Evidence map›Paper›PMID 23325693›Full record

ArticleJournal of virology2013

The large groove found in the gH/gL structure is an important functional domain for Epstein-Barr virus fusion.

Jia Chen, Theodore S Jardetzky, Richard Longnecker

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 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

28 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Epithelial cell infection by Epstein-Barr virus.FEMS microbiology reviews · 2019
    Article
  8. Article
  9. Article
  10. Inhibition of EBV-mediated membrane fusion by anti-gHgL antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Structural and biochemical studies of HCMV gH/gL/gO and Pentamer reveal mutually exclusive cell entry complexes.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

3 authors at 2 institutions in 1 country.

Jia ChenDepartment of Microbiology and Immunology, The Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA.
Theodore S Jardetzky
Richard Longnecker
Northwestern University · USStanford University · US

Funding

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
NCI NIH HHS CA117794NCI NIH HHS R01 CA093444NCI NIH HHS R01 CA117794NIAID NIH HHS AI076183NIAID NIH HHS R01 AI076183
6 · The paper itself

Abstract

Epstein-Barr virus (EBV) mediates viral entry into cells using four glycoproteins-gB, the gH/gL complex, and gp42-and fusion is cell type specific. gB and gH/gL are required for epithelial cell fusion; B cell fusion also requires gp42. To investigate functional domains within the gH/gL structure, we constructed site-directed EBV gH/gL mutants with alterations of residues located in a large groove that separates domain I (D-I) from domain II (D-II) within the gH/gL structure. We found that substitution of alanine for leucine 207 reduces both epithelial and B cell fusion and is accompanied by reduced gp42 binding. We also observed that substitution of alanine for arginine 152, histidine 154, or threonine 174 reduces fusion with epithelial cells but not with B cells. To test whether flexibility of the region between D-I and D-II of gH/gL could be important for membrane fusion activity and to allow potential interactions across the D-I/D-II groove, we mutated D-I amino acids V47, P48, and G49 to cysteine, allowing novel intersubunit disulfide bonds to form with the free C153 located in D-II. We found that the G49C mutant, predicted to bridge D-I and D-II with C153 of gH/gL, had normal B cell fusion activity but reduced epithelial cell fusion activity, which was partially restored by treatment with dithiothreitol. We conclude that structural rearrangements and/or interactions across the D-I/D-II groove of gH/gL are required for fusion with epithelial cells but not for fusion with B cells.

Indexed as

Models, MolecularProtein ConformationVirus InternalizationAnimalsBlotting, WesternCHO CellsCricetinaeCricetulusElectrophoresis, Polyacrylamide GelEnzyme-Linked Immunosorbent AssayHerpesvirus 4, HumanLuciferasesMembrane GlycoproteinsMolecular ChaperonesMultiprotein ComplexesMutagenesis, Site-Directedglycoprotein L, Human herpesvirus 4LuciferasesMembrane GlycoproteinsMolecular ChaperonesMultiprotein ComplexesViral Proteins

Identifiers

PMID23325693
PMCPMC3624213
OpenAlexW2058224233

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.