Evidence map›Paper›PMID 34643427›Full record

ArticleJournal of virology2022

The Human STAT2 Coiled-Coil Domain Contains a Degron for Zika Virus Interferon Evasion.

Jean-Patrick Parisien, Jessica J Lenoir, Gloria Alvarado, Curt M Horvath

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Pathogenesis of Zika Virus Infection.Annual review of pathology · 2023
    Review
  8. Review
  9. Article
  10. Review
  11. 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

4 authors at 1 institution in 1 country.

Jean-Patrick ParisienDepartment of Molecular Biosciences, Northwestern Universitygrid.16753.36, Evanston, Illinois, USA.
Jessica J LenoirDepartment of Molecular Biosciences, Northwestern Universitygrid.16753.36, Evanston, Illinois, USA.
Gloria AlvaradoDepartment of Molecular Biosciences, Northwestern Universitygrid.16753.36, Evanston, Illinois, USA.
Curt M HorvathDepartment of Molecular Biosciences, Northwestern Universitygrid.16753.36, Evanston, Illinois, USA.ORCID 0000-0003-2449-225X
Northwestern University · US

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI LEONIDAS C. PLATANIAS · 1993 to 2026
$153.9M
CELLULAR &MOLECULAR BASIS OF DISEASE TRAINING PROGRAMT32GM008061 · NIGMS · NORTHWESTERN UNIVERSITY · PI CARTHEW, RICHARD W. · 1985 to 2022
$17.1M
5-laser 30-parameter FACSymphony-S6 SORP Cell Sorter from BD BiosciencesS10OD026814 · OD · NORTHWESTERN UNIVERSITY AT CHICAGO · PI PERLMAN, HARRIS R · 2019 to 2019
$904k
FACSAria SORP Cell SorterS10OD011996 · OD · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GOOLSBY, CHARLES L. · 2012 to 2012
$482k
Mechanisms and Modifiers of Zika Virus Innate Immune EvasionR21AI148949 · NIAID · NORTHWESTERN UNIVERSITY · PI HORVATH, CURT M · 2020 to 2021
$426k
NCI NIH HHS P30 CA060553NIAID NIH HHS R21 AI148949NIGMS NIH HHS T32 GM008061NIH HHS S10 OD011996NIH HHS S10 OD026814
6 · The paper itself

Abstract

The ability of viruses to evade the host antiviral immune system determines their level of replication fitness, species specificity, and pathogenic potential. Flaviviruses rely on the subversion of innate immune barriers, including the type I and type III interferon (IFN) antiviral systems. Zika virus infection induces the degradation of STAT2, an essential component of the IFN-stimulated gene transcription factor ISGF3. The mechanisms that lead to STAT2 degradation by Zika virus are poorly understood, but it is known to be mediated by the viral NS5 protein that binds to STAT2 and targets it for proteasome-mediated destruction. To better understand how NS5 engages and degrades STAT2, functional analysis of the protein interactions that lead to Zika virus and NS5-dependent STAT2 proteolysis were investigated. Data implicate the STAT2 coiled-coil domain as necessary and sufficient for NS5 interaction and proteasome degradation after Zika virus infection. Molecular dissection reveals that the first two α-helices of the STAT2 coiled-coil domain contain a specific targeting region for IFN antagonism. These functional interactions provide a more complete understanding of the essential protein-protein interactions needed for Zika virus evasion of the host antiviral response and identify new targets for antiviral therapeutic approaches.

Indexed as

Host-Pathogen InteractionsDisease SusceptibilityHumansInterferonsProteasome Endopeptidase ComplexProtein BindingProtein Interaction Domains and MotifsProteolysisSTAT2 Transcription FactorViral Nonstructural ProteinsZika VirusZika Virus InfectionInterferonsPOLY protein, Zika virusProteasome Endopeptidase ComplexSTAT2 protein, humanSTAT2 Transcription FactorViral Nonstructural ProteinsNS5STAT2Zika virus

Identifiers

PMID34643427
PMCPMC8754212
OpenAlexW3203657275

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.