Evidence map›Paper›PMID 27058774›Full record

ArticleAntiviral research2016

An inducible heat shock protein 70 small molecule inhibitor demonstrates anti-dengue virus activity, validating Hsp70 as a host antiviral target.

Matthew K Howe, Brittany L Speer, Philip F Hughes, David R Loiselle, Subhash Vasudevan, Timothy A J Haystead

Open access · greenAbstract read
In one paragraph

Article in Antiviral research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
7.3field-weighted citation impact, top 3% 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

27 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
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  11. Heat shock proteins and viral infection.Frontiers in immunology · 2022
    Review
  12. Review
  13. Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection.International journal of molecular sciences · 2021
    Review
  14. Article
  15. Review
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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.

Matthew K HoweDepartment of Pharmacology and Cancer Biology, Duke University School of Medicine, Durham, NC, USA.
Brittany L SpeerDepartment of Pharmacology and Cancer Biology, Duke University School of Medicine, Durham, NC, USA.
Philip F HughesDepartment of Pharmacology and Cancer Biology, Duke University School of Medicine, Durham, NC, USA.
David R LoiselleDepartment of Pharmacology and Cancer Biology, Duke University School of Medicine, Durham, NC, USA.
Subhash VasudevanEmerging Infectious Diseases Program, Duke-NUS Graduate and Medical School, Singapore.
Timothy A J HaysteadDepartment of Pharmacology and Cancer Biology, Duke University School of Medicine, Durham, NC, USA. Electronic address: timothy.haystead@dm.duke.edu.
Duke University · USDuke-NUS Medical School · SG

Funding

ORGANIZATION AND FUNCTIONS OF CELLULAR STRUCTUREST32GM007184 · NIGMS · DUKE UNIVERSITY · PI JINKS-ROBERTSON, SUE · 1985 to 2019
$18.2M
Pharmacological Sciences Training ProgramT32GM007105 · NIGMS · DUKE UNIVERSITY · PI KUHN, CYNTHIA M · 1985 to 2019
$9.0M
Discovery and development of broad spectrum anti-flaviviral drugsR01AI089526 · NIAID · DUKE UNIVERSITY · PI ENGEL, DANIEL A, GARCIA-BLANCO, MARIANO A. · 2010 to 2014
$4.1M
NIAID NIH HHS R01 AI089526NIGMS NIH HHS T32 GM007105NIGMS NIH HHS T32 GM007184
6 · The paper itself

Abstract

An estimated three billion people are at risk of Dengue virus (DENV) infection worldwide and there are currently no approved therapeutic interventions for DENV infection. Due to the relatively small size of the DENV genome, DENV is reliant on host factors throughout the viral life cycle. The inducible form of Heat Shock Protein 70 (Hsp70i) has been implicated as a host factor in DENV pathogenesis, however the complete role remains to be elucidated. Here we further illustrate the importance of Hsp70i in dengue virus pathogenesis and describe the antiviral activity of the allosteric small molecule inhibitor that is selective for Hsp70i, called HS-72. In monocytes, Hsp70i is expressed at low levels preceding DENV infection, but Hsp70i expression is induced upon DENV infection. Targeting Hsp70i with HS-72, results in a dose dependent reduction in DENV infected monocytes, while cell viability was maintained. HS-72 works to reduce DENV infection by inhibiting the entry stage of the viral life cycle, through disrupting the association of Hsp70i with the DENV receptor complex. This work highlights Hsp70i as an antiviral target and HS-72 as a potential anti-DENV therapeutic agent.

Indexed as

AnimalsAntiviral AgentsBenzimidazolesCell LineCell MembraneCells, CulturedDengueDengue VirusHost-Pathogen InteractionsHSP70 Heat-Shock ProteinsHumansNipecotic AcidsProtein BindingProtein TransportProteomeProteomicsAntiviral AgentsBenzimidazolesHS-72 compoundHSP70 Heat-Shock ProteinsNipecotic AcidsProteomeReceptors, VirusAntiviral targetAntiviral therapyDengue virusHeat shock protein 70Small molecule inhibitor

Identifiers

PMID27058774
PMCPMC4955699
OpenAlexW2328009556

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.