Evidence map›Paper›PMID 20106914›Full record

ArticleJournal of virology2010

The N-terminal region of severe acute respiratory syndrome coronavirus protein 6 induces membrane rearrangement and enhances virus replication.

Haixia Zhou, Debra Ferraro, Jincun Zhao, Snawar Hussain, Jianqiang Shao, Jonathan Trujillo, Jason Netland, Thomas Gallagher, Stanley Perlman

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2010. 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
1.4field-weighted citation impact, top 21% 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, 41 citations in OpenAlex.

  1. Quantitative comparison of nuclear transport inhibition by SARS coronavirus ORF6 reveals the importance of oligomerization.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Review
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  11. An aberrant STAT pathway is central to COVID-19.Cell death and differentiation · 2020
    Review
  12. Article
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  19. A sorting signal suppresses IFITM1 restriction of viral entry.The Journal of biological chemistry · 2015
    Article
  20. Article
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

9 authors at 2 institutions in 1 country.

Haixia ZhouDepartment of Microbiology, University of Iowa, 3-712 BSB, Iowa City, IA 52242, USA.
Debra Ferraro
Jincun Zhao
Snawar Hussain
Jianqiang Shao
Jonathan Trujillo
Jason Netland
Thomas Gallagher
Stanley Perlman
Loyola University Chicago · USUniversity of Iowa · US

Funding

SARS-CoV Proteins in Heterologous Viral InfectionP01AI060699 · NIAID · UNIVERSITY OF IOWA · PI PERLMAN, STANLEY · 2004 to 2021
$21.5M
Multidisciplinary Lung Research Career Development ProgramT32HL007638 · NHLBI · UNIVERSITY OF IOWA · PI WELSH, MICHAEL J., ZABNER, JOSEPH · 1986 to 2020
$16.9M
MEDICAL SCIENTIST TRAINING PROGRAMT32GM007337 · NIGMS · UNIVERSITY OF IOWA · PI GEYER, PAMELA K., LENTZ, STEVEN R · 1985 to 2020
$15.9M
NHLBI NIH HHS T32 HL007638NHLBI NIH HHS T32 HL07638NIAID NIH HHS P01 AI060699NIGMS NIH HHS T32 GM007337
6 · The paper itself

Abstract

The severe acute respiratory syndrome coronavirus (SARS-CoV) accessory protein 6 (p6) is a 63-amino-acid multifunctional Golgi-endoplasmic reticulum (ER) membrane-associated protein, with roles in enhancing virus replication and in evading the innate immune response to infection by inhibiting STAT1 (signal transducer and activator of transcription factor 1) translocation to the nucleus. Here, we demonstrate that p6 has an N-terminal region-cytoplasm-C-terminal region-cytoplasm configuration with residues 2 to 37 likely membrane embedded. Expression of p6, or of its N-terminal 41-amino-acid region, in the absence of other viral proteins, induced the formation of membranous structures, some of which were similar to double membrane vesicles involved in virus replication. Consistent with a role in virus replication, p6 partially colocalized with nonstructural protein 3 (nsp3), a marker for virus replication complexes. Further, while the C-terminal region is required for preventing STAT1 translocation to the nucleus, our results also indicated that the N-terminal 18 amino acids were necessary for maximal inhibition. Collectively, these results support the notion that p6 is a two-domain protein, although the function of each is not completely independent of the other.

Indexed as

Virus ReplicationActive Transport, Cell NucleusCell MembraneCells, CulturedHumansProtein Structure, SecondaryProtein TransportSevere acute respiratory syndrome-related coronavirusSTAT1 Transcription FactorViral Proteinsprotein 6, SARS virusSTAT1 protein, humanSTAT1 Transcription FactorViral Proteins

Identifiers

PMID20106914
PMCPMC2838104
OpenAlexW2003907005

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.