Evidence map›Paper›PMID 28157624›Full record

ArticleVirology2017

An interaction domain in human SAMD9 is essential for myxoma virus host-range determinant M062 antagonism of host anti-viral function.

Bernice Nounamo, Yibo Li, Peter O'Byrne, Aoife M Kearney, Amir Khan, Jia Liu

Abstract read
In one paragraph

Article in Virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 1 pooled it
1.2field-weighted citation impact, top 23% 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, 1 synthesis or guideline pooled it, 39 citations in OpenAlex.

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  13. Structure and function of an effector domain in antiviral factors and tumor suppressors SAMD9 and SAMD9L.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

6 authors at 2 institutions in 2 countries.

Bernice NounamoDepartment of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, AR, USA.
Yibo LiDepartment of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, AR, USA.
Peter O'ByrneSchool of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, Ireland.
Aoife M KearneySchool of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, Ireland.
Amir KhanSchool of Biochemistry and Immunology, Trinity College Dublin, Dublin 2, Ireland. Electronic address: amirrafk@tcd.ie.
Jia LiuDepartment of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, AR, USA; The Center for Microbial Pathogenesis and Host Inflammatory Responses, University of Arkansas for Medical Sciences, Little Rock, AR, USA. Electronic address: jliu4@uams.edu.
Trinity College Dublin · IEUniversity of Arkansas for Medical Sciences · US

Funding

Study of the Cell-specific Inflammasome Responses During Defense Against Gram-negative BacteriaP20GM103625 · NIGMS · UNIV OF ARKANSAS FOR MED SCIS · PI AACHOUI, YOUSSEF · 2012 to 2021
$21.5M
Arkansas Center for Clinical and Translational ResearchUL1TR000039 · NCATS · UNIV OF ARKANSAS FOR MED SCIS · PI BECK, CORNELIA MARIE, JAMES, LAURA P · 2012 to 2014
$10.0M
Studies in Poxvirus Evasion of SAMD9 PathwayR01AI139106 · NIAID · UNIV OF ARKANSAS FOR MED SCIS · PI LIU, JIA · 2019 to 2023
$1.9M
Characterization of Antiviral Functions of Sterile Alpha Motif-Containing DomainK22AI099184 · NIAID · UNIV OF ARKANSAS FOR MED SCIS · PI LIU, JIA · 2013 to 2014
$268k
NCATS NIH HHS UL1 TR000039NIAID NIH HHS K22 AI099184NIAID NIH HHS R01 AI139106NIGMS NIH HHS P20 GM103625
6 · The paper itself

Abstract

In humans, deleterious mutations in the sterile α motif domain protein 9 (SAMD9) gene are associated with cancer, inflammation, weakening of the immune response, and developmental arrest. However, the biological function of SAMD9 and its sequence-structure relationships remain to be characterized. Previously, we found that an essential host range factor, M062 protein from myxoma virus (MYXV), antagonized the function of human SAMD9. In this study, we examine the interaction between M062 and human SAMD9 to identify regions that are critical to SAMD9 function. We also characterize the in vitro kinetics of the interaction. In an infection assay, exogenous expression of SAMD9 N-terminus leads to a potent inhibition of wild-type MYXV infection. We reason that this effect is due to the sequestration of viral M062 by the exogenously expressed N-terminal SAMD9 region. Our studies reveal the first molecular insight into viral M062-dependent mechanisms that suppress human SAMD9-associated antiviral function.

Indexed as

A549 CellsAnimalsCell Line, TumorHEK293 CellsHeLa CellsHost SpecificityHumansIntracellular Signaling Peptides and ProteinsMiceMyxoma virusProteinsProtein Structure, TertiaryViral ProteinsIntracellular Signaling Peptides and ProteinsM062 protein, myxoma virusProteinsSAMD9 protein, humanViral ProteinsC7L superfamilyHost range factorImmunoprecipitationMYXVPolymerizationProtein-protein interactionSAMD9Surface plasmon resonance (SPR)

Identifiers

PMID28157624
PMCPMC5419587
OpenAlexW2585413864

What OpenQuestion holds

Textmetadata
LicenceTDM
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.