Identification of enolase as a laminin-binding protein on the surface of Staphylococcus aureus

Carneiro, César Alves

doi:10.1016/s1286-4579(04)00080-2

Cited by 35 publications

(41 citation statements)

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“…Enolase, a 46-kDa glycolytic enzyme, is highly conserved in prokaryotes and eukaryotes. Even though no signal peptide for secretion or localization to the outer membrane has yet been identified, enolases of bacteria and eukaryotic cells have been shown to be localized in the outer membrane (11,21,43,56,60). Indeed, the recruitment of plasminogen to cellular surfaces by enolase seems to be a conserved pattern in different cells, including bacteria, fungi, and eukaryotic cells (5,36,38,41,46).…”

Section: Discussionmentioning

confidence: 99%

Cytosolic Proteins Contribute to Surface Plasminogen Recruitment ofNeisseria meningitidis

et al. 2007

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Plasminogen recruitment is a common strategy of pathogenic bacteria and results in a broad-spectrum surface-associated protease activity. Neisseria meningitidis has previously been shown to bind plasminogen. In this study, we show by several complementary approaches that endolase, DnaK, and peroxiredoxin, which are usually intracellular proteins, can also be located in the outer membrane and act as plasminogen receptors. Internal binding motifs, rather than C-terminal lysine residues, are responsible for plasminogen binding of the N. meningitidis receptors. Recombinant receptor proteins inhibit plasminogen association with N. meningitidis in a concentration-dependent manner. Besides binding purified plasminogen, N. meningitidis can also acquire plasminogen from human serum. Activation of N. meningitidis-associated plasminogen by urokinase results in functional activity and allows the bacteria to degrade fibrinogen. Furthermore, plasmin bound to N. meningitidis is protected against inactivation by ␣ 2 -antiplasmin.

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Section: Discussionmentioning

confidence: 99%

Cytosolic Proteins Contribute to Surface Plasminogen Recruitment ofNeisseria meningitidis

et al. 2007

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“…Besides GAPDH, enolase is one of most frequent members of the class of surface-localized glycolytic enzymes, as described in phylogenetically different species such as Aeromonas hydrophila (Sha et al, 2009), Bacillus anthracis (Agarwal et al, 2008), Borrelia burgdorferi (Nogueira et al, 2012), Bifidobacterium sp. , C. albicans (Jong et al, 2003), Lactobacillus plantarum (Castaldo et al, 2009), Paracoccidioides brasiliensis (Donofrio et al, 2009), Staphylococcus aureus (Carneiro et al, 2004), S. pneumoniae (Bergmann et al, 2001) and Trichomonas vaginalis (Mundodi et al, 2008). In most cases, enolases interact with plasminogen but binding to fibronectin and laminin has also been reported (Carneiro et al, 2004;Castaldo et al, 2009;Donofrio et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

“…, C. albicans (Jong et al, 2003), Lactobacillus plantarum (Castaldo et al, 2009), Paracoccidioides brasiliensis (Donofrio et al, 2009), Staphylococcus aureus (Carneiro et al, 2004), S. pneumoniae (Bergmann et al, 2001) and Trichomonas vaginalis (Mundodi et al, 2008). In most cases, enolases interact with plasminogen but binding to fibronectin and laminin has also been reported (Carneiro et al, 2004;Castaldo et al, 2009;Donofrio et al, 2009). The M. pneumoniae enolase shows typical putative plasminogen-binding sites, such as lysine in the C terminus, 448 FKNIK 452 , and a lysine-rich internal motif, 268 KRYVFKKGIKAKILDEK 284 (Bergmann et al, 2003;Derbise et al, 2004;Yavlovich et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

Characterization of pyruvate dehydrogenase subunit B and enolase as plasminogen-binding proteins in Mycoplasma pneumoniae

2013

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The obligate pathogenic mycoplasma species Mycoplasma pneumoniae uses a limited but effective repertoire of virulence factors to infect and colonize the human respiratory tract. Besides the development of a unique adhesion complex and the expression of tissue-damaging factors, surface-located glycolytic enzymes and their capacity to bind to components of the human extracellular matrix (ECM) support pathogen-host interactions. Here, we demonstrated that the glycolytic enzymes enolase (Mpn606) and pyruvate dehydrogenase subunit B (Mpn392; PDHB) of M. pneumoniae show concentration-dependent binding to human plasminogen. Monospecific polyclonal antisera against both recombinant proteins reduced the binding to plasminogen significantly. The surface location of PDHB but not of enolase was demonstrated using Triton X fractionation of M. pneumoniae total protein content, membrane fractionation, colony blotting, mild proteolysis of mycoplasma cells, and immunofluorescence tests. To characterize the binding site of plasminogen in surface-displaced PDHB, the mycoplasmal protein was separated into four recombinant proteins followed by investigation of the binding behaviour of peptides that overlap the protein part interacting with plasminogen. Spot analysis resulted in a novel region of 12 amino acids (FPAMFQIFTHAA, position 91 to 102 of PDHB), which is responsible exclusively for binding of human plasminogen and also interacts in a dose-dependent manner with this host protein. The data indicate that the plasminogen-binding enzymes enolase and especially the surface-associated PDHB may contribute to the pathogenesis of M. pneumoniae infections.

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“…Motility, mediated by flagella, is required for H. pylori survival and colonization of the gastric niche (38,39), and FlaA and FlaB, the major flagellin subunits, were significantly upregulated under conditions of iron deficiency. Iron depletion was associated with increased expression of H. pylori enolase (Eno), which mediates adherence, invasion, and immune suppression for many bacterial pathogens, including Staphylococcus aureus (40), Bacillus anthracis (40), and Borrelia burgdorferi (41). Additional H. pylori survival factors upregulated by iron deficiency included urease, the heat shock protein GroEL, and glu-…”

Section: Figurementioning

confidence: 99%

Iron deficiency accelerates Helicobacter pylori–induced carcinogenesis in rodents and humans

Noto¹,

Gaddy²,

Lee³

et al. 2012

J. Clin. Invest.

157

243

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Gastric adenocarcinoma is strongly associated with Helicobacter pylori infection; however, most infected persons never develop this malignancy. H. pylori strains harboring the cag pathogenicity island (cag + ), which encodes CagA and a type IV secretion system (T4SS), induce more severe disease outcomes. H. pylori infection is also associated with iron deficiency, which similarly augments gastric cancer risk. To define the influence of iron deficiency on microbial virulence in gastric carcinogenesis, Mongolian gerbils were maintained on iron-depleted diets and infected with an oncogenic H. pylori cag + strain. Iron depletion accelerated the development of H. pylori-induced premalignant and malignant lesions in a cagA-dependent manner. H. pylori strains harvested from iron-depleted gerbils or grown under iron-limiting conditions exhibited enhanced virulence and induction of inflammatory factors. Further, in a human population at high risk for gastric cancer, H. pylori strains isolated from patients with the lowest ferritin levels induced more robust proinflammatory responses compared with strains isolated from patients with the highest ferritin levels, irrespective of histologic status. These data demonstrate that iron deficiency enhances H. pylori virulence and represents a measurable biomarker to identify populations of infected persons at high risk for gastric cancer.

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Identification of enolase as a laminin-binding protein on the surface of Staphylococcus aureus

Cited by 35 publications

References 0 publications

Cytosolic Proteins Contribute to Surface Plasminogen Recruitment ofNeisseria meningitidis

Cytosolic Proteins Contribute to Surface Plasminogen Recruitment ofNeisseria meningitidis

Characterization of pyruvate dehydrogenase subunit B and enolase as plasminogen-binding proteins in Mycoplasma pneumoniae

Iron deficiency accelerates Helicobacter pylori–induced carcinogenesis in rodents and humans

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