Evidence map›Paper›PMID 14517274›Full record

ArticleThe Journal of experimental medicine2003

Evasion of phagocytosis through cooperation between two ligand-binding regions in Streptococcus pyogenes M protein.

Fredric Carlsson, Karin Berggård, Margaretha Stålhammar-Carlemalm, Gunnar Lindahl

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
10.5field-weighted citation impact, top 2% 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

59 citing papers in PubMed, 158 citations in OpenAlex.

  1. Molecular & cellular proteomics : MCP · 2018
    Trial
  2. Trial
  3. Review
  4. Article
  5. Article
  6. EmergentInfection and immunity · 2024
    Article
  7. Article
  8. The germ theory revisited: A noncentric view on infection outcome.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Diverse Functions of C4b-Binding Protein in Health and Disease.Journal of immunology (Baltimore, Md. : 1950) · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Subdominance in Antibody Responses: Implications for Vaccine Development.Microbiology and molecular biology reviews : MMBR · 2020
    Review
  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

4 authors at 1 institution in 1 country.

Fredric CarlssonDept. of Medical Microbiology, Dermatology, and Infection, Lund University, Sölvegatan 23, SE-22362 Lund, Sweden.
Karin Berggård
Margaretha Stålhammar-Carlemalm
Gunnar Lindahl
Lund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The M protein of Streptococcus pyogenes is a major bacterial virulence factor that confers resistance to phagocytosis. To analyze how M protein allows evasion of phagocytosis, we used the M22 protein, which has features typical of many M proteins and has two well-characterized regions binding human plasma proteins: the hypervariable NH2-terminal region binds C4b-binding protein (C4BP), which inhibits the classical pathway of complement activation; and an adjacent semivariable region binds IgA-Fc. Characterization of chromosomal S. pyogenes mutants demonstrated that each of the ligand-binding regions contributed to phagocytosis resistance, which could be fully explained as cooperation between the two regions. Deposition of complement on S. pyogenes occurred almost exclusively via the classical pathway, even under nonimmune conditions, but was down-regulated by bacteria-bound C4BP, providing an explanation for the ability of bound C4BP to inhibit phagocytosis. Different opsonizing antisera shared the ability to block binding of both C4BP and IgA, suggesting that the two regions in M22 play important roles also under immune conditions, as targets for protective antibodies. These data indicate that M22 and similar M proteins confer resistance to phagocytosis through ability to bind two components of the human immune system.

Indexed as

Antigens, BacterialGlycoproteinsPhagocytosisAmino Acid SequenceAnimalsAntibodies, BacterialBacterial Outer Membrane ProteinsBinding SitesCarrier ProteinsComplement Inactivator ProteinsComplement Pathway, ClassicalHumansImmunoglobulin AMolecular Sequence DataRabbitsStreptococcus pyogenesAntibodies, BacterialAntigens, BacterialBacterial Outer Membrane ProteinsCarrier ProteinsComplement Inactivator ProteinsGlycoproteinsImmunoglobulin Astreptococcal M protein

Identifiers

PMID14517274
PMCPMC2194224
OpenAlexW2162575803

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.