Evidence map›Paper›PMID 23532847›Full record

ArticleThe Journal of biological chemistry2013

Group A streptococcal cysteine protease cleaves epithelial junctions and contributes to bacterial translocation.

Tomoko Sumitomo, Masanobu Nakata, Miharu Higashino, Yutaka Terao, 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 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
5.2field-weighted citation impact, top 5% 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

33 citing papers in PubMed, 55 citations in OpenAlex.

  1. Trial
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  7. Research progress on the microbiota in bladder cancer tumors.Frontiers in cellular and infection microbiology · 2024
    Review
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  9. Review
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  11. Article
  12. Article
  13. Article
  14. Playing With Fire: Proinflammatory Virulence Mechanisms of Group AFrontiers in cellular and infection microbiology · 2021
    Review
  15. Article
  16. Article
  17. Article
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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

5 authors at 1 institution in 1 country.

Tomoko SumitomoDepartment of Oral and Molecular Microbiology, Osaka University Graduate School of Dentistry, Suita, Osaka, 565-0871, Japan.
Masanobu Nakata
Miharu Higashino
Yutaka Terao
Shigetada Kawabata
Osaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundGroup A Streptococcus (GAS) translocates across the host epithelial barrier.

resultsStreptococcal pyrogenic exotoxin B (SpeB) directly cleaves junctional proteins.

conclusionThe proteolytic efficacy of SpeB allows GAS to translocate across the epithelial barrier. SIGNIFICANCE: SpeB-mediated dysfunction of the epithelial barrier may have important implications for not only bacterial invasion but also dissemination of other virulence factors throughout intercellular spaces. Group A Streptococcus (GAS) is an important human pathogen that possesses an ability to translocate across the epithelial barrier. In this study, culture supernatants of tested GAS strains showed proteolytic activity against human occludin and E-cadherin. Utilizing various types of protease inhibitors and amino acid sequence analysis, we identified SpeB (streptococcal pyrogenic exotoxin B) as the proteolytic factor that cleaves E-cadherin in the region neighboring the calcium-binding sites within the extracellular domain. The cleaving activities of culture supernatants from several GAS isolates were correlated with the amount of active SpeB, whereas culture supernatants from an speB mutant showed no such activities. Of note, the wild type strain efficiently translocated across the epithelial monolayer along with cleavage of occludin and E-cadherin, whereas deletion of the speB gene compromised those activities. Moreover, destabilization of the junctional proteins was apparently relieved in cells infected with the speB mutant, as compared with those infected with the wild type. Taken together, our findings indicate that the proteolytic efficacy of SpeB in junctional degradation allows GAS to invade deeper into tissues.

Indexed as

Bacterial TranslocationAntigens, CDBacterial ProteinsCaco-2 CellsCadherinsCysteine EndopeptidasesElectric ImpedanceEpithelial CellsEpitheliumExotoxinsHost-Pathogen InteractionsHumansIntercellular JunctionsProtein Structure, TertiaryProteolysisSequence DeletionAntigens, CDBacterial ProteinsCadherinsCDH1 protein, humanCysteine Endopeptidaseserythrogenic toxinExotoxinsBacterial PathogenesisCell PolarityCysteine ProteaseEpithelial CellJunctions

Identifiers

PMID23532847
PMCPMC3650370
OpenAlexW2022233387

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.