The interaction of Streptococcus dysgalactiae with plasmin and plasminogen

Leigh, James A.; Hodgkinson, S.M; Lincoln, Ruth A.

doi:10.1016/s0378-1135(98)00179-5

Cited by 27 publications

(25 citation statements)

References 27 publications

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“…Several types of gram-positive bacteria, including Staphylococcus aureus, streptococci groups A, C and G and S. dysgalactiae, can bind plasminogen [7][8][9][10]. Important gram-negative pathogens including Neisseria meningitidis, Haemophilus influenzae, Borrelia burgdorferi, Salmonella enterica and Helicobacter pylori also bind substantial amounts of plasminogen [11][12][13][14].…”

Section: Introductionmentioning

confidence: 99%

Purification of native α-enolase from Streptococcus pneumoniae that binds plasminogen and is immunogenic

Whiting

Evans

Patel

et al. 2002

Journal of Medical Microbiology

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Many pathogenic bacteria express plasminogen receptors on their surface, which may play a role in the dissemination of organisms by binding plasminogen that, when converted to plasmin, can digest extracellular matrix proteins. A 45-kDa protein was purified from Streptococcus pneumoniae and confirmed as an AE-enolase by its ability to catalyse the dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate and by Nterminal sequencing. The activity of AE-enolase was found in the cytoplasm and in whole cells. Activity was also demonstrated in cell wall fractions, which confirmed that AEenolase is a cytoplasmic antigen also expressed on the surface of S. pneumoniae. The plasminogen-binding activity of AE-enolase was examined by Western blot, which showed that purified AE-enolase was able to bind human plasminogen. Immunoblots of the purified 45-kDa AE-enolase with 22 sera from patients with pneumococcal disease showed binding in 15 cases, indicating that pneumococcal enolase is immunogenic.

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Section: Introductionmentioning

confidence: 99%

Purification of native α-enolase from Streptococcus pneumoniae that binds plasminogen and is immunogenic

Whiting

Evans

Patel

et al. 2002

Journal of Medical Microbiology

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“…dysgalactiae (GCS) is a pathogen frequently associated with clinical and subclinical bovine mastitis, a disease that causes major economic losses in the dairy industry (51,67). Virulence determinants have been identified for this pathogen, such as surface proteins which specifically interact with plasma or extracellular matrix proteins of the host, such as alpha-2-macroglobulin, plasminogen, albumin, fibrinogen, fibronectin, vitronectin, and collagen (30,35,46,64), and genes coding for proteins assumed to play a role in mastitis, such as the alpha-2-macroglobulin-, immunoglobulin G-, or immunoglobulin Abinding protein Mig (25,55); the alpha 2-macroglobulin-or immunoglobulin G-binding protein Mag (24); and a fibrinogen-binding M-like protein (65).…”

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confidence: 99%

Virulence Gene Pool Detected in Bovine Group C Streptococcus dysgalactiae subsp. dysgalactiae Isolates by Use of a Group A S. pyogenes Virulence Microarray

et al. 2011

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A custom-designed microarray containing 220 virulence genes of Streptococcus pyogenes (group A Streptococcus [GAS]) was used to test group C Streptococcus dysgalactiae subsp. dysgalactiae (GCS) field strains causing bovine mastitis and group C or group G Streptococcus dysgalactiae subsp. equisimilis (GCS/GGS) isolates from human infections, with the latter being used for comparative purposes, for the presence of virulence genes. All bovine and all human isolates carried a fraction of the 220 genes (23% and 39%, respectively). The virulence genes encoding streptolysin S, glyceraldehyde-3-phosphate dehydrogenase, the plasminogen-binding M-like protein PAM, and the collagen-like protein SclB were detected in the majority of both bovine and human isolates (94 to 100%). Virulence factors, usually carried by human beta-hemolytic streptococcal pathogens, such as streptokinase, laminin-binding protein, and the C5a peptidase precursor, were detected in all human isolates but not in bovine isolates. Additionally, GAS bacteriophage-associated virulence genes encoding superantigens, DNase, and/or streptodornase were detected in bovine isolates (72%) but not in the human isolates. Determinants located in non-bacteriophage-related mobile elements, such as the gene encoding R28, were detected in all bovine and human isolates. Several virulence genes, including genes of bacteriophage origin, were shown to be expressed by reverse transcriptase PCR (RT-PCR). Phylogenetic analysis of superantigen gene sequences revealed a high level (>98%) of identity among genes of bovine GCS, of the horse pathogen Streptococcus equi subsp. equi, and of the human pathogen GAS. Our findings indicate that alphahemolytic bovine GCS, an important mastitis pathogen and considered to be a nonhuman pathogen, carries important virulence factors responsible for virulence and pathogenesis in humans.

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“…Correspondingly, a number of novel streptococcal plasminogen activators distinct from classical SK have been identified over this period. These include ESK and PSK, identified from equine and porcine isolates of S. equisimilis (6,27), PadA, identified in S. dysgalactiae (20), and PauA, the well-characterized plasminogen activator of S. uberis (14,18,31,33). Intriguingly, each of these plasminogen activators exhibits activity towards mammalian plasminogen in a species-specific manner.…”

Section: Discussionmentioning

confidence: 99%

“…A 32-kDa plasminogen activator isolated from S. uberis, PauA, displayed a preference for bovine, ovine, and equine plasminogen but was unable to activate porcine or human plasminogen (18). Similarly, a further unrelated 16-kDa plasminogen activator (designated PadA for plasminogen activator dysgalactiae A) was identified in bovine isolates of Streptococcus dysgalactiae which could activate bovine, ovine, equine, and rabbit but not human plasminogens (20). In the course of cloning pauA, which encodes the 32-kDa plasminogen activator from S. uberis, a single isolate (SK880) from a panel of 11 strains tested was reported to display plasminogen-dependent fibrinolysis due to a plasminogen activator of ϳ45 kDa (14).…”

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Characterization of PauB, a Novel Broad-Spectrum Plasminogen Activator from Streptococcus uberis

Ward¹,

Leigh²

2002

J Bacteriol

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A bovine plasminogen activator of atypical molecular mass (ϳ45 kDa) from Streptococcus uberis strain SK880 had been identified previously (L. B. Johnsen, K. Poulsen, M. Kilian, and T. E. Petersen. Infect. Immun. 67:1072-1078, 1999). The strain was isolated from a clinical case of bovine mastitis. The isolate was found not to secrete PauA, a bovine plasminogen activator expressed by the majority of S. uberis strains. Analysis of the locus normally occupied by pauA revealed an absence of the pauA open reading frame. However, an alternative open reading frame was identified within the same locus. Sequence analysis of the putative gene suggested limited but significant homology to other plasminogen activators. A candidate signal peptide sequence and cleavage site were also identified. Expression cloning of DNA encoding the predicted mature protein (lacking signal peptide) confirmed that the open reading frame encoded a plasminogen activator of the expected size, which we have named PauB. Both native and recombinant forms of PauB displayed an unexpectedly broad specificity profile for bovine, ovine, equine, caprine, porcine, rabbit, and human plasminogen. Clinical and nonclinical field isolates from nine United Kingdom sites were screened for the pauB gene and none were identified as carrying it. Similarly, clinical isolates from 20 Danish herds were all found to encode PauA and not PauB. Therefore, PauB represents a novel but rare bacterial plasminogen activator which displays very broad specificity.Mammalian plasminogen activator and plasmin systems play a key role in numerous biological processes including fibrinolysis, degradation of extracellular matrix proteins, cellular migration, and cancer metastasis. Conversion of the plasma zymogen plasminogen to the serine protease plasmin represents the end point of a cascade of reactions culminating in fibrinolytic dissolution of blood clots (3). Plasmin also plays a role in tissue remodeling through its ability to hydrolyze extracellular matrix proteins (34) and can also initiate activation of further metalloproteinases (11). By commandeering elements of this system, a wide range of bacteria are able to bind plasmin(ogen) and thereby augment their pathogenesis over less able competitors (23). A smaller subset of bacterial species that are able to bind plasmin(ogen) also produce potent plasminogen activators. Staphylokinase (SAK), a 15.5-kDa protein secreted by Staphylococcus aureus, forms a complex in association with either fibrin-bound human plasmin or free plasmin in preference to plasminogen (reviewed recently in reference 9). The SAK-plasmin complex can in turn activate other plasminogen molecules to plasmin. Streptokinase (SK), a 47-kDa protein, was the first streptococcal plasminogen activator described for which a mechanism of action was determined (24). In contrast to SAK, SK can associate with either human plasminogen or plasmin to form an activator complex which can then interact with further plasminogen molecules to generate plasmin (29).Once activated, pla...

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The interaction of Streptococcus dysgalactiae with plasmin and plasminogen

Cited by 27 publications

References 27 publications

Purification of native α-enolase from Streptococcus pneumoniae that binds plasminogen and is immunogenic

Purification of native α-enolase from Streptococcus pneumoniae that binds plasminogen and is immunogenic

Virulence Gene Pool Detected in Bovine Group C Streptococcus dysgalactiae subsp. dysgalactiae Isolates by Use of a Group A S. pyogenes Virulence Microarray

Characterization of PauB, a Novel Broad-Spectrum Plasminogen Activator from Streptococcus uberis

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