Purification and characterization of a 52-kilodalton immunoglobulin G-binding protein from Streptococcus suis capsular type 2

Serhir, Bouchra; Dubreuil, Daniel; Higgins, Robert; Jacques, Mario

doi:10.1128/jb.177.13.3830-3836.1995

Cited by 21 publications

(24 citation statements)

References 47 publications

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“…The receptor was also resistant to heating (Fig. 1), as are the S. suis immunoglobulin G and fibronectin receptors previously reported (7,23). 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).…”

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confidence: 56%

“…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.…”

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confidence: 99%

“…1). Several plasma proteins were tested for their ability to reduce plasminogen binding, since previous studies reported that S. suis binds immunoglobulin G, fibronectin, and albumin (7,21,23). No plasma proteins significantly interfered with plasminogen binding, suggesting that there is a specific plasminogen receptor.…”

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confidence: 99%

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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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Acquisition of Host Plasmin Activity by the Swine PathogenStreptococcus suisSerotype 2

Jobin

Brassard²,

Quessy

et al. 2004

Infect Immun

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“…Surface proteins encoding IgA-binding receptors have been reported in S. pneumoniae, and streptococcal strains of groups A and B, but these proteins specifically bind only H-IgA (Bessen, 1994 ;Cleat & Timmis, 1987 ;Fagan et al, 2001 ;Hammerschmidt et al, 1997 ;Hede! n et al, 1991 ;Johnsson et al, 1994 ;Russell-Jones et al, 1984 ;Serhir et al, 1995 ;Stenberg et al, 1994). Since IgA-binding receptors might play a role in bacterial pathogenesis, we were interested in examining the existence of B-IgAbinding receptors in S. dysgalactiae, an environmental pathogen that can infect and cause subsequent inflammation of the bovine mammary gland.…”

Section: Discussionmentioning

confidence: 99%

“…Although all of them show specific binding activities to H-IgA, the group A streptococcal receptors bind both serum and secretory IgA (sIgA), whereas the group B streptococcal receptor binds mainly serum IgA . Other H-IgA-binding receptors were also reported in Streptococcus pneumoniae, including a 52 kDa protein (Serhir et al, 1995) and a 59 kDa protein SpsA that specifically binds H-IgA secretory component (Hammerschmidt et al, 1997). One of the possible roles of the IgA-binding proteins appears to be protection against phagocytosis, since binding of H-IgA to receptors in Streptococcus pyogenes has been found to interfere with bacterial adhesion to the host cells (Fluckiger et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Bovine immunoglobulin A (IgA)-binding activities of the surface-expressed Mig protein of Streptococcus dysgalactiae

Song¹,

Perez-Casal²,

Fontaine³

et al. 2002

Microbiology

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Pros and Cons of Obtaining Antibodies from Chickens’ Eggs Rather than from Mammals’ Serum

Schade

Schwarzkopf²,

Erhard

2001

Chicken Egg Yolk Antibodies, Production and Application

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Purification and characterization of a 52-kilodalton immunoglobulin G-binding protein from Streptococcus suis capsular type 2

Cited by 21 publications

References 47 publications

Acquisition of Host Plasmin Activity by the Swine PathogenStreptococcus suisSerotype 2

Acquisition of Host Plasmin Activity by the Swine PathogenStreptococcus suisSerotype 2

Bovine immunoglobulin A (IgA)-binding activities of the surface-expressed Mig protein of Streptococcus dysgalactiae

Pros and Cons of Obtaining Antibodies from Chickens’ Eggs Rather than from Mammals’ Serum

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