Enhanced activation of bound plasminogen on <i>Staphylococcus aureus</i> by staphylokinase

Mölkänen, Tomi; Tyynelä, Jaana; Helin, Jari; Kalkkinen, Nisse; Kuusela, Pentti

doi:10.1016/s0014-5793(02)02580-2

Cited by 77 publications

(65 citation statements)

References 31 publications

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“…Enolase has also been identified as a novel plasminogen receptor on the surface of many eukaryotic cells (Miles et al, 1991; Nakajima et al, 1994). This unexpected feature has also been described in several bacteria (such as Staphylococcus aureus and many streptococci), fungi and nematodes (Bergmann et al, 2001;Jolodar et al, 2003;Jong et al, 2003;Molkanen et al, 2002;Pancholi & Fischetti, 1998;Sharma et al, 2006). While the role of plasminogen as an important component in streptoccoci adhesion is well established (Pancholi et al, 2003), the role of enolase in bacterial adherence and host cell invasion has not, to our knowledge, been investigated previously.…”

Section: Introductionmentioning

confidence: 69%

Isolation and characterization of α-enolase, a novel fibronectin-binding protein from Streptococcus suis

et al. 2008

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Streptococcus suis is an important swine pathogen that causes meningitis, endocarditis, arthritis and septicaemia. As a zoonotic agent, S. suis also causes similar diseases in humans. Binding of pathogenic bacteria to extracellular matrix components enhances their adhesion to and invasion of host cells. In the present study we isolated and identified a novel fibronectin-binding protein from S. suis. The native protein (designated SsEno) possessed not only high homology with other bacterial enolases but also enolase activity. We cloned, expressed and purified SsEno and showed that it is ubiquitously expressed by all S. suis serotypes and we identified its surface localization using immunoelectron microscopy. ELISA demonstrated that SsEno binds specifically to fibronectin and plasminogen in a lysine-dependent manner. Additional surface plasmon resonance assays demonstrated that SsEno binds to fibronectin or plasminogen with low nanomolar affinity. Inhibition experiments with anti-SsEno antibodies also showed that bacterial SsEno is important for the adhesion to and invasion of brain microvascular endothelial cells by S. suis. Overall, the present work is the first study, to our knowledge, to demonstrate a fibronectinbinding activity of a bacterial enolase, and shows that, similar to other bacterial fibronectin-binding proteins, SsEno may contribute to the virulence of S. suis. INTRODUCTIONStreptococcus suis is a major swine pathogen that causes septicaemia, meningitis, endocarditis and arthritis (Higgins & Gottschalk, 2005). Of the 35 known serotypes, serotype 2 is the most frequently isolated and associated with disease (Higgins & Gottschalk, 2005). It has been proposed that two serotypes (serotypes 32 and 34) be excluded from S. suis and redesignated Streptococcus orisratti (Hill et al., 2005). S. suis, especially serotype 2, has also been described as an important zoonotic agent that affects people in close contact with infected pigs or pork-derived products (Lun et al., 2007). Indeed, an important number of cases of human disease with a high rate of mortality in China were linked directly to a concurrent outbreak of S. suis infection in pigs (Ye et al., 2006).Little is known about S. suis virulence factors. The capsule polysaccharide (CPS) is a critical virulence factor, given that unencapsulated isogenic mutants are completely avirulent and rapidly cleared from the circulation in pig and mouse infection models (Charland et al., 2000;Smith et al., 1999). However, non-virulent strains are also encapsulated, indicating that the virulence of this pathogen is a multifactorial process . Other potential virulence factors have also been described in S. suis, including a haemolysin (suilysin), a 136 kDa muramidase-released protein (MRP), a 110 kDa extracellular factor (EF) protein, a hyaluronidase, a superoxide dismutase, various proteases, a serum opacity factor and different adhesins (Baums et al., 2006;.The pathogenesis of S. suis infection is not fully understood and likely involves many steps . Binding between b...

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Section: Introductionmentioning

confidence: 69%

Isolation and characterization of α-enolase, a novel fibronectin-binding protein from Streptococcus suis

et al. 2008

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“…EbpS is implicated in interactions between S. aureus and elastin, one of the major protein components of the extracellular matrix (31,32). Finally, Sak, the staphylokinase, may have an important physiological function in helping cells to disseminate in host tissue by activating plasminogen (28). A comparison of candidates for YycG/YycF regulation in B. subtilis and S. aureus reveals several similarities.…”

Section: See Materials and Methods) His-tagged Yycf Andmentioning

confidence: 99%

Identification of Genes Controlled by the Essential YycG/YycF Two-Component System ofStaphylococcus aureus

2004

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“…It has also been shown that activation of plasminogen to plasmin by staphylokinase is not only protected from the inhibitor, ␣ 2 -antiplasmin, but the activation is enhanced in the presence of S. aureus cells and solubilized staphylococcal cell walls (45). It was shown that these putative plasminogen-binding proteins were IMP dehydrogenase, ␣-enolase, and ribonucleotide reductase subunit 2 (45).…”

Section: Vol 190 2008 Extracellular Protein Profile Of S Aureus Uamentioning

confidence: 99%

“…It was shown that these putative plasminogen-binding proteins were IMP dehydrogenase, ␣-enolase, and ribonucleotide reductase subunit 2 (45). ␣-Enolase has also been shown to bind laminin on the surface of S. aureus (7).…”

Section: Vol 190 2008 Extracellular Protein Profile Of S Aureus Uamentioning

confidence: 99%

Relative Quantitative Comparisons of the Extracellular Protein Profiles ofStaphylococcus aureusUAMS-1 and ItssarA,agr, andsarA agrRegulatory Mutants Using One-Dimensional Polyacrylamide Gel Electrophoresis and Nanocapillary Liquid Chromatography Coupled with Tandem Mass Spectrometry

et al. 2008

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One-dimensional polyacrylamide gel electrophoresis followed by nanocapillary liquid chromatography coupled with mass spectrometry was used to analyze proteins isolated from Staphylococcus aureus UAMS-1 after 3, 6, 12, and 24 h of in vitro growth. Protein abundance was determined using a quantitative value termed normalized peptide number, and overall, proteins known to be associated with the cell wall were more abundant early on in growth, while proteins known to be secreted into the surrounding milieu were more abundant late in growth. In addition, proteins from spent media and cell lysates of strain UAMS-1 and its isogenic sarA, agr, and sarA agr regulatory mutant strains during exponential growth were identified, and their relative abundances were compared. Extracellular proteins known to be regulated by the global regulators sarA and agr displayed protein levels in accordance with what is known regarding the effects of these regulators.

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Enhanced activation of bound plasminogen on Staphylococcus aureus by staphylokinase

Cited by 77 publications

References 31 publications

Isolation and characterization of α-enolase, a novel fibronectin-binding protein from Streptococcus suis

Isolation and characterization of α-enolase, a novel fibronectin-binding protein from Streptococcus suis

Identification of Genes Controlled by the Essential YycG/YycF Two-Component System ofStaphylococcus aureus

Relative Quantitative Comparisons of the Extracellular Protein Profiles ofStaphylococcus aureusUAMS-1 and ItssarA,agr, andsarA agrRegulatory Mutants Using One-Dimensional Polyacrylamide Gel Electrophoresis and Nanocapillary Liquid Chromatography Coupled with Tandem Mass Spectrometry

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