Evidence map›Paper›PMID 22491453›Full record

ArticleJournal of virology2012

Characterization of the viral O-glycopeptidome: a novel tool of relevance for vaccine design and serodiagnosis.

Emiliano Cló, Stjepan K Kracun, Aaron S Nudelman, Knud J Jensen, Jan-Åke Liljeqvist, Sigvard Olofsson, Tomas Bergström, Ola Blixt

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-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

20 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Multiplexed Detection of Autoantibodies to Glycopeptides Using Microarray.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Glycan Array Technology.Advances in biochemical engineering/biotechnology · 2021
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Tumor-targeting peptides from combinatorial libraries.Advanced drug delivery reviews · 2017
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Carbohydrate microarrays.Chemical Society reviews · 2013
    Review
  20. Review
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 2 institutions in 2 countries.

Emiliano ClóCopenhagen Center for Glycomics, Department of Cellular & Molecular Medicine, University of Copenhagen, Copenhagen, Denmark.
Stjepan K Kracun
Aaron S Nudelman
Knud J Jensen
Jan-Åke Liljeqvist
Sigvard Olofsson
Tomas Bergström
Ola Blixt
University of Gothenburg · SEUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Viral envelope proteins mediate interactions with host cells, leading to internalization and intracellular propagation. Envelope proteins are glycosylated and are known to serve important functions in masking host immunity to viral glycoproteins. However, the viral infectious cycle in cells may also lead to aberrant glycosylation that may elicit immunity. Our knowledge of immunity to aberrant viral glycans and glycoproteins is limited, potentially due to technical limitations in identifying immunogenic glycans and glycopeptide epitopes. This work describes three different complementary methods for high-throughput screening and identification of potential immunodominant O-glycopeptide epitopes on viral envelope glycoproteins: (i) on-chip enzymatic glycosylation of scan peptides, (ii) chemical glycopeptide microarray synthesis, and (iii) a one-bead-one-compound random glycopeptide library. We used herpes simplex virus type 2 (HSV-2) as a model system and identified a simple O-glycopeptide pan-epitope, (501)PPA(GalNAc)TAPG(507), on the mature gG-2 glycoprotein that was broadly recognized by IgG antibodies in HSV-2-infected individuals but not in HSV-1-infected or noninfected individuals. Serum reactivity to the extended sialyl-T glycoform was tolerated, suggesting that self glycans can participate in immune responses. The methods presented provide new insight into viral immunity and new targets for immunodiagnostic and therapeutic measures.

Indexed as

Computational BiologyEpitopesGlycoproteinsHerpesvirus 2, HumanHumansPolysaccharidesSerologic TestsVaccinesViral Envelope ProteinsEpitopesGlycoproteinsPolysaccharidesVaccinesViral Envelope Proteins

Identifiers

PMID22491453
PMCPMC3372205
OpenAlexW2133780183

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.