Evidence map›Paper›PMID 9151851›Full record

ArticleJournal of virology1997

Role of the extracellular domain of human herpesvirus 7 glycoprotein B in virus binding to cell surface heparan sulfate proteoglycans.

P Secchiero, D Sun, A L De Vico, R W Crowley, M S Reitz, G Zauli, P Lusso, R C Gallo

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

32 citing papers in PubMed, 91 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Is heparan sulfate a target for inhibition of RNA virus infection?American journal of physiology. Cell physiology · 2022
    Review
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  16. Amplification of autoimmune disease by infection.Arthritis research & therapy · 2005
    Review
  17. Review
  18. Article
  19. Article
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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

8 authors at 1 institution in 1 country.

P SecchieroInstitute of Human Virology, Medical Biotechnology Center, University of Maryland at Baltimore, 21201, USA. secchier@umbi.umd.edu
D Sun
A L De Vico
R W Crowley
M S Reitz
G Zauli
P Lusso
R C Gallo
University of Maryland, Baltimore · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In an attempt to identify the human herpesvirus 7 (HHV-7) envelope protein(s) involved in cell surface binding, the extracellular domain of the HHV-7 glycoprotein B (gB) homolog protein was cloned and expressed as a fusion product with the Fc domain of human immunoglobulin G heavy chain gamma1 (gB-Fc) in an eukaryotic cell system. Indirect immunofluorescence followed by flow cytometric analysis revealed specific binding of gB-Fc to the membrane of SupT1 cells but not to other CD4+ T-lymphoblastoid cell lines, such as Jurkat or PM1, clearly indicating that gB-Fc did not bind to the CD4 molecule. This was also suggested by the ability of gB-Fc to bind to CD4-negative fibroblastoid Chinese hamster ovary (CHO) cells. The binding was abrogated by enzymatic removal of cell surface heparan sulfate proteoglycans by heparinase and heparitinase but not by treatment with condroitinase ABC. In addition, binding of the gB-Fc fusion protein to CHO cells was severely impaired in the presence of soluble heparin, as well as when heparan sulfate-deficient mutant CHO cells were used. Consistent with these findings, soluble heparin was found to block HHV-7 infection and syncytium formation in the SupT1 cell line. Although the CD4 antigen is a critical component of the receptor for the T-lymphotropic HHV-7, these findings suggest that heparin-like molecules also play an important role in HHV-7-cell surface interactions required for infection and that gB represents one of the HHV-7 envelope proteins involved in the adsorption of virus-to-cell surface proteoglycans.

Indexed as

AnimalsCell FusionCHO CellsCricetinaeGlycosylationHeparan SulfateHeparan Sulfate ProteoglycansHeparinHerpesvirus 7, HumanHumansImmunoglobulin Fc FragmentsMembrane GlycoproteinsProteoglycansReceptors, VirusRecombinant Fusion ProteinsViral Envelope Proteinsglycoprotein B, human herpesvirus 7Heparan SulfateHeparan Sulfate ProteoglycansHeparinImmunoglobulin Fc FragmentsMembrane GlycoproteinsProteoglycansReceptors, VirusRecombinant Fusion ProteinsViral Envelope Proteins

Identifiers

PMID9151851
PMCPMC191679
OpenAlexW1543232849

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.