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Infection and immunity1999; 67(12); 6478-6486; doi: 10.1128/IAI.67.12.6478-6486.1999

Cloning, expression, sequence analysis, and characterization of streptokinases secreted by porcine and equine isolates of Streptococcus equisimilis.

Abstract: Streptokinases secreted by nonhuman isolates of group C streptococci (Streptococcus equi, S. equisimilis, and S. zooepidemicus) have been shown to bind to different mammalian plasminogens but exhibit preferential plasminogen activity. The streptokinase genes from S. equisimilis strains which activated either equine or porcine plasminogen were cloned, sequenced, and expressed in Escherichia coli. The streptokinase secreted by the equine isolate had little similarity to any known streptokinases secreted by either human or porcine isolates. The streptokinase secreted by the porcine isolate had limited structural and functional similarities to streptokinases secreted by human isolates. Plasminogen activation studies with immobilized (His)(6)-tagged recombinant streptokinases indicated that these recombinant streptokinases interacted with plasminogen in a manner similar to that observed when streptokinase and plasminogen interact in the fluid phase. Analysis of the cleavage products of the streptokinase-plasminogen interaction indicated that human, equine, and porcine plasminogens were all cleaved at the same highly conserved site. The site at which streptokinase was cleaved to form altered streptokinase (Sk*) was also determined. This study confirmed not only the presence of streptokinases in nonhuman S. equisimilis isolates but also that these proteins belong to a family of plasminogen activators more diverse than previously thought.
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Publication Date: 1999-11-24 PubMed ID: 10569766PubMed Central: PMC97058DOI: 10.1128/IAI.67.12.6478-6486.1999Google Scholar: Lookup
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  • Non-U.S. Gov't
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  • U.S. Gov't
  • P.H.S.

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research involves cloning, sequencing, and studying the similarity and differences of streptokinases, specifically those produced by porcine and equine isolates of Streptococcus equisimilis. The findings suggest that these streptokinases cause plasminogen activity and resemble each other in some ways, but they also show some significant differences from known streptokinases.

Streptokinases and Plasminogen Activation

  • The study mentions streptokinases, enzymes produced by various types of streptococci bacteria, including group C species like S. equi, S. equisimilis, and S. zooepidemicus.
  • These streptokinases have been found to bind to different mammals’ plasminogens and demonstrate preferential plasminogen activity, implying they foster the conversion of plasminogen into plasmin, a crucial process in the breakdown of blood clots.

Cloning and Sequencing of Streptokinase Genes

  • The research involved cloning and sequencing streptokinase genes from S. equisimilis strains known to activate either horse or pig plasminogen.
  • The resulting sequenced genes were then expressed in Escherichia coli, a common bacteria often used in genetic research due to its rapid growth and well-understood genetics.

Comparative Analysis of Streptokinases

  • The streptokinase secreted by equine isolate showed minimal similarity to known streptokinases from human and pig isolates. The discrepancy might imply distinct evolutionary paths or functional mechanisms among these enzymes.
  • In contrast, the streptokinase produced by the pig isolate had some structural and functional resemblance to known human streptokinases, although these similarities were limited.

Plasminogen Interaction with Recombinant Streptokinases

  • Experiments with immobilized (His)(6)-tagged recombinant streptokinases pointed out that these interacted with plasminogen similarly to how streptokinase and plasminogen interact in a fluid phase.
  • The research found that all three types of plasminogen (human, horse, and pig) were cleaved at the same highly conserved position from their interaction with the streptokinase.

Broader Implications

  • This study confirms the presence of streptokinases in nonhuman S. equisimilis isolates and reveals that these proteins belong to a group of plasminogen activators more diverse than previously thought.
  • This discovery has significant implications for understanding the physiological roles of streptokinases, their potential therapeutic uses, and the broader mechanisms of plasminogen activation and fibrinolysis in different species.

Cite This Article

APA
Caballero AR, Lottenberg R, Johnston KH. (1999). Cloning, expression, sequence analysis, and characterization of streptokinases secreted by porcine and equine isolates of Streptococcus equisimilis. Infect Immun, 67(12), 6478-6486. https://doi.org/10.1128/IAI.67.12.6478-6486.1999

Publication

Infection and immunity
ISSN: 0019-9567
NlmUniqueID: 0246127
Country: United States
Language: English
Volume: 67
Issue: 12
Pages: 6478-6486

Researcher Affiliations

Caballero, A R
  • Department of Microbiology, Immunology and Parasitology, Louisiana State University Medical Center, New Orleans, Louisiana 70112, USA.
Lottenberg, R
    Johnston, K H

      MeSH Terms

      • Amino Acid Sequence
      • Animals
      • Base Sequence
      • Cloning, Molecular
      • Horse Diseases / microbiology
      • Horses
      • Humans
      • Molecular Sequence Data
      • Plasminogen / isolation & purification
      • Plasminogen / metabolism
      • Plasminogen Activators / metabolism
      • Polymerase Chain Reaction
      • Sequence Analysis, DNA
      • Streptococcal Infections / microbiology
      • Streptococcal Infections / veterinary
      • Streptococcus / enzymology
      • Streptococcus / genetics
      • Streptokinase / chemistry
      • Streptokinase / genetics
      • Streptokinase / metabolism
      • Swine
      • Swine Diseases / microbiology

      Grant Funding

      • R01DK45014 / NIDDK NIH HHS

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      Citations

      This article has been cited 11 times.
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