Evidence map›Paper›PMID 26578811›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Structural basis for antagonizing a host restriction factor by C7 family of poxvirus host-range proteins.

Xiangzhi Meng, Brian Krumm, Yongchao Li, Junpeng Deng, Yan Xiang

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Article
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  11. Article
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  14. Emerging phenotypes linked to variants inFrontiers in endocrinology · 2022
    Article
  15. Article
  16. Article
  17. Review
  18. Oncolytic Virotherapy with Myxoma Virus.Journal of clinical medicine · 2020
    Review
  19. 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

5 authors.

Xiangzhi MengDepartment of Microbiology and Immunology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229;
Brian KrummDepartment of Biochemistry and Molecular biology, Oklahoma State University, Stillwater, OK 74078.
Yongchao LiDepartment of Biochemistry and Molecular biology, Oklahoma State University, Stillwater, OK 74078.
Junpeng DengDepartment of Biochemistry and Molecular biology, Oklahoma State University, Stillwater, OK 74078 Junpeng.deng@okstate.edu XiangY@uthscsa.edu.
Yan XiangDepartment of Microbiology and Immunology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229; Junpeng.deng@okstate.edu XiangY@uthscsa.edu.

Funding

Structure-Function Studies of MsvR, a Methanogen-Specific Transcriptional RegulaP20GM103640 · NIGMS · UNIVERSITY OF OKLAHOMA · PI MOOERS, BLAINE H. M. · 2012 to 2021
$20.4M
Poxvirus Immune Evasion MechanismsR01AI079217 · NIAID · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI XIANG, YAN · 2008 to 2018
$3.3M
Structure-function studies on a key signaling module from interleukin 17 receptorR21AI113539 · NIAID · OKLAHOMA STATE UNIVERSITY STILLWATER · PI DENG, JUNPENG · 2014 to 2015
$395k
NIAID NIH HHS AI079217NIAID NIH HHS AI113539NIAID NIH HHS R01 AI079217NIAID NIH HHS R21 AI113539NIGMS NIH HHS P20 GM103640NIGMS NIH HHS P20GM103640
6 · The paper itself

Abstract

Human sterile alpha motif domain-containing 9 (SAMD9) protein is a host restriction factor for poxviruses, but it can be overcome by some poxvirus host-range proteins that share homology with vaccinia virus C7 protein. To understand the mechanism of action for this important family of host-range factors, we determined the crystal structures of C7 and myxoma virus M64, a C7 family member that is unable to antagonize SAMD9. Despite their different functions and only 23% sequence identity, the two proteins have very similar overall structures, displaying a previously unidentified fold comprised of a compact 12-stranded antiparallel β-sandwich wrapped in two short α helices. Extensive structure-guided mutagenesis of C7 identified three loops clustered on one edge of the β sandwich as critical for viral replication and binding with SAMD9. The loops are characterized with functionally important negatively charged, positively charged, and hydrophobic residues, respectively, together forming a unique "three-fingered molecular claw." The key residues of the claw are not conserved in two C7 family members that do not antagonize SAMD9 but are conserved in distantly related C7 family members from four poxvirus genera that infect diverse mammalian species. Indeed, we found that all in the latter group of proteins bind SAMD9. Taken together, our data indicate that diverse mammalian poxviruses use a conserved molecular claw in a C7-like protein to target SAMD9 and overcome host restriction.

Indexed as

Crystallography, X-RayHumansIntracellular Signaling Peptides and ProteinsMyxoma virusProteinsProtein Structure, SecondaryVaccinia virusViral ProteinsIntracellular Signaling Peptides and ProteinsProteinsSAMD9 protein, humanViral ProteinsC7Lcrystal structurehost-range factorspoxvirusSAMD9

Identifiers

PMID26578811
PMCPMC4672790

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Registered trials

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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.