Evidence map›Paper›PMID 22025718›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Structure-function analysis of varicella-zoster virus glycoprotein H identifies domain-specific roles for fusion and skin tropism.

Susan E Vleck, Stefan L Oliver, Jennifer J Brady, Helen M Blau, Jaya Rajamani, Marvin H Sommer, Ann M Arvin

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.4field-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

42 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. The Structures and Functions of VZV Glycoproteins.Current topics in microbiology and immunology · 2023
    Article
  11. Review
  12. Article
  13. Entry of Alphaherpesviruses.Current issues in molecular biology · 2021
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Insights into the pathogenesis of varicella viruses.Current clinical microbiology reports · 2019
    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

7 authors at 1 institution in 1 country.

Susan E VleckDepartment of Pediatrics, Stanford University School of Medicine, Stanford, CA 94305, USA. sevleck@stanford.edu
Stefan L Oliver
Jennifer J Brady
Helen M Blau
Jaya Rajamani
Marvin H Sommer
Ann M Arvin
Stanford University · US

Funding

MOLECULAR BASIS OF HOST-PARASITE INTERACTIONT32AI007328 · NIAID · STANFORD UNIVERSITY · PI JUSTIN L SONNENBURG · 1987 to 2026
$11.9M
Varicella-Zoster Virus: T Cell/Skin Tropisms &ImmunityR01AI020459 · NIAID · STANFORD UNIVERSITY · PI OLIVER, STEFAN LYNE · 1985 to 2023
$6.4M
ACTIVATORS OF MUSCLE GENESR01AG009521 · NIA · STANFORD UNIVERSITY · PI BLAU, HELEN M · 1990 to 2014
$4.7M
NIAID NIH HHS AI007328NIAID NIH HHS AI20459NIAID NIH HHS R01 AI020459NIAID NIH HHS T32 AI007328NIA NIH HHS R01 AG009521NIGMS NIH HHS GM007279
6 · The paper itself

Abstract

Enveloped viruses require membrane fusion for cell entry and replication. For herpesviruses, this event is governed by the multiprotein core complex of conserved glycoproteins (g)B and gH/gL. The recent crystal structures of gH/gL from herpes simplex virus 2, pseudorabies virus, and Epstein-Barr virus revealed distinct domains that, surprisingly, do not resemble known viral fusogens. Varicella-zoster virus (VZV) causes chicken pox and shingles. VZV is an α-herpesvirus closely related to herpes simplex virus 2, enabling prediction of the VZV gH structure by homology modeling. We have defined specific roles for each gH domain in VZV replication and pathogenesis using structure-based site-directed mutagenesis of gH. The distal tip of domain (D)I was important for skin tropism, entry, and fusion. DII helices and a conserved disulfide bond were essential for gH structure and VZV replication. An essential (724)CXXC(727) motif was critical for DIII structural stability and membrane fusion. This assignment of domain-dependent mechanisms to VZV gH links elements of the glycoprotein structure to function in herpesvirus replication and virulence.

Indexed as

Herpesvirus 3, HumanMembrane FusionModels, MolecularMutagenesis, Site-DirectedSkinStructure-Activity RelationshipViral Envelope ProteinsViral TropismVirulenceVirus ReplicationViral Envelope Proteins

Identifiers

PMID22025718
PMCPMC3215059
OpenAlexW2124672231

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.