The interaction of Streptococcus dysgalactiae with plasmin and plasminogen.
Abstract: The activation of plasminogen and the binding of plasmin by bacteria may have many effects which promote infection. The occurrence of such activities in streptococci is well documented; however, these are yet to be demonstrated for S. dysgalactiae. Consequently, the ability of this bacterium to activate mammalian plasminogen and bind either plasmin or its zymogen was investigated. Activation of bovine plasminogen was dependent on both the strain and the growth medium used for cultivation. Eighteen strain were able to activate bovine and ovine plasminogen and some of these also activated plasminogen from the horse, rabbit and pig. None activated human plasminogen and one strain (CE127) did not activate plasminogen from any source. Tricine-SDS PAGE and zymographic analysis of culture supernatants showed that bovine plasminogen was activated by four out of six strains at two locations corresponding to 16 kDa and 10 kDa. Following the growth of five strains in the presence of bovine plasminogen, all but strain CE127 bound high levels of plasmin activity. In contrast, following growth in human plasminogen none of the strains exhibited bound plasmin activity although all could bind human plasmin directly. All strains were also able to bind bovine and human plasminogen in such a way as to allow its activation by urokinase. We conclude that S. dysgalactiae is capable of activating mammalian plasminogen in a species-specific fashion and that the bacterium is also capable of binding plasmin and plasminogen with an apparent preference for bovine plasmin over human plasmin and/or plasminogen from either species.
Publication Date: 1998-07-01 PubMed ID: 9646471DOI: 10.1016/s0378-1135(98)00179-5Google Scholar: Lookup
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- Journal Article
Summary
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The research focuses on the interaction of Streptococcus dysgalactiae bacteria with plasmin and plasminogen, proteins related to the control of coagulation in the body, with findings suggesting that these bacteria can activate plasminogen and bind to both plasmin and plasminogen in a species-specific manner.
Introduction and Research Objectives
- The research paper starts by mentioning how the activation of plasminogen and the binding of plasmin by bacteria can promote infection. This becomes the motivation for the study, as such activities in streptococci (a type of bacteria) are well-documented but have not been confirmed for a particular strain: Streptococcus dysgalactiae.
- The main objectives of the research are to investigate if S. dysgalactiae can activate mammalian plasminogen and bind either plasmin or its zymogen (precursor).
Methodology
- The researchers investigated the activation of bovine plasminogen by S. dysgalactiae, keeping factors like the bacterial strain and growth medium constant.
- A total of eighteen strains were tested to activate bovine and ovine plasminogen. Out of these, some were able to activate plasminogen from horses, rabbits, and pigs. However, none activated human plasminogen, and one strain (CE127) did not activate plasminogen from any source.
- Several experiments involving Tricine-SDS PAGE and zymographic analysis, growth in the presence of bovine or human plasminogen, and binding tests with bovine and human plasminogen were performed to explore these interactions.
Results and Observations
- Out of the six tested strains of S. dysgalactiae, four were observed to activate bovine plasminogen. This was deduced from the Tricine-SDS PAGE and zymographic analysis.
- Upon growing five strains in the presence of bovine plasminogen, all except strain CE127 bound high levels of plasmin activity. Thus, showing that S. dysgalactiae can bind plasmin.
- In contrast, when the strains were grown with human plasminogen, none showed bound plasmin activity. However, they could bind human plasmin directly. This suggests that the binding ability of these bacteria is species-specific.
Conclusion
- The study concluded that S. dysgalactiae can activate mammalian plasminogen and bind both plasmin and plasminogen in a species-specific manner.
- However, these bacteria showed an apparent preference for bovine plasmin over human plasmin and/or plasminogen from either species. This finding could shed new light on the mechanisms of S. dysgalactiae infections, particularly in the context of their interaction with host proteins.
Cite This Article
APA
Leigh JA, Hodgkinson SM, Lincoln RA.
(1998).
The interaction of Streptococcus dysgalactiae with plasmin and plasminogen.
Vet Microbiol, 61(1-2), 121-135.
https://doi.org/10.1016/s0378-1135(98)00179-5 Publication
Researcher Affiliations
- Institute for Animal Health, Compton Laboratory, Newbury, Berkshire, UK. James.Leigh@BBSRC.AC.UK
MeSH Terms
- Animals
- Cattle
- Enzyme Activation
- Fibrinolysin / metabolism
- Horses
- Humans
- Mammals
- Plasminogen / metabolism
- Plasminogen Activators / isolation & purification
- Plasminogen Activators / metabolism
- Rabbits
- Sheep
- Species Specificity
- Streptococcus / physiology
- Swine
Citations
This article has been cited 9 times.- Babu V, Subathra Devi C. In vitro thrombolytic activity of purified streptokinase extracted from Streptococcus equinus VIT_VB2 isolated from bovine milk. J Thromb Thrombolysis 2015 Jan;39(1):71-8.
- Egan SA, Ward PN, Watson M, Field TR, Leigh JA. Vru (S뀔4) controls expression of proven and putative virulence determinants and alters the ability of Streptococcus uberis to cause disease in dairy cattle. Microbiology (Reading) 2012 Jun;158(Pt 6):1581-1592.
- Rato MG, Nerlich A, Bergmann R, Bexiga R, Nunes SF, Vilela CL, Santos-Sanches I, Chhatwal GS. Virulence gene pool detected in bovine group C Streptococcus dysgalactiae subsp. dysgalactiae isolates by use of a group A S. pyogenes virulence microarray. J Clin Microbiol 2011 Jul;49(7):2470-9.
- 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.
- 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.
- Vasi J, Frykberg L, Carlsson LE, Lindberg M, Guss B. M-like proteins of Streptococcus dysgalactiae. Infect Immun 2000 Jan;68(1):294-302.
- 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.
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