Evidence map›Paper›PMID 22114560›Full record

ArticlePLoS pathogens2011

Antibody evasion by a gammaherpesvirus O-glycan shield.

Bénédicte Machiels, Céline Lété, Antoine Guillaume, Jan Mast, Philip G Stevenson, Alain Vanderplasschen, Laurent Gillet

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

38 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Glycoprotein molecular dynamics analysis: SARS-CoV-2 spike glycoprotein case study.Advances in protein chemistry and structural biology · 2022
    Article
  11. Article
  12. Mucin-Type O-GalNAc Glycosylation in Health and Disease.Advances in experimental medicine and biology · 2021
    Article
  13. Article
  14. MASS SPECTROMETRY IN VIROLOGICAL SCIENCES.Mass spectrometry reviews · 2020
    Review
  15. The SARS-CoV-2 Coronavirus and the COVID-19 Outbreak.International braz j urol : official journal of the Brazilian Society of Urology · 2020
    Review
  16. Article
  17. Article
  18. Article
  19. Exploitation of glycosylation in enveloped virus pathobiology.Biochimica et biophysica acta. General subjects · 2019
    Review
  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

7 authors at 3 institutions in 2 countries.

Bénédicte MachielsImmunology-Vaccinology B43b, Department of Infectious and Parasitic Diseases B43b, Faculty of Veterinary Medicine, University of Liège, Liège, Belgium.
Céline Lété
Antoine Guillaume
Jan Mast
Philip G Stevenson
Alain Vanderplasschen
Laurent Gillet
University of Liège · BEUniversity of Cambridge · GBVeterinary and Agrochemical Research Centre · BE

Funding

Medical Research Council G0701185Medical Research Council G9800943Wellcome TrustWellcome Trust GR076956MA
6 · The paper itself

Abstract

All gammaherpesviruses encode a major glycoprotein homologous to the Epstein-Barr virus gp350. These glycoproteins are often involved in cell binding, and some provide neutralization targets. However, the capacity of gammaherpesviruses for long-term transmission from immune hosts implies that in vivo neutralization is incomplete. In this study, we used Bovine Herpesvirus 4 (BoHV-4) to determine how its gp350 homolog--gp180--contributes to virus replication and neutralization. A lack of gp180 had no impact on the establishment and maintenance of BoHV-4 latency, but markedly sensitized virions to neutralization by immune sera. Antibody had greater access to gB, gH and gL on gp180-deficient virions, including neutralization epitopes. Gp180 appears to be highly O-glycosylated, and removing O-linked glycans from virions also sensitized them to neutralization. It therefore appeared that gp180 provides part of a glycan shield for otherwise vulnerable viral epitopes. Interestingly, this O-glycan shield could be exploited for neutralization by lectins and carbohydrate-specific antibody. The conservation of O-glycosylation sites in all gp350 homologs suggests that this is a general evasion mechanism that may also provide a therapeutic target.

Indexed as

Amino Acid SequenceAnimalsEpitopesGlycosylationHerpesvirus 4, BovineMembrane GlycoproteinsMolecular Sequence DataNeutralization TestsRabbitsSequence AlignmentViral Envelope ProteinsVirionVirus ReplicationEpitopesMembrane GlycoproteinsViral Envelope Proteins

Identifiers

PMID22114560
PMCPMC3219721
OpenAlexW2060425354

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.