Evidence map›Paper›PMID 17229687›Full record

ArticleJournal of virology2007

Sialic acid on herpes simplex virus type 1 envelope glycoproteins is required for efficient infection of cells.

Jeremy R Teuton, Curtis R Brandt

Abstract read
In one paragraph

Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  4. Review
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  8. Article
  9. Sialic acid-modified antigens impose tolerance via inhibition of T-cell proliferation and de novo induction of regulatory T cells.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. Article
  11. Article
  12. Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILRα.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  13. Article
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  15. 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

2 authors at 2 institutions in 2 countries.

Jeremy R TeutonDepartment of Medical Microbiology and Immunology, University of Wisconsin-Madison, School of Medicine and Public Health, 6630 Medical Sciences Center, 1300 University Avenue, Madison, WI 53706, USA.
Curtis R Brandt
Institute of Molecular and Cell Biology · RUUniversity of Wisconsin–Madison · US

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI HEAD, STEVEN R · 2001 to 2010
$80.3M
UW Vision Research Core - Administrative CoreP30EY016665 · NEI · UNIVERSITY OF WISCONSIN-MADISON · PI AKIHIRO IKEDA · 2005 to 2026
$12.6M
PEPTIDE INHIBITORS OF PAPILLOMAVIRAL INFECTIONP01AI052049 · NIAID · UNIVERSITY OF WISCONSIN MADISON · PI BRANDT, CURTIS R · 2001 to 2004
$3.5M
VIRUS SPECIFIC FACTORS OF HSV TO CORNEAL DISEASER01EY007336 · NEI · UNIVERSITY OF WISCONSIN-MADISON · PI BRANDT, CURTIS R · 1987 to 2008
$1.8M
NEI NIH HHS P30 EY016665NEI NIH HHS R01 EY007336NEI NIH HHS R01-EY07336NIAID NIH HHS P01 AI052049NIAID NIH HHS P01-AI52089NIGMS NIH HHS GM-62116NIGMS NIH HHS U54 GM062116
6 · The paper itself

Abstract

Herpes simplex virus type 1 (HSV-1) envelope proteins are posttranslationally modified by the addition of sialic acids to the termini of the glycan side chains. Although gC, gD, and gH are sialylated, it is not known whether sialic acids on these envelope proteins are functionally important. Digestion of sucrose gradient purified virions for 4 h with neuraminidases that remove both alpha2,3 and alpha2,6 linked sialic acids reduced titers by 1,000-fold. Digestion with a alpha2,3-specific neuraminidase had no effect, suggesting that alpha2,6-linked sialic acids are required for infection. Lectins specific for either alpha2,3 or alpha2,6 linkages blocked attachment and infection to the same extent. In addition, the mobility of gH, gB, and gD in sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels was altered by digestion with either alpha2,3 specific neuraminidase or nonspecific neuraminidases, indicating the presence of both linkages on these proteins. The infectivity of a gC-1-null virus, DeltagC2-3, was reduced to the same extent as wild-type virus after neuraminidase digestion, and attachment was not altered. Neuraminidase digestion of virions resulted in reduced VP16 translocation to the nucleus, suggesting that the block occurred between attachment and entry. These results show for the first time that sialic acids on HSV-1 virions play an important role in infection and suggest that targeting virion sialic acids may be a valid antiviral drug development strategy.

Indexed as

AnimalsAntiviral AgentsCell NucleusChlorocebus aethiopsCytoplasmElectrophoresis, Polyacrylamide GelElectrophoretic Mobility Shift AssayGene DeletionGlycoproteinsHerpes Simplex Virus Protein Vmw65Herpesvirus 1, HumanLectinsN-Acetylneuraminic AcidNeuraminidaseProtein TransportVero CellsAntiviral Agentsbovine herpesvirus type-1 glycoproteinsglycoprotein D, Human herpesvirus 1glycoprotein gC, herpes simplex virus type 1glycoprotein H, herpes simplex virus type 1GlycoproteinsHerpes Simplex Virus Protein Vmw65LectinsN-Acetylneuraminic AcidNeuraminidaseViral Envelope ProteinsViral Proteins

Identifiers

PMID17229687
PMCPMC1866119
OpenAlexW2149644924

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.