Evidence map›Paper›PMID 21550622›Full record

ArticleVirology2011

Investigation of the function of the putative self-association site of Epstein-Barr virus (EBV) glycoprotein 42 (gp42).

Cynthia L Rowe, Hisae Matsuura, Theodore S Jardetzky, Richard Longnecker

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.4field-weighted citation impact, top 36% 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

7 citing papers in PubMed, 8 citations in OpenAlex.

  1. Neutralizing antibodies against EBV gp42 show potentEmerging microbes & infections · 2023
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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.

Cynthia L RoweDepartment of Microbiology and Immunology, The Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA. c-rowe@northwestern.edu
Hisae Matsuura
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
EBV gB Function in Viral Fusion, Entry, and EgressR01AI067048 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI LONGNECKER, RICHARD M · 2007 to 2011
$1.9M
Discovery of New Treatment Options for EBV-associated Lymphoma and PTLDR01CA133063 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI LONGNECKER, RICHARD M · 2008 to 2012
$1.9M
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 CA133063NCI NIH HHS R01 CA093444NCI NIH HHS R01 CA117794NCI NIH HHS R01 CA133063NIAID NIH HHS AI067048NIAID NIH HHS AI076183NIAID NIH HHS R01 AI067048NIAID NIH HHS R01 AI076183
6 · The paper itself

Abstract

The Epstein-Barr virus (EBV) glycoprotein 42 (gp42) is a type II membrane protein essential for entry into B cells but inhibits entry into epithelial cells. X-ray crystallography suggests that gp42 may form dimers when bound to human leukocyte antigen (HLA) class II receptor (Mullen et al., 2002) or multimerize when not bound to HLA class II (Kirschner et al., 2009). We investigated this self-association of gp42 using several different approaches. We generated soluble mutants of gp42 containing mutations within the self-association site and found that these mutants have a defect in fusion. The gp42 mutants bound to gH/gL and HLA class II, but were unable to bind wild-type gp42 or a cleavage mutant of gp42. Using purified gp42, gH/gL, and HLA, we found these proteins associate 1:1:1 by gel filtration suggesting that gp42 dimerization or multimerization does not occur or is a transient event undetectable by our methods.

Indexed as

AnimalsCell LineEpstein-Barr Virus InfectionsGlycoproteinsHerpesvirus 4, HumanHistocompatibility Antigens Class IIHumansProtein BindingProtein MultimerizationViral ProteinsBZLF2 protein, Herpesvirus 4, HumanGlycoproteinsHistocompatibility Antigens Class IIViral Proteins

Identifiers

PMID21550622
PMCPMC3107886
OpenAlexW1974105917

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.