ZIKV) is an emerging mosquito borne flavivirus and a major public health concern causing severe disease. Due to the presence of a lipid membrane and structural heterogeneity, attaining an atomic resolution structure is challenging, but important to understand virus assembly and life cycle mechanisms that offer distinct targets for therapeutic intervention. We here use subvolume refinement to achieve a 3.4 Å resolution structure and identify two distinct lipid moieties. The first arises from the inner leaflet and is coordinated by hydrophobic residues of the M and E transmembrane helices that form a binding pocket not previously characterized. The second lipid arises from the outer leaflet coordinate between two E protein helices. Structure-based mutagenesis identifies critical hydrophobic interactions and their effect on the virus life cycle. Results show that lipids play an essential role in the ZIKV assembly pathway revealing a potential target of lipid based antiviral drug development.

Indexed as

AnimalsChlorocebus aethiopsHEK293 CellsHumansVero CellsVirionVirus AssemblyZika Virus

Identifiers

PMID33009400
PMCPMC7532219
OpenAlexW3091378315

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.