Evidence map›Paper›PMID 23637415›Full record

ArticleJournal of virology2013

Cross-inhibition of chikungunya virus fusion and infection by alphavirus E1 domain III proteins.

Claudia Sánchez-San Martín, Soumya Nanda, Yan Zheng, Whitney Fields, Margaret Kielian

Abstract read
In one paragraph

Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Near-germline human monoclonal antibodies neutralize and protect against multiple arthritogenic alphaviruses.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Residue-level resolution of alphavirus envelope protein interactions in pH-dependent fusion.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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.

Claudia Sánchez-San MartínDepartment of Cell Biology, Albert Einstein College of Medicine, Bronx, New York, USA.
Soumya Nanda
Yan Zheng
Whitney Fields
Margaret Kielian

Funding

WORD PROCESSORP30CA013330 · NCI · YESHIVA UNIVERSITY · PI THOMAS E ROHAN · 1985 to 2026
$111.2M
Viral Pathogenesis and TherapeuticsU54AI057158 · NIAID · WADSWORTH CENTER · PI LIPKIN, W. IAN · 2003 to 2014
$100.8M
TRAINING PROGRAM IN CELLULAR &MOLEC. BIOLOGY &GENETICST32GM007491 · NIGMS · YESHIVA UNIVERSITY · PI QUERY, CHARLES C · 1985 to 2021
$17.0M
Molecular Analysis of Alphavirus Membrane Fusion ProteinR01AI075647 · NIAID · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI KIELIAN, MARGARET · 2007 to 2023
$9.0M
NCI NIH HHS P30 CA013330NCI NIH HHS P30-CA13330NIAID NIH HHS R01 AI075647NIAID NIH HHS R01-AI075647NIAID NIH HHS U54 AI057158NIAID NIH HHS U54-AI057158NIGMS NIH HHS T32 GM007491
6 · The paper itself

Abstract

Alphaviruses are small enveloped RNA viruses that include important emerging human pathogens, such as chikungunya virus (CHIKV). These viruses infect cells via a low-pH-triggered membrane fusion reaction, making this step a potential target for antiviral therapies. The E1 fusion protein inserts into the target membrane, trimerizes, and refolds to a hairpin-like conformation in which the combination of E1 domain III (DIII) and the stem region (DIII-stem) pack against a core trimer composed of E1 domains I and II (DI/II). Addition of exogenous DIII proteins from Semliki Forest virus (SFV) has been shown to inhibit E1 hairpin formation and SFV fusion and infection. Here we produced and characterized DIII and DI/II proteins from CHIKV and SFV. Unlike SFV DIII, both core trimer binding and fusion inhibition by CHIKV DIII required the stem region. CHIKV DIII-stem and SFV DIII-stem showed efficient cross-inhibition of SFV, Sindbis virus, and CHIKV infections. We developed a fluorescence anisotropy-based assay for the binding of SFV DIII-stem to the core trimer and used it to demonstrate the relatively high affinity of this interaction (Kd [dissociation constant], ∼85 nM) and the importance of the stem region. Together, our results support the conserved nature of the key contacts of DIII-stem in the alphavirus E1 homotrimer and describe a sensitive and quantitative in vitro assay for this step in fusion protein refolding.

Indexed as

Virus AttachmentAlphavirus InfectionsAnimalsCell LineChikungunya virusCricetinaeDrosophilaFluorescence PolarizationHumansLiposomesProtein BindingSemliki forest virusSindbis VirusViral Envelope ProteinsViral Fusion ProteinsLiposomesViral Envelope ProteinsViral Fusion Proteins

Identifiers

PMID23637415
PMCPMC3700285

What OpenQuestion holds

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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.