Evidence map›Paper›PMID 26861873›Full record

ArticleThe Journal of biological chemistry2016

Identification and Characterization of IgdE, a Novel IgG-degrading Protease of Streptococcus suis with Unique Specificity for Porcine IgG.

Christian Spoerry, Jana Seele, Peter Valentin-Weigand, Christoph G Baums, Ulrich von Pawel-Rammingen

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

15 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Article
  4. Top-Down and Middle-Down Mass Spectrometry of Antibodies.Molecular & cellular proteomics : MCP · 2025
    Review
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  8. Virulence · 2021
    Article
  9. Article
  10. Selectivity over coverage inChemical science · 2020
    Article
  11. Review
  12. Article
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  14. Review
  15. 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

5 authors.

Christian SpoerryFrom the Department of Molecular Biology and Umeå Centre for Microbial Research, Umeå University, 90187 Umeå, Sweden.
Jana Seelethe Institute for Microbiology, Center for Infection Medicine, University of Veterinary Medicine Hannover, 30173 Hannover, Germany, and.
Peter Valentin-Weigandthe Institute for Microbiology, Center for Infection Medicine, University of Veterinary Medicine Hannover, 30173 Hannover, Germany, and.
Christoph G Baumsthe Institute for Microbiology, Center for Infection Medicine, University of Veterinary Medicine Hannover, 30173 Hannover, Germany, and the Institute for Bacteriology und Mycology, Centre for Infectious Diseases, College of Veterinary Medicine, University Leipzig, 04103 Leipzig, Germany.
Ulrich von Pawel-RammingenFrom the Department of Molecular Biology and Umeå Centre for Microbial Research, Umeå University, 90187 Umeå, Sweden, ulrich.von-pawel@molbiol.umu.se.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Streptococcus suisis a major endemic pathogen of pigs causing meningitis, arthritis, and other diseases. ZoonoticS. suisinfections are emerging in humans causing similar pathologies as well as severe conditions such as toxic shock-like syndrome. Recently, we discovered an IdeS family protease ofS. suisthat exclusively cleaves porcine IgM and represents the first virulence factor described, linkingS. suisto pigs as their natural host. Here we report the identification and characterization of a novel, unrelated protease ofS. suisthat exclusively targets porcine IgG. This enzyme, designated IgdE forimmunoglobulinG-degradingenzyme ofS. suis, is a cysteine protease distinct from previous characterized streptococcal immunoglobulin degrading proteases of the IdeS family and mediates efficient cleavage of the hinge region of porcine IgG with a high degree of specificity. The findings that allS. suisstrains investigated possess the IgG proteolytic activity and that piglet serum samples contain specific antibodies against IgdE strongly indicate that the protease is expressedin vivoduring infection and represents a novel and putative important bacterial virulence/colonization determinant, and a thus potential therapeutic target.

Indexed as

Amino Acid SequenceAnimalsBacterial ProteinsCatalytic DomainCysteine ProteasesImmunoglobulin GModels, MolecularMolecular Sequence DataProteolysisStreptococcal InfectionsStreptococcus suisSubstrate SpecificitySwineBacterial ProteinsCysteine ProteasesImmunoglobulin Gantibodycysteine proteaseimmunoglobulin G (IgG)proteolytic enzymeStreptococcussubstrate specificity

Identifiers

PMID26861873
PMCPMC4824999

What OpenQuestion holds

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Registered trials

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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.