Evidence map›Paper›PMID 20147401›Full record

ArticleJournal of virology2010

Venezuelan equine Encephalitis virus capsid protein forms a tetrameric complex with CRM1 and importin alpha/beta that obstructs nuclear pore complex function.

Svetlana Atasheva, Alexander Fish, Maarten Fornerod, Elena I Frolova

Abstract 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 88 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed, 1 pooled it
3.8field-weighted citation impact, top 6% 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

88 citing papers in PubMed, 1 synthesis or guideline pooled it, 125 citations in OpenAlex.

  1. Pooled it
  2. Review
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  4. Review
  5. Article
  6. Article
  7. Article
  8. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
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  17. Review
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  19. bioRxiv : the preprint server for biology · 2023
    Article
  20. Article

28 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

Svetlana AtashevaDepartment of Microbiology, University of Alabama at Birmingham, 1530 Third Avenue South, BBRB 373/Box 3, Birmingham, AL 53294-2170, USA.
Alexander Fish
Maarten Fornerod
Elena I Frolova
University of Alabama at Birmingham · USThe Netherlands Cancer Institute · NL

Funding

The Molecular Basis of VEEV PathogenesisR01AI070207 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI FROLOV, ILYA V. · 2008 to 2012
$1.6M
Sindbis nonstructural protein nsP2: Interaction with cellular proteinsR01AI073301 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI FROLOVA, ELENA I · 2008 to 2012
$1.6M
NIAID NIH HHS AI070207NIAID NIH HHS AI073301NIAID NIH HHS R01 AI070207NIAID NIH HHS R01 AI073301
6 · The paper itself

Abstract

Development of the cellular antiviral response requires nuclear translocation of multiple transcription factors and activation of a wide variety of cellular genes. To counteract the antiviral response, several viruses have developed an efficient means of inhibiting nucleocytoplasmic traffic. In this study, we demonstrate that the pathogenic strain of Venezuelan equine encephalitis virus (VEEV) has developed a unique mechanism of nuclear import inhibition. Its capsid protein forms a tetrameric complex with the nuclear export receptor CRM1 and the nuclear import receptor importin alpha/beta. This unusual complex accumulates in the center channel of the nuclear pores and blocks nuclear import mediated by different karyopherins. The inhibitory function of VEEV capsid protein is determined by a short 39-amino-acid-long peptide that contains both nuclear import and supraphysiological nuclear export signals. Mutations in these signals or in the linker peptide attenuate or completely abolish capsid-specific inhibition of nuclear traffic. The less pathogenic VEEV strains contain a wide variety of mutations in this peptide that affect its inhibitory function in nuclear import. Thus, these mutations appear to be the determinants of this attenuated phenotype. This novel mechanism of inhibiting nuclear transport also shows that the nuclear pore complex is vulnerable to unusual cargo receptor complexes and sheds light on the importance of finely adjusted karyopherin-nucleoporin interactions for efficient cargo translocation.

Indexed as

alpha KaryopherinsAmino Acid SequenceAnimalsbeta KaryopherinsCapsid ProteinsCell LineCricetinaeEncephalitis Virus, Venezuelan EquineExportin 1 ProteinKaryopherinsMolecular Sequence DataNuclear PoreProtein BindingProtein Interaction MappingProtein MultimerizationReceptors, Cytoplasmic and Nuclearalpha Karyopherinsbeta KaryopherinsCapsid ProteinsExportin 1 ProteinKaryopherinsReceptors, Cytoplasmic and Nuclear

Identifiers

PMID20147401
PMCPMC2863722
OpenAlexW2169793634

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.