Characterization of the interaction of bovine plasmin with Streptococcus uberis

Lincoln, Matthew R.; Leigh,

doi:10.1046/j.1365-2672.1998.00452.x

Cited by 10 publications

(12 citation statements)

References 15 publications

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“…4 are likely to represent plasminogen binding proteins of mycoplasmal origin. Many studies conducted on streptococcal pathogens have shown that there are variations in plasminogen binding capacity between species and strains of species (10,11,12,13,18). A direct comparison between plasminogen binding to the four different strains of mycoplasmas further supported this observation, as the different species displayed variations in plasminogen binding capacity.…”

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confidence: 55%

Cell Surface Antigens of Mycoplasma Species Bovine Group 7 Bind to and Activate Plasminogen

et al. 2003

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confidence: 55%

Cell Surface Antigens of Mycoplasma Species Bovine Group 7 Bind to and Activate Plasminogen

et al. 2003

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“…The interaction of plasminogen with S. suis S735 was not affected at the pHs (5 to 10) or salt concentrations (0 to 0.225 M) tested (data not shown). The plasminogen-binding capabilities of Borrelia burgdorferi (13), Streptococcus uberis (16), Mycoplasma fermentans (27), and Fusobacterium nucleatum (5) are also inhibited by EACA, but not EDTA. There is thus a strong similarity between the receptors of these pathogens and that of S. suis.…”

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confidence: 99%

Acquisition of Host Plasmin Activity by the Swine PathogenStreptococcus suisSerotype 2

Jobin

Brassard²,

Quessy

et al. 2004

Infect Immun

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In this study, the plasminogen-binding activity of Streptococcus suis serotype 2 was investigated. Bound human plasminogen was activated by purified streptokinase, urokinase, or Streptococcus dysgalactiae subsp. equisimilis culture supernatant. Both human and porcine plasminogen were bound by S. suis. Binding was inhibited by -aminocaproic acid, and the plasminogen receptor was heat and sodium dodecyl sulfate resistant. One of the receptors was identified as glyceraldehyde-3-phosphate dehydrogenase. S. suis-associated plasmin activity was capable of activating free plasminogen, which in turn could contribute to degradation of fibronectin. This is the first report on the plasminogen-binding activity of S. suis. Further studies may reveal a contribution of this activity to the virulence of S. suis.Streptococcus suis, an important swine pathogen worldwide, is made up of 35 serotypes (1 to 34 and 1/2) (12). Although all serotypes can cause infections, serotype 2 is the most prevalent one isolated from diseased pigs (9, 11). Septicemia, arthritis, meningitis, and sudden death are the most important clinical signs associated with S. suis infections (11). Cases of meningitis and endocarditis caused by S. suis have also been reported in workers associated with the pig industry (11). Although several S. suis virulence factors have been identified and characterized, the exact mechanisms by which this bacterium invades the host and causes infections are still unclear. The only factor considered essential for the pathogenicity of S. suis is the polysaccharide capsule (3). An important feature, which could play an important role in the pathogenicity of S. suis, is its ability to bind host proteins, which may camouflage it and thus protect it from the host immune system. Fibronectin (7), albumin (21), and immunoglobulin G (1, 23) receptors have been identified on the cell surface of S. suis and have been proposed as virulence factors.Plasminogen is a 92-kDa protein that is an important component of the fibrinolytic system. Its activation into plasmin, a serine protease, is tightly regulated by the equilibrium between plasmin activators (urokinase plasmin activator [u-PA] as well as tissue plasminogen activator) and inhibitors (␣2-antiplasmin and ␣2-macroglobulin) (15). Plasminogen can also be activated by microbial products including streptokinase and staphylokinase produced by group A streptococci and Staphylococcus aureus, respectively (15). Many group A and C streptococci bind plasminogen on their cell surfaces (15). In a number of cases, the receptors have been characterized and identified as glyceraldehyde-3-phosphate dehydrogenase (GAPDH) or ␣-enolase (17,19,20,24). The plasmin activity generated on the bacterial cell surface is protected from host inhibitors and can activate latent u-PA and tissue plasminogen activator, which subsequently activate plasminogen (15). This mechanism of acquisition of a host proteinase activity increases the invasive potential of some pathogens, including Streptococcus pneumoniae (8). The ...

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“…It has been hypothesized that activation of plasminogen to plasmin and acquisition of plasmin at the bacterial surface (33) may facilitate growth of this auxotrophic bacterium (42) in milk due to the release of peptides and amino acids from host proteins (30,50). In support of this hypothesis, it has been shown that S. uberis can utilize plasmin-derived peptides from casein as a source of essential amino acids (42) and that immunization, which is capable of inducing a neutral-izing response to PauA, can reduce colonization of a lactating gland by S. uberis following experimental challenge (32).…”

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confidence: 99%

MtuA, a Lipoprotein Receptor Antigen from Streptococcus uberis , Is Responsible for Acquisition of Manganese during Growth in Milk and Is Essential for Infection of the Lactating Bovine Mammary Gland

Smith¹,

Ward²,

Field³

et al. 2003

Infect Immun

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A mutant strain of Streptococcus uberis (AJS001) that was unable to grow in bovine milk was isolated following random insertional mutagenesis. The level of growth in milk was restored to that of the parental strain (strain 0140J) following addition of MnSO 4 but not following addition of other metal ions. The mutant contained a single insertion within mtuA, a homologue of mtsA and psaA, which encode metal-binding proteins in Streptococcus pyogenes and Streptococcus pneumoniae, respectively. Strain AJS001 was unable to infect any of eight quarters on four dairy cows following intramammary challenge with 10 5 CFU. Bacteria were never recovered directly from milk of these animals but were detected following enrichment in Todd-Hewitt broth in three of eight milk samples obtained within 24 h of challenge. The animals showed no inflammatory response and no signs of mastitis. Three mammary quarters on two different animals simultaneously challenged with 600 CFU of the parental strain, strain 0140J, became colonized, shed high numbers of S. uberis organisms in milk, displayed a marked inflammatory response to infection, and showed overt signs of mastitis. These data indicate that mtuA was required for efficient uptake of Mn 2؉ during growth in bovine milk and infection of the lactating bovine mammary gland.

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Characterization of the interaction of bovine plasmin with Streptococcus uberis

Cited by 10 publications

References 15 publications

Cell Surface Antigens of Mycoplasma Species Bovine Group 7 Bind to and Activate Plasminogen

Cell Surface Antigens of Mycoplasma Species Bovine Group 7 Bind to and Activate Plasminogen

Acquisition of Host Plasmin Activity by the Swine PathogenStreptococcus suisSerotype 2

MtuA, a Lipoprotein Receptor Antigen from Streptococcus uberis , Is Responsible for Acquisition of Manganese during Growth in Milk and Is Essential for Infection of the Lactating Bovine Mammary Gland

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