Evidence map›Paper›PMID 27140614›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Peptidoglycan-linked protein A promotes T cell-dependent antibody expansion during Staphylococcus aureus infection.

Hwan Keun Kim, Fabiana Falugi, Dominique M Missiakas, Olaf Schneewind

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

32 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Immunoglobulin G subclasses confer protection againstProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Antimicrobial Treatment ofAntibiotics (Basel, Switzerland) · 2023
    Review
  9. Article
  10. Engineered human antibodies for the opsonization and killing ofProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. The molecular characterization of antibody binding to a superantigen-like protein from a commensal microbe.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Glycosylation-dependent opsonophagocytic activity of staphylococcal protein A antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  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

4 authors at 1 institution in 1 country.

Hwan Keun KimDepartment of Microbiology, University of Chicago, Chicago, IL 60637.
Fabiana FalugiDepartment of Microbiology, University of Chicago, Chicago, IL 60637.
Dominique M MissiakasDepartment of Microbiology, University of Chicago, Chicago, IL 60637.
Olaf SchneewindDepartment of Microbiology, University of Chicago, Chicago, IL 60637 oschnee@bsd.uchicago.edu.
University of Chicago · US

Funding

Surface Proteins of Gram-Positive BacteriaR01AI038897 · NIAID · UNIVERSITY OF CHICAGO · PI MISSIAKAS, DOMINIQUE M. · 1996 to 2024
$8.9M
Vaccine Assembly from Surface Proteins of Staphylococcus AureusR01AI052474 · NIAID · UNIVERSITY OF CHICAGO · PI Dominique Missiakas · 2002 to 2026
$8.8M
NIAID NIH HHS R01 AI038897NIAID NIH HHS R01 AI052474
6 · The paper itself

Abstract

A hallmark of Staphylococcus aureus disease in humans is persistent infections without development of protective immune responses. Infected patients generate VH3 plasmablast expansions and increased VH3 idiotype Ig; however, the mechanisms for staphylococcal modification of immune responses are not known. We report here that S. aureus-infected mice generate VH3 antibody expansions via a mechanism requiring MHC-restricted antigen presentation to CD4(+) T cells and staphylococcal protein A (SpA), a cell wall-anchored surface molecule that binds Fcγ and VH3 variant heavy chains of Ig. VH3 expansion occurred with peptidoglycan-linked SpA from the bacterial envelope but not with recombinant SpA, and optimally required five tandem repeats of its Ig-binding domains. Signaling via receptor-interacting serine/threonine protein kinase 2 (RIPK2) was essential for implementing peptidoglycan-linked SpA superantigen activity. VH3 clan IgG from S. aureus-infected or SpA-treated animals was not pathogen-specific, suggesting that SpA cross-linking of VH3 idiotype B-cell receptors and activation via attached peptidoglycan are the determinants of staphylococcal escape from adaptive immune responses.

Indexed as

AnimalsAntibodies, BacterialAntibody FormationMice, Inbred BALB CMice, Inbred C57BLPeptidoglycanStaphylococcal InfectionsStaphylococcal Protein AStaphylococcus aureusT-LymphocytesAntibodies, BacterialPeptidoglycanStaphylococcal Protein AB-cell superantigenRIPK2staphylococcal protein AT cellVH3 clonal antibody

Identifiers

PMID27140614
PMCPMC4878465
OpenAlexW2345602998

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.