Evidence map›Paper›PMID 20162447›Full record

ArticleVirus genes2010

Characteristics of Epstein-Barr virus envelope protein gp42.

Pamela L Shaw, Austin N Kirschner, Theodore S Jardetzky, Richard Longnecker

Open access · greenAbstract read
In one paragraph

Article in Virus genes, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Neutralizing antibodies against EBV gp42 show potentEmerging microbes & infections · 2023
    Article
  3. Review
  4. Article
  5. Epithelial cell infection by Epstein-Barr virus.FEMS microbiology reviews · 2019
    Article
  6. Review
  7. HLA-DQJCI insight · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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

4 authors at 2 institutions in 1 country.

Pamela L ShawDepartment of Microbiology and Immunology, The Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
Austin N Kirschner
Theodore S Jardetzky
Richard Longnecker
Northwestern University · USStanford University · US

Funding

MULTIDISCIPLINARY CLINICAL AND TRANSLATIONAL SCIENCE (MCTS) PROGRAM (UL1)UL1RR025741 · NCRR · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GREENLAND, PHILIP · 2008 to 2011
$24.7M
Structural and Functional Studies of gp42 and HLA Class II in EBV EntryR01AI076183 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI JARDETZKY, THEODORE S, LONGNECKER, RICHARD M · 2008 to 2017
$4.6M
Inhibitors of the Epstein-Barr Virus Entry MachineryR01CA117794 · NCI · STANFORD UNIVERSITY · PI JARDETZKY, THEODORE S, LONGNECKER, RICHARD M · 2006 to 2016
$3.0M
EBV gB Function in Viral Fusion, Entry, and EgressR01AI067048 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI LONGNECKER, RICHARD M · 2007 to 2011
$1.9M
Developing Skills in Research BioinformaticsF37LM009568 · NLM · NORTHWESTERN UNIVERSITY AT CHICAGO · PI SHAW, PAMELA L · 2007 to 2008
$43k
NCI NIH HHS CA117794NCI NIH HHS R01 CA117794NCRR NIH HHS UL1 RR025741NIAID NIH HHS AI067048NIAID NIH HHS AI076183NIAID NIH HHS R01 AI067048NIAID NIH HHS R01 AI076183NLM NIH HHS F37 LM009568NLM NIH HHS F37LM009568
6 · The paper itself

Abstract

Epstein-Barr virus (EBV) glycoprotein 42 (gp42) is a membrane protein essential for fusion and entry of EBV into host B-lymphocytes. Gp42 is a member of the protein-fold family C-type lectin or lectin-like domains (CLECT or CTLD) and specifically is classified as a natural-killer receptor (NKR)-like CLECT. Literature review and phylogenetic comparison show that EBV gp42 shares a common structure with other NKR-like CLECTs and possibly with many viral CTLDs, but does not appear to exhibit some common binding characteristics of many CTLDs, such as features required for calcium binding. The flexible N-terminal region adjacent to the CTLD fold is important for binding to other EBV glycoproteins and for a cleavage site that is necessary for infection of host cells. From structural studies of gp42 unbound and bound to receptor and extensive mutational analysis, a general model of how gp42 triggers membrane fusion utilizing both the flexible N-terminal region and the CTLD domain has emerged.

Indexed as

Virus InternalizationAmino Acid SequenceCalciumComputational BiologyGlycoproteinsHerpesvirus 4, HumanModels, MolecularMolecular Sequence DataPhylogenyProtein BindingProtein Structure, SecondaryProtein Structure, TertiarySequence HomologyViral ProteinsBZLF2 protein, Herpesvirus 4, HumanCalciumGlycoproteinsViral Proteins

Identifiers

PMID20162447
PMCPMC2854865
OpenAlexW1974762536

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.