Evidence map›Paper›PMID 15128793›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2004

Glycoprotein 96 can chaperone both MHC class I- and class II-restricted epitopes for in vivo presentation, but selectively primes CD8+ T cell effector function.

Amy D H Doody, Joseph T Kovalchin, Marianne A Mihalyo, Adam T Hagymasi, Charles G Drake, Adam J Adler

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

48 citing papers in PubMed, 141 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. A new antisarcoma strategy: multisubtype heat shock protein/peptide immunotherapy combined with PD-L1 immunological checkpoint inhibitors.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2021
    Article
  5. The HSP Immune Network in Cancer.Frontiers in immunology · 2021
    Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Immunogenic Apoptosis as a Novel Tool for Anticancer Vaccine Development.International journal of molecular sciences · 2018
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Clients and Oncogenic Roles of Molecular Chaperone gp96/grp94.Current topics in medicinal chemistry · 2016
    Review
  16. Article
  17. Review
  18. Article
  19. 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

6 authors at 2 institutions in 1 country.

Amy D H DoodyCenter for Immunotherapy of Cancer and Infectious Diseases, University of Connecticut Health Center, Farmington, CT 06030, USA.
Joseph T Kovalchin
Marianne A Mihalyo
Adam T Hagymasi
Charles G Drake
Adam J Adler
UConn Health · USSidney Kimmel Comprehensive Cancer Center · US

Funding

Comparing Toleragenic Versus Immunogenic APC FunctionR21AI049813 · NIAID · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI ADLER, ADAM J · 2001 to 2003
$651k
NIAID NIH HHS AI49813NIAID NIH HHS R21 AI049813
6 · The paper itself

Abstract

The ability of mature T lymphocytes to develop effector capacity after encounter with cognate Ag is generally dependent upon inflammatory signals associated with infection that induce dendritic cell activation/maturation. These inflammatory signals can derive directly from pathogens or can be expressed by host cells in response to infection. Heat shock proteins (HSPs) are a class of host-derived inflammatory mediators that perform the dual function of both chaperoning MHC class I-restricted epitopes into the cross-presentation pathway of DCs and inducing the activation/maturation of these DCs to allow priming of cognate CD8(+) T cell effector responses. Although the ability of HSPs to elicit effector CD8 cell responses has been well established, their potential to prime CD4 cell effector responses has been relatively unexplored. In the current study we compared the ability of the endoplasmic reticulum-resident HSP gp96 to prime CD4 vs CD8 cells using TCR transgenic adoptive transfer systems and soluble gp96-peptide complexes. As expected, gp96 facilitated the cross-presentation of a class I-restricted peptide and priming of effector function in cognate CD8 cells. Interestingly, gp96 also facilitated the in vivo presentation of a class II-restricted peptide; however, the resulting CD4 cell response did not involve the development of effector function. Taken together, these data suggest that gp96 is an inflammatory mediator that selectively primes CD8 cell effector function.

Indexed as

AnimalsAntigen PresentationAntigens, NeoplasmCD4-Positive T-LymphocytesCD8-Positive T-LymphocytesClonal AnergyCytotoxicity, ImmunologicEpitopes, T-LymphocyteHeat-Shock ProteinsHistocompatibility Antigens Class IHistocompatibility Antigens Class IIInflammation MediatorsLymphocyte ActivationMiceMice, Inbred C57BLMice, TransgenicAntigens, NeoplasmEpitopes, T-LymphocyteHeat-Shock ProteinsHistocompatibility Antigens Class IHistocompatibility Antigens Class IIInflammation MediatorsMolecular Chaperonessarcoma glycoprotein gp96 rejection antigens

Identifiers

PMID15128793
PMCPMC2846363
OpenAlexW1540090690

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.