Evidence map›Paper›PMID 34578329›Full record

ArticleViruses2021

Protease, Growth Factor, and Heparanase-Mediated Syndecan-1 Shedding Leads to Enhanced HSV-1 Egress.

Ghadah A Karasneh, Divya Kapoor, Navya Bellamkonda, Chandrashekhar D Patil, Deepak Shukla

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

13 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. HerpDock: A GUI-based gateway to HSV-1 molecular docking insights.Computational and structural biotechnology journal · 2024
    Article
  5. Emerging drugs for the treatment of herpetic keratitis.Expert opinion on emerging drugs · 2024
    Review
  6. Article
  7. Tunneling Nanotubes: The Cables for Viral Spread and Beyond.Results and problems in cell differentiation · 2024
    Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. 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 at 1 institution in 1 country.

Ghadah A KarasnehDepartment of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, 835 S. Wolcott, Chicago, IL 60612, USA.
Divya KapoorDepartment of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, 835 S. Wolcott, Chicago, IL 60612, USA.ORCID 0000-0001-7142-3025
Navya BellamkondaDepartment of Ophthalmology and Visual Sciences, College of Medicine, University of Illinois at Chicago, 1855 W. Taylor, Chicago, IL 60612, USA.ORCID 0000-0003-0167-3111
Chandrashekhar D PatilDepartment of Ophthalmology and Visual Sciences, College of Medicine, University of Illinois at Chicago, 1855 W. Taylor, Chicago, IL 60612, USA.ORCID 0000-0002-5641-4523
Deepak ShuklaDepartment of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, 835 S. Wolcott, Chicago, IL 60612, USA.ORCID 0000-0002-3039-6953
University of Illinois Chicago · US

Funding

NIH HHS EY01792NIH HHS EY029426
6 · The paper itself

Abstract

Heparan sulfate (HS) and heparan sulfate proteoglycans (HSPGs) are considered important for the entry of many different viruses. Previously, we demonstrated that heparanase (HPSE), the host enzyme responsible for cleaving HS chains, is upregulated by herpes simplex virus-1 (HSV-1) infection. Higher levels of HPSE accelerate HS removal from the cell surface, facilitating viral release from infected cells. Here, we study the effects of overexpressing HPSE on viral entry, cell-to-cell fusion, plaque formation, and viral egress. We provide new information that higher levels of HPSE reduce syncytial plaque formation while promoting egress and extracellular release of the virions. We also found that transiently enhanced expression of HPSE did not affect HSV-1 entry into host cells or HSV-1-induced cell-to-cell fusion, suggesting that HPSE activation is tightly regulated and facilitates extracellular release of the maturing virions. We demonstrate that an HSPG-shedding agonist, PMA; a protease, thrombin; and a growth factor, EGF as well as bacterially produced recombinant heparinases resulted in enhanced HSV-1 release from HeLa and human corneal epithelial (HCE) cells. Our findings here underscore the significance of syndecan-1 functions in the HSV-1 lifecycle, provide evidence that the shedding of syndecan-1 ectodomain is another way HPSE works to facilitate HSV-1 release, and add new evidence on the significance of various HSPG shedding agonists in HSV-1 release from infected cells.

Indexed as

CorneaEpidermal Growth FactorEpithelial CellsHeLa CellsHeparin LyaseHerpesvirus 1, HumanHumansSyndecan-1ThrombinUp-RegulationVirionVirus InternalizationVirus ReleaseEpidermal Growth FactorHeparin LyaseSDC1 protein, humanSyndecan-1Thrombinheparan sulfateheparan sulfate proteoglycanHSV-1

Identifiers

PMID34578329
PMCPMC8473078
OpenAlexW3198150552

What OpenQuestion holds

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LicenceCC BY
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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.