Evidence map›Paper›PMID 14970177›Full record

ArticleThe Journal of experimental medicine2004

N-linked glycosylation is required for optimal function of Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6.

Charles S Dela Cruz, Yoomi Lee, Srinivas R Viswanathan, Ayman S El-Guindy, Jennifer Gerlach, Sarah Nikiforow, Duane Shedd, Lyn Gradoville, George Miller

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Cytokine homologs of human gammaherpesviruses.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2012
    Review
  12. Viral interleukin-6: role in Kaposi's sarcoma-associated herpesvirus: associated malignancies.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2011
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

9 authors at 1 institution in 1 country.

Charles S Dela CruzDepartment of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520, USA.
Yoomi Lee
Srinivas R Viswanathan
Ayman S El-Guindy
Jennifer Gerlach
Sarah Nikiforow
Duane Shedd
Lyn Gradoville
George Miller
Yale University · US

Funding

AIDS LYMPHOMA--HARBORING TWO GAMMA HERPESVIRUSESR01CA070036 · NCI · YALE UNIVERSITY · PI MILLER, I. GEORGE · 1995 to 2003
$1.4M
NCI NIH HHS CA70036NCI NIH HHS R01 CA070036
6 · The paper itself

Abstract

Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6). hIL-6 and vIL-6 exhibit similar biological functions and both act via the gp130 receptor subunit to activate the Janus tyrosine kinase (JAK)1 and signal transducer and activator of transcription (STAT)1/3 pathway. Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay. Although hIL-6 is also N-glycosylated at N73 and multiply O-glycosylated, neither N-linked nor O-linked glycosylation is necessary for IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3. As distinct from vIL-6, unglycosylated hIL-6 is as potent as glycosylated hIL-6 in stimulating B cell proliferation. These findings highlight distinct functional roles of N-linked glycosylation in viral and cellular IL-6.

Indexed as

B-LymphocytesCell DivisionCell LineCell Line, TumorCloning, MolecularContactinsEscherichia coliGlycosylationHerpesvirus 8, HumanHumansInterleukin-6Lymphocyte ActivationNeural Cell Adhesion MoleculesPeptide FragmentsPlasmidsRecombinant ProteinsContactinsInterleukin-6Neural Cell Adhesion MoleculesPeptide FragmentsRecombinant Proteins

Identifiers

PMID14970177
PMCPMC2211829
OpenAlexW2112636167

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.