Streptokinases produced by pathogenic group C streptococci demonstrate species-specific plasminogen activation.
Abstract: The species specificities of plasminogen activation and binding of plasmin by pathogenic group C streptococci isolated from humans, horses, and pigs were examined. Of 56 streptococcal isolates, 52 elaborated plasminogen activator activity and 49 of these had specificity for plasminogen of the homologous host. Analysis of supernatants from 13 isolates indicated that the plasminogen activator activity resulted from secreted streptokinases. These 13 streptokinases were antigenically related and bound all three plasminogens, indicating that the binding recognition sites were conserved despite the observed species-specific activation. In addition, all group C isolates tested demonstrated surface receptors that bound human, equine, and porcine plasmin. Species-specific plasminogen activation may be an early step in events resulting in infection and may account for the species preference of certain streptococci.
Publication Date: 1991-09-01 PubMed ID: 1869838DOI: 10.1093/infdis/164.3.515Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- Journal Article
- Research Support
- 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.
The research examines the activation and binding specificities of a protein called plasminogen by group C streptococci, a type of bacteria, in different species. The findings suggest that this process may be an initial step in the occurrence of infections and could explain why certain streptococci show preference for specific species.
Research Objectives and Methods
- The main goal of the research was to investigate how pathogenic group C streptococci, from humans, horses, and pigs interacted with plasminogen, a protein that plays a key role in blood clotting. Specific focus was on plasminogen activation and the binding of the protein plasmin.
- The study featured 56 isolates of streptococci, 52 of which displayed plasminogen activator activity, with 49 demonstrating specificity for homologous host plasminogen.
- The team also studied supernatants–the liquid phase of a sample after centrifugation–from 13 isolates to reveal the source of plasminogen activating activity.
Key Findings
- The study found that the plasminogen activating activity comes from secreted streptokinases, enzymes that convert plasminogen into plasmin. The 13 streptokinases identified were antigenically related, meaning they stimulated an immune response.
- These streptokinases bound all three kinds of plasminogen, suggesting that the recognition sites that bind them are conserved despite different species-specific activation.
- All group C isolates demonstrated receptors on their surfaces that could bind to human, equine, and porcine plasmin.
Potential Implications
- The observation of species-specific plasminogen activation suggests this might be an early step leading to infection. This could also explain why some streptococci display a preference for certain species, potentially opening avenues for new treatment strategies.
- Understanding pathogen behavior at a microscopic level can support the development of targeted pharmaceuticals and interventions.
Cite This Article
APA
McCoy HE, Broder CC, Lottenberg R.
(1991).
Streptokinases produced by pathogenic group C streptococci demonstrate species-specific plasminogen activation.
J Infect Dis, 164(3), 515-521.
https://doi.org/10.1093/infdis/164.3.515 Publication
Researcher Affiliations
- Department of Medicine, University of Florida, College of Medicine, Gainesville 32610-0277.
MeSH Terms
- Animals
- Horses
- Humans
- Plasminogen Activators
- Species Specificity
- Streptococcal Infections / microbiology
- Streptococcus / enzymology
- Streptokinase / biosynthesis
- Streptokinase / metabolism
- Swine
Grant Funding
- HL-41898 / NHLBI NIH HHS
Citations
This article has been cited 21 times.- Porcellato D, Smistad M, Skeie SB, Jørgensen HJ, Austbø L, Oppegaard O. Whole genome sequencing reveals possible host species adaptation of Streptococcus dysgalactiae.. Sci Rep 2021 Aug 30;11(1):17350.
- Ji HJ, Zhi Y, Lee JH, Ahn KB, Seo HS, Sullam PM. Inhibition of Fibrinolysis by Streptococcal Phage Lysin(SM1).. mBio 2021 Jun 29;12(3):e0074621.
- Bhardwaj S, Angayarkanni J. Streptokinase production from Streptococcus dysgalactiae subsp. equisimilis SK-6 in the presence of surfactants, growth factors and trace elements.. 3 Biotech 2015 Apr;5(2):187-193.
- Ko YP, Flick MJ. Fibrinogen Is at the Interface of Host Defense and Pathogen Virulence in Staphylococcus aureus Infection.. Semin Thromb Hemost 2016 Jun;42(4):408-21.
- Vieira ML, Atzingen MV, Oliveira R, Mendes RS, Domingos RF, Vasconcellos SA, Nascimento AL. Plasminogen binding proteins and plasmin generation on the surface of Leptospira spp.: the contribution to the bacteria-host interactions.. J Biomed Biotechnol 2012;2012:758513.
- Sun H, Xu Y, Sitkiewicz I, Ma Y, Wang X, Yestrepsky BD, Huang Y, Lapadatescu MC, Larsen MJ, Larsen SD, Musser JM, Ginsburg D. Inhibitor of streptokinase gene expression improves survival after group A streptococcus infection in mice.. Proc Natl Acad Sci U S A 2012 Feb 28;109(9):3469-74.
- Chung MC, Tonry JH, Narayanan A, Manes NP, Mackie RS, Gutting B, Mukherjee DV, Popova TG, Kashanchi F, Bailey CL, Popov SG. Bacillus anthracis interacts with plasmin(ogen) to evade C3b-dependent innate immunity.. PLoS One 2011 Mar 25;6(3):e18119.
- Fan HC, Hu CF, Juan CJ, Chen SJ. Current proceedings of childhood stroke.. Stroke Res Treat 2011 Feb 7;2011:432839.
- Vieira ML, Vasconcellos SA, Gonçales AP, de Morais ZM, Nascimento AL. Plasminogen acquisition and activation at the surface of leptospira species lead to fibronectin degradation.. Infect Immun 2009 Sep;77(9):4092-101.
- Sun H, Wang X, Degen JL, Ginsburg D. Reduced thrombin generation increases host susceptibility to group A streptococcal infection.. Blood 2009 Feb 5;113(6):1358-64.
- Mundodi V, Kucknoor AS, Alderete JF. Immunogenic and plasminogen-binding surface-associated alpha-enolase of Trichomonas vaginalis.. Infect Immun 2008 Feb;76(2):523-31.
- Kunamneni A, Abdelghani TT, Ellaiah P. Streptokinase--the drug of choice for thrombolytic therapy.. J Thromb Thrombolysis 2007 Feb;23(1):9-23.
- Friedrich R, Panizzi P, Kawabata S, Bode W, Bock PE, Fuentes-Prior P. Structural basis for reduced staphylocoagulase-mediated bovine prothrombin activation.. J Biol Chem 2006 Jan 13;281(2):1188-95.
- Ward PN, Field TR, Rapier CD, Leigh JA. The activation of bovine plasminogen by PauA is not required for virulence of Streptococcus uberis.. Infect Immun 2003 Dec;71(12):7193-6.
- Gladysheva IP, Turner RB, Sazonova IY, Liu L, Reed GL. Coevolutionary patterns in plasminogen activation.. Proc Natl Acad Sci U S A 2003 Aug 5;100(16):9168-72.
- Bower K, Djordjevic SP, Andronicos NM, Ranson M. Cell surface antigens of Mycoplasma species bovine group 7 bind to and activate plasminogen.. Infect Immun 2003 Aug;71(8):4823-7.
- Ward PN, Leigh JA. Characterization of PauB, a novel broad-spectrum plasminogen activator from Streptococcus uberis.. J Bacteriol 2002 Jan;184(1):119-25.
- Schroeder B, Boyle MD, Sheerin BR, Asbury AC, Lottenberg R. Species specificity of plasminogen activation and acquisition of surface-associated proteolytic activity by group C streptococci grown in plasma.. Infect Immun 1999 Dec;67(12):6487-95.
- Caballero AR, Lottenberg R, Johnston KH. Cloning, expression, sequence analysis, and characterization of streptokinases secreted by porcine and equine isolates of Streptococcus equisimilis.. Infect Immun 1999 Dec;67(12):6478-86.
- Johnsen LB, Poulsen K, Kilian M, Petersen TE. Purification and cloning of a streptokinase from Streptococcus uberis.. Infect Immun 1999 Mar;67(3):1072-8.
- Lottenberg R, Broder CC, Boyle MD, Kain SJ, Schroeder BL, Curtiss R 3rd. Cloning, sequence analysis, and expression in Escherichia coli of a streptococcal plasmin receptor.. J Bacteriol 1992 Aug;174(16):5204-10.
Use Nutrition Calculator
Check if your horse's diet meets their nutrition requirements with our easy-to-use tool Check your horse's diet with our easy-to-use tool
Talk to a Nutritionist
Discuss your horse's feeding plan with our experts over a free phone consultation Discuss your horse's diet over a phone consultation
Submit Diet Evaluation
Get a customized feeding plan for your horse formulated by our equine nutritionists Get a custom feeding plan formulated by our nutritionists
