Evidence map›Paper›PMID 23589297›Full record

ArticleThe Journal of biological chemistry2013

Cysteine proteinase from Streptococcus pyogenes enables evasion of innate immunity via degradation of complement factors.

Mariko Honda-Ogawa, Taiji Ogawa, Yutaka Terao, Tomoko Sumitomo, Masanobu Nakata, Kazunori Ikebe, Yoshinobu Maeda, Shigetada Kawabata

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
6.8field-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

40 citing papers in PubMed, 76 citations in OpenAlex.

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  16. IL-33/ST2 Axis Plays a Protective Effect inInternational journal of molecular sciences · 2021
    Article
  17. Article
  18. Review
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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

8 authors at 2 institutions in 1 country.

Mariko Honda-OgawaDepartment of Oral and Molecular Microbiology, Osaka University Graduate School of Dentistry, 1-8, Yamadaoka, Suita, Osaka 565-0871, Japan.
Taiji Ogawa
Yutaka Terao
Tomoko Sumitomo
Masanobu Nakata
Kazunori Ikebe
Yoshinobu Maeda
Shigetada Kawabata
Osaka University · JPNiigata University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Streptococcus pyogenes is an important human pathogen that causes invasive diseases such as necrotizing fasciitis, sepsis, and streptococcal toxic shock syndrome. We investigated the function of a major cysteine protease from S. pyogenes that affects the amount of C1-esterase inhibitor (C1-INH) and other complement factors and aimed to elucidate the mechanism involved in occurrence of streptococcal toxic shock syndrome from the aspect of the complement system. First, we revealed that culture supernatant of a given S. pyogenes strain and recombinant SpeB degraded the C1-INH. Then, we determined the N-terminal sequence of the C1-INH fragment degraded by recombinant SpeB. Interestingly, the region containing one of the identified cleavage sites is not present in patients with C1-INH deficiency. Scanning electron microscopy of the speB mutant incubated in human serum showed the abnormal superficial architecture and irregular oval structure. Furthermore, unlike the wild-type strain, that mutant strain showed lower survival capacity than normal as compared with heat-inactivated serum, whereas it had a significantly higher survival rate in serum without the C1-INH than in normal serum. Also, SpeB degraded multiple complement factors and the membrane attack complex. Flow cytometric analyses revealed deposition of C9, one of the components of membrane the attack complex, in greater amounts on the surface of the speB mutant, whereas lower amounts of C9 were bound to the wild-type strain surface. These results suggest that SpeB can interrupt the human complement system via degrading the C1-INH, thus enabling S. pyogenes to evade eradication in a hostile environment.

Indexed as

Immune EvasionImmunity, InnateProteolysisBacterial ProteinsComplement C1 Inhibitor ProteinComplement C9Complement Membrane Attack ComplexCysteine EndopeptidasesExotoxinsHumansProtein Structure, TertiaryStreptococcus pyogenesBacterial ProteinsComplement C1 Inhibitor ProteinComplement C9Complement Membrane Attack ComplexCysteine Endopeptidaseserythrogenic toxinExotoxinsC1-Esterase InhibitorComplement SystemCysteine ProteaseInnate ImmunityMembrane Attack ComplexProtease InhibitorSpeBStreptococcus pyogenes

Identifiers

PMID23589297
PMCPMC3668742
OpenAlexW2080840270

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.