Evidence map›Paper›PMID 27061054›Full record

ArticleVirology2016

The BDLF3 gene product of Epstein-Barr virus, gp150, mediates non-productive binding to heparan sulfate on epithelial cells and only the binding domain of CD21 is required for infection.

Liudmila S Chesnokova, Sarah M Valencia, Lindsey M Hutt-Fletcher

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Virology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 22% 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

12 citing papers in PubMed, 1 synthesis or guideline pooled it, 19 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Pathogens that infect mammalian cells via sulfonated glycosaminoglycans.Frontiers in cellular and infection microbiology · 2025
    Review
  5. Article
  6. Is heparan sulfate a target for inhibition of RNA virus infection?American journal of physiology. Cell physiology · 2022
    Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. 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 1 institution in 1 country.

Liudmila S ChesnokovaDepartment of Microbiology and Immunology, Center for Molecular and Tumor Virology and Feist-Weiller Cancer Center, Louisiana State University Health Sciences Center, 1501 Kings Highway, Shreveport, LA 71130, USA. Electronic address: lchesn@lsuhsc.edu.
Sarah M ValenciaDepartment of Microbiology and Immunology, Center for Molecular and Tumor Virology and Feist-Weiller Cancer Center, Louisiana State University Health Sciences Center, 1501 Kings Highway, Shreveport, LA 71130, USA. Electronic address: sarah.valencia@nih.gov.
Lindsey M Hutt-FletcherDepartment of Microbiology and Immunology, Center for Molecular and Tumor Virology and Feist-Weiller Cancer Center, Louisiana State University Health Sciences Center, 1501 Kings Highway, Shreveport, LA 71130, USA. Electronic address: lhuttf@lsuhsc.edu.
Louisiana State University Health Sciences Center Shreveport · US

Funding

EBV Entry and Spread in the Oral CavityR01DE016669 · NIDCR · LOUISIANA STATE UNIV HSC SHREVEPORT · PI HUTT-FLETCHER, LINDSEY M. · 2005 to 2013
$3.6M
Early events in infection of epithelial cells with Epstein-Barr VirusF31DE019599 · NIDCR · LOUISIANA STATE UNIV HSC SHREVEPORT · PI VALENCIA, SARAH M · 2008 to 2011
$80k
NIDCR NIH HHS F31 DE019599NIDCR NIH HHS R01 DE016669
6 · The paper itself

Abstract

The cell surface molecules used by Epstein-Barr virus (EBV) to attach to epithelial cells are not well-defined, although when CD21, the B cell receptor for EBV is expressed epithelial cell infection increases disproportionately to the increase in virus bound. Many herpesviruses use low affinity charge interactions with molecules such as heparan sulfate to attach to cells. We report here that the EBV glycoprotein gp150 binds to heparan sulfate proteoglycans, but that attachment via this glycoprotein is not productive of infection. We also report that only the aminoterminal two short consensus repeats of CD21 are required for efficient infection, This supports the hypothesis that, when expressed on an epithelial cell CD21 serves primarily to cluster the major attachment protein gp350 in the virus membrane and enhance access of other important glycoproteins to the epithelial cell surface.

Indexed as

Virus AttachmentAnimalsCell LineCells, CulturedCHO CellsCricetulusEpithelial CellsHeparan SulfateHerpesvirus 4, HumanHumansMembrane GlycoproteinsProtein BindingProtein Interaction Domains and MotifsReceptors, Complement 3dViral ProteinsBDLF-3 protein, Human herpesvirus 4Heparan SulfateMembrane GlycoproteinsReceptors, Complement 3dViral ProteinsCD21Epithelial cell infectionEpstein-Barr virusGlycoprotein 150Heparan-binding

Identifiers

PMID27061054
PMCPMC4884462
OpenAlexW2331645664

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.