Evidence map›Paper›PMID 23843635›Full record

ArticleJournal of virology2013

Mutations in the cytoplasmic tail of herpes simplex virus 1 gH reduce the fusogenicity of gB in transfected cells.

Jessica L Silverman, Ekaterina E Heldwein

Open access · bronzeAbstract 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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. mBio · 2021
    Article
  8. Review
  9. The structural basis of herpesvirus entry.Nature reviews. Microbiology · 2021
    Review
  10. Entry of Alphaherpesviruses.Current issues in molecular biology · 2021
    Review
  11. Article
  12. Melittin: a venom-derived peptide with promising anti-viral properties.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2020
    Review
  13. The COMPLEXity in herpesvirus entry.Current opinion in virology · 2017
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Jessica L SilvermanDepartment of Molecular Biology and Microbiology and Graduate Program in Molecular Microbiology, Tufts University School of Medicine, Boston, Massachusetts, USA.
Ekaterina E Heldwein
Tufts University · US

Funding

COLLABORATIVE CHRONIC DISEASE, HEALTH PROMOTION, AND SURVEILLANCE PROGRAMU58DP001996 · DP · WASHINGTON STATE DEPARTMENT OF HEALTH · PI NANDI, PAJ · 2009 to 2014
$16.8M
Structural and mechanistic studies of herpesvirus entry into host cellsDP2OD001996 · OD · TUFTS UNIVERSITY BOSTON · PI HELDWEIN, EKATERINA · 2007 to 2007
$2.5M
NCCDPHP CDC HHS 1DP20D001996
6 · The paper itself

Abstract

Mutations within the cytoplasmic tail (cytotail) of herpes simplex virus 1 (HSV-1) gH were previously observed to suppress the syncytial phenotype of gB cytoplasmic domain mutant A855V in infected cells. Here, we examined the effects of gH cytotail mutations on virus-free cell-cell fusion in transfected cells to exclude the contributions of viral proteins other than gD, gH/gL, and gB. We show that a truncation at residue 832 coupled with the point mutation V831A within the cytotail of gH reduces fusion regardless of whether the wild type (WT) or a syn gB allele is present. We hypothesize that the gH cytotail mutations either reduce activation of gB by gH/gL or suppress the fusogenicity of gB through another, as yet unknown mechanism. The gB cytodomain and the gH cytotail do not interact in vitro, suggesting that mutations in the gH cytotail may instead affect the function of the gH/gL ectodomain. Nevertheless, we cannot exclude the possibility that the gB cytodomain and the gH cytotail interact in the context of full-length membrane-anchored proteins. The observed fusion suppression in transfected cells is less prominent than what was seen in infected cells, and we propose that gH cytotail mutations may additionally suppress syncytium formation in cells infected with syn HSV-1 by acting on other viral proteins, reinforcing the idea that fusion of HSV-infected cells is a complex phenomenon. Although fusion suppression by the gH cytotail mutant in transfected cells was evident when syncytia were visualized and counted, it was not detected by the luciferase assay, highlighting the differences between the two assays.

Indexed as

MutationVirus InternalizationGiant CellsHerpesvirus 1, HumanHumansMutant ProteinsViral Envelope Proteinsglycoprotein B, Simplexvirusglycoprotein H, herpes simplex virus type 1Mutant ProteinsViral Envelope Proteins

Identifiers

PMID23843635
PMCPMC3753984
OpenAlexW2139936735

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.