Evidence map›Paper›PMID 7722449›Full record

ArticleThe Journal of experimental medicine1995

Intracellular targeting of antigens internalized by membrane immunoglobulin in B lymphocytes.

R N Mitchell, K A Barnes, S A Grupp, M Sanchez, Z Misulovin, M C Nussenzweig, A K Abbas

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

23 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Aberrant B cell receptor signaling from B29 (Igbeta, CD79b) gene mutations of chronic lymphocytic leukemia B cells.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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 1 institution in 1 country.

R N MitchellDepartment of Pathology, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA.
K A Barnes
S A Grupp
M Sanchez
Z Misulovin
M C Nussenzweig
A K Abbas
Brigham and Women's Hospital · US

Funding

SIGNAL TRANSDUCTION BY IGM IN B LYMPHOCYTESR01AI033890 · NIAID · ROCKEFELLER UNIVERSITY · PI NUSSENZWEIG, MICHEL C · 1998 to 2002
$583k
REGULATORY MECHANISMS IN ANTIBODY PRODUCTIONR01AI022802 · NIAID · BRIGHAM AND WOMEN'S HOSPITAL · PI ABBAS, ABUL K. · 1986 to 1994
–
SIGNAL TRANSDUCTION BY IGM IN B LYMPHOCYTESR29AI033890 · NIAID · ROCKEFELLER UNIVERSITY · PI NUSSENZWEIG, MICHEL C · 1993 to 1997
–
NIAID NIH HHS AI-22802NIAID NIH HHS AI-33890NIGMS NIH HHS GM-47726
6 · The paper itself

Abstract

An important function of membrane immunoglobulin (mIg), the B cell antigen receptor, is to endocytose limiting quantities of antigen for efficient presentation to class II-restricted T cells. We have used a panel of mIg mutants to analyze the mechanism of mIg-mediated antigen presentation, and specifically to explore the ability of mIg to target internalized antigen to intracellular processing compartments. Transfected mIgs carrying substitutions for the transmembrane Tyr587 residue fail to efficiently present specifically bound antigen. However, these mutants internalize antigen normally, and their defect cannot be attributed to a lack of mIg-associated Ig alpha/Ig beta molecules. A novel functional assay for detecting antigenic peptides in subcellular fractions shows that wild-type mIg transfectants generate class II-peptide complexes intracellularly, whereas only free antigenic peptides are detectable in the mutant mIg transfectants. Furthermore, an antigen competition assay reveals that antigen internalized by the mutant mIgs fails to enter the intracellular processing compartment accessed by wild-type mIg. Therefore, mIg specifically targets bound and endocytosed antigen to the intracellular compartment where processed peptides associate with class II molecules, and the transmembrane Tyr587 residue plays an obligatory role in this process. Targeting of internalized antigen may be mediated by receptor-associated chaperones, and may be a general mechanism for optimizing the presentation of specifically bound and endocytosed antigens in b lymphocytes and other antigen-presenting cells.

Indexed as

Antigen PresentationAmino Acid SequenceAnimalsB-LymphocytesCell LineEndocytosisMiceMolecular Sequence DataReceptors, Antigen, B-CellTransfectionReceptors, Antigen, B-Cell

Identifiers

PMID7722449
PMCPMC2192014
OpenAlexW2140661709

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.