Surface bound plasmin promotes migration ofStreptococcus pneumoniaethrough reconstituted basement membranes

Eberhard, Thomas; Kronvall, Göran; Ullberg, Måns

doi:10.1006/mpat.1998.0262

Cited by 66 publications

(54 citation statements)

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“…The ability of AE-enolase to bind plasminogen demonstrated here supports the idea that this antigen may be responsible in part for the plasminogen activity that has already been demonstrated on the surface of S. pneumoniae [4]. It also means that AE-enolase may be responsible, in part, for the ability of S. pneumoniae to cross tissue barriers [4].…”

Section: Discussionsupporting

confidence: 86%

“…An adhesin CbpA promotes increased attachment to activated human cells [29]. Recent studies showed that pneumococci could bind to reconstituted basement membrane as well as to a purified laminin component [4]. Furthermore, they can bind other extracellular matrix components such as fibronectin, laminin, collagen and vitronectin [30,31].…”

Section: Discussionmentioning

confidence: 99%

“…The pneumococcal AE-enolase is a plasminogen-binding protein similar to the enolase that has been described on the surface of S. pyogenes [6,21] and surface plasminogen activation has been described in S. pneumoniae [4]. The plasminogen system plays an important role in host defence by dissolving fibrin clots and maintaining homeostasis and vascular patency.…”

Section: Discussionmentioning

confidence: 99%

“…It also means that AE-enolase may be responsible, in part, for the ability of S. pneumoniae to cross tissue barriers [4].…”

Section: Discussionmentioning

confidence: 99%

“…Pneumococci have been shown to adhere to and subsequently migrate across the reconstituted basement membrane of an invitro model system. Migration is thought to be mediated by plasminogen, which can be converted to plasmin, a serine protease, by the action of host urokinase or tissue plasminogen activator (t-PA) [4,5]. Surface-bound plasmin acquires proteolytic activity, which facilitates the migration of pneumococci through reconstituted basement membranes [4].…”

Section: Introductionmentioning

confidence: 99%

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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: Discussionsupporting

confidence: 86%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

“…It also means that AE-enolase may be responsible, in part, for the ability of S. pneumoniae to cross tissue barriers [4].…”

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

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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Triosephosphate isomerase of Streptococcus pneumoniae is released extracellularly by autolysis and binds to host plasminogen to promote its activation

et al. 2022

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Recruitment of plasminogen is an important infection strategy of the human pathogen Streptococcus pneumoniae to invade host tissues. In Streptococcus aureus, triosephosphate isomerase (TPI) has been reported to bind plasminogen. In this study, the TPI of S. pneumoniae (TpiA) was identified through proteomic analysis of bronchoalveolar lavage fluid from a murine pneumococcal pneumonia model. The binding kinetics of recombinant pneumococcal TpiA with plasminogen were characterized using surface plasmon resonance (SPR, Biacore), ligand blot analyses, and enzyme‐linked immunosorbent assay. Enhanced plasminogen activation and subsequent degradation by plasmin were also shown. Release of TpiA into the culture medium was observed to be dependent on autolysin. These findings suggest that S. pneumoniae releases TpiA via autolysis, which then binds to plasminogen and promotes its activation, thereby contributing to tissue invasion via degradation of the extracellular matrix.

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The cell wall subproteome of Listeria monocytogenes

et al. 2004

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The surface subproteome of Listeria monocytogenes that includes many proteins already known to be involved in virulence and interaction with host cells has been characterized. A new method for the isolation of a defined surface proteome of low complexity has been established based on serial extraction of proteins by different salts at high concentration, and in all 55 proteins were identified by N-terminal sequencing and mass spectrometry. About 16% of these proteins are of unknown function and three proteins have no orthologue in the nonpathogenic L. innocua and might be involved in virulence mechanisms. Remarkably, a relatively high number of proteins with a function in the cytoplasmic compartment was identified in this surface proteome. These proteins had neither predicted or detectable signal peptides nor could any modification be observed except removal of the N-terminal methionine. Enolase (Lmo2455) is one of these proteins. It was shown to be present in the cell wall of the pathogen by immunoelectron microscopy and, along with heat shock factor DnaK (Lmo1473), elongation factor TU (Lmo2653), and glyceraldehyde-3-phosphate dehydrogenase (Lmo2459), it was found to be able to bind human plasminogen in overlay blots and surface plasmon resonance (SPR) experiments. The KD values of these interactions were determined by SPR measurements. The data indicate a possible role of these proteins as receptors for human plasminogen on the bacterial cell surface. The potential role of this recruitment of a host protease for extracellular invasion mechanisms is discussed.

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Surface bound plasmin promotes migration ofStreptococcus pneumoniaethrough reconstituted basement membranes

Cited by 66 publications

References 0 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

Triosephosphate isomerase of Streptococcus pneumoniae is released extracellularly by autolysis and binds to host plasminogen to promote its activation

The cell wall subproteome of Listeria monocytogenes

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