Evidence map›Paper›PMID 29046455›Full record

ArticleJournal of virology2018

Extended Synaptotagmin 1 Interacts with Herpes Simplex Virus 1 Glycoprotein M and Negatively Modulates Virus-Induced Membrane Fusion.

Imane El Kasmi, Bita Khadivjam, Miki Lackman, Johanne Duron, Eric Bonneil, Pierre Thibault, Roger Lippé

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Exploring gastric cancer genetics: A turning point in common variable immunodeficiency.The journal of allergy and clinical immunology. Global · 2024
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  7. LIVE-CELL FLUORESCENCE MICROSCOPY OF HSV-1 CELLULAR EGRESS BY EXOCYTOSIS.bioRxiv : the preprint server for biology · 2023
    Article
  8. SUN2 Modulates the Propagation of HSV-1.Journal of virology · 2022
    Article
  9. Article
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  11. 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

7 authors at 2 institutions in 1 country.

Imane El KasmiDepartment of Pathology and Cell Biology, University of Montreal, Montreal, Québec, Canada.
Bita KhadivjamDepartment of Pathology and Cell Biology, University of Montreal, Montreal, Québec, Canada.
Miki LackmanDepartment of Pathology and Cell Biology, University of Montreal, Montreal, Québec, Canada.
Johanne DuronDepartment of Pathology and Cell Biology, University of Montreal, Montreal, Québec, Canada.
Eric BonneilInstitute for Research in Immunology and Cancer, Department of Chemistry, University of Montreal, Montreal, Québec, Canada.
Pierre ThibaultInstitute for Research in Immunology and Cancer, Department of Chemistry, University of Montreal, Montreal, Québec, Canada.
Roger LippéDepartment of Pathology and Cell Biology, University of Montreal, Montreal, Québec, Canada roger.lippe@umontreal.ca.ORCID http://orcid.org/0000-0001-5066-3070
Université de Montréal · CAInstitute for Research in Immunology and Cancer · CA

Funding

CIHR MOP258030
6 · The paper itself

Abstract

Enveloped viruses typically encode their own fusion machinery to enter cells. Herpesviruses are unusual, as they fuse with a number of cellular compartments throughout their life cycles. As uncontrolled fusion of the host membranes should be avoided in these events, tight regulation of the viral fusion machinery is critical. While studying herpes simplex virus 1 (HSV-1) glycoprotein gM, we identified the cellular protein E-Syt1 (extended synaptotagmin 1) as an interaction partner. The interaction took place in both infected and transfected cells, suggesting other viral proteins were not required for the interaction. Most interestingly, E-Syt1 is a member of the synaptotagmin family of membrane fusion regulators. However, the protein is known to promote the tethering of the endoplasmic reticulum (ER) to the plasma membrane. We now show that E-Syt1, along with the related E-Syt3, negatively modulates viral release into the extracellular milieu, cell-to-cell viral spread, and viral entry, all processes that implicate membrane fusion events. Similarly, these E-Syt proteins impacted the formation of virus-induced syncytia. Altogether, these findings hint at the modulation of the viral fusion machinery by the E-Syt family of proteins.

Indexed as

Membrane FusionGiant CellsHeLa CellsHerpesvirus 1, HumanHumansImmunoprecipitationMembrane GlycoproteinsRNA, Small InterferingSynaptotagminsViral ProteinsVirus ReleaseESYT1 protein, humanESYT2 protein, humanESYT3 protein, humanMembrane GlycoproteinsRNA, Small InterferingSynaptotagminsUL10 protein, Human herpesvirus 1Viral ProteinsE-Syt1E-Syt2E-Syt3fusiongMHSVsynaptotagminsyncytiaUL10

Identifiers

PMID29046455
PMCPMC5730791
OpenAlexW2767038038

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.