Evidence map›Paper›PMID 23086939›Full record

ArticleThe Journal of biological chemistry2012

Characterization of streptokinases from group A Streptococci reveals a strong functional relationship that supports the coinheritance of plasminogen-binding M protein and cluster 2b streptokinase.

Yueling Zhang, Zhong Liang, Hsing-Tse Hsueh, Victoria A Ploplis, Francis J Castellino

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. 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
5.0field-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, 45 citations in OpenAlex.

  1. Trial
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  3. Group aMicrobiology spectrum · 2025
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  10. Group AFrontiers in cardiovascular medicine · 2021
    Article
  11. A unique combination of glycoside hydrolases inThe Journal of biological chemistry · 2020
    Article
  12. Article
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  15. Article
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  18. Conformationally organized lysine isosteres inThe Journal of biological chemistry · 2017
    Article
  19. 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.

Yueling ZhangW. M. Keck Center for Transgene Research and Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, USA. .
Zhong Liang
Hsing-Tse Hsueh
Victoria A Ploplis
Francis J Castellino
University of Notre Dame · US

Funding

STRUCTURE-FUNCTION STUDIES ON PLASMINOGEN AND PLASMINR01HL013423 · NHLBI · UNIVERSITY OF NOTRE DAME · PI CASTELLINO, FRANCIS J, LEE, SHAUN · 1985 to 2021
$7.9M
Plasminogen and Plasmin: Structure and FunctionR56HL013423 · NHLBI · UNIVERSITY OF NOTRE DAME · PI CASTELLINO, FRANCIS J, LEE, SHAUN · 2022 to 2022
$743k
STRUCTURE/FUNCTION STUDIES ON PLASMINOGEN AND PLASMINR37HL013423 · NHLBI · UNIVERSITY OF NOTRE DAME · PI CASTELLINO, FRANCIS J · 1990 to 1999
–
NHLBI NIH HHS HL013423NHLBI NIH HHS R01 HL013423NHLBI NIH HHS R37 HL013423NHLBI NIH HHS R56 HL013423
6 · The paper itself

Abstract

Group A streptococcus (GAS) strains secrete the protein streptokinase (SK), which functions by activating host human plasminogen (hPg) to plasmin (hPm), thus providing a proteolytic framework for invasive GAS strains. The types of SK secreted by GAS have been grouped into two clusters (SK1 and SK2) and one subcluster (SK2a and SK2b). SKs from cluster 1 (SK1) and cluster 2b (SK2b) display significant evolutionary and functional differences, and attempts to relate these properties to GAS skin or pharynx tropism and invasiveness are of great interest. In this study, using four purified SKs from each cluster, new relationships between plasminogen-binding group A streptococcal M (PAM) protein and SK2b have been revealed. All SK1 proteins efficiently activated hPg, whereas all subclass SK2b proteins only weakly activated hPg in the absence of PAM. Surface plasmon resonance studies revealed that the lower affinity of SK2b to hPg served as the basis for the attenuated activation of hPg by SK2b. Binding of hPg to either human fibrinogen (hFg) or PAM greatly enhanced activation of hPg by SK2b but minimally influenced the already effective activation of hPg by SK1. Activation of hPg in the presence of GAS cells containing PAM demonstrated that PAM is the only factor on the surface of SK2b-expressing cells that enabled the direct activation of hPg by SK2b. As the binding of hPg to PAM is necessary for hPg activation by SK2b, this dependence explains the coinherant relationship between PAM and SK2b and the ability of these particular strains to generate the proteolytic activity that disrupts the innate barriers that limit invasiveness.

Indexed as

ProteolysisAmino Acid SequenceAnimalsBacterial ProteinsCarrier ProteinsCell LineEnzyme ActivationHumansMolecular Sequence DataPlasminogenProtein BindingSheepStreptococcal InfectionsStreptococcus pyogenesStreptokinaseBacterial ProteinsCarrier ProteinsPlasminogenplasminogen-binding protein, bacteriaStreptokinase

Identifiers

PMID23086939
PMCPMC3516755
OpenAlexW2068047966

What OpenQuestion holds

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LicenceCC BY-NC
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.