Evidence map›Paper›PMID 19217393›Full record

ArticleStructure (London, England : 1993)2009

Structure of Epstein-Barr virus glycoprotein 42 suggests a mechanism for triggering receptor-activated virus entry.

Austin N Kirschner, Jessica Sorem, Richard Longnecker, Theodore S Jardetzky

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

50 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Neutralizing antibodies against EBV gp42 show potentEmerging microbes & infections · 2023
    Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. The structural basis of herpesvirus entry.Nature reviews. Microbiology · 2021
    Review
  17. Review
  18. Article
  19. Epstein-Barr Virus and the Human Leukocyte Antigen Complex.Current clinical microbiology reports · 2019
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Austin N KirschnerDepartment of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208, USA.
Jessica Sorem
Richard Longnecker
Theodore S Jardetzky
Northwestern University · USStanford University · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM008152 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI ARDEHALI, HOSSEIN · 1987 to 2021
$24.0M
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
Functional Studies of gp42 and HLA Class 11 in EBVR01CA093444 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI LONGNECKER, RICHARD M · 2002 to 2006
$1.8M
Training Program in Viral ReplicationT32AI060523 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI LAIMINS, LAIMONIS A. · 2004 to 2013
$1.4M
NCI NIH HHS CA117794NCI NIH HHS CA93444NCI NIH HHS R01 CA093444NCI NIH HHS R01 CA117794NIAID NIH HHS R01 AI076183NIAID NIH HHS T32 AI060523NIGMS NIH HHS 5 T32 GM008152NIGMS NIH HHS T32 GM008152
6 · The paper itself

Abstract

Epstein-Barr virus requires glycoproteins gH/gL, gB, and gp42 to fuse its lipid envelope with B cells. Gp42 is a type II membrane protein consisting of a flexible N-terminal region, which binds gH/gL, and a C-terminal lectin-like domain that binds to the B-cell entry receptor human leukocyte antigen (HLA) class II. Gp42 triggers membrane fusion after HLA binding, a process that requires simultaneous binding to gH/gL and a functional hydrophobic pocket in the lectin domain adjacent to the HLA binding site. Here we present the structure of gp42 in its unbound form. Comparisons to the previously determined structure of a gp42:HLA complex reveals additional N-terminal residues forming part of the gH/gL binding site and structural changes in the receptor binding domain. Although the core of the lectin domain remains similar, significant shifts in two loops and an alpha helix bordering the essential hydrophobic pocket suggest a structural mechanism for triggering fusion.

Indexed as

Virus InternalizationAnimalsBinding SitesB-LymphocytesCells, CulturedCHO CellsCricetinaeCricetulusHerpesvirus 4, HumanHLA AntigensMembrane GlycoproteinsModels, BiologicalModels, MolecularProtein BindingProtein ConformationProtein Interaction Domains and MotifsHLA AntigensMembrane GlycoproteinsViral Proteins

Identifiers

PMID19217393
PMCPMC3085316
OpenAlexW2068289773

What OpenQuestion holds

Textmetadata
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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.