Analysis of Expression of a Cytosolic Enzyme on the Surface of Streptococcus pyogenes

D’Costa, Sybil; Romer, Terence G; Boyle, Michael D. P.

doi:10.1006/bbrc.2000.3884

Cited by 32 publications

(15 citation statements)

References 35 publications

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“…Some of the proteins identified were reported previously to be associated with the cell surface of Streptococcus agalactiae, among them phosphoglycerate kinase, glucose 6 phosphate isomerase and glyceraldehyde-3-phosphate dehydrogenase [38]. Recently, similar observations were published regarding S. pyogenes [39].…”

Section: Discussionsupporting

confidence: 53%

Glycolytic enzymes associated with the cell surface of Streptococcus pneumoniae are antigenic in humans and elicit protective immune responses in the mouse

Ling

Feldman

Portnoi

et al. 2004

Clinical and Experimental Immunology

181

156

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SUMMARYStreptococcus pneumoniae is a leading cause of otitis media, sinusitis, pneumonia, bacteraemia and meningitis worldwide. The drawbacks associated with the limited number of various capsular polysaccharides that can be included in the polysaccharide-based vaccines focuses much attention on pneumococcal proteins as vaccine candidates. We extracted an enriched cell wall fraction from S. pneumoniae WU2. Approximately 150 soluble proteins could be identified by 2D gel electrophoresis. The proteins were screened by 2D-Western blotting using sera that were obtained longitudinally from children attending day-care centres at 18, 30 and 42 months of age and sera from healthy adult volunteers. The proteins were further identified using matrix-assisted laser desorption ionization-time of flight mass spectrometry. Seventeen proteins were antigenic in children and adults, of which 13 showed an increasing antibody response with age in all eight children analysed. Two immunogenic proteins, fructose-bisphosphate aldolase (FBA) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and a control protein with known low immunogenicity, heat shock protein 70 (DnaK), were expressed in Escherichia coli , purified and used to immunize mice. Mouse antibodies elicited to the recombinant (r) FBA and rGAPDH were cross-reactive with several genetically unrelated strains of different serotypes and conferred protection to respiratory challenge with virulent pneumococci. In addition, the FBA used in this study (NP_345117) does not have a human ortholog and warrants further investigation as a candidate for a pneumococcal vaccine. In conclusion, the immunoproteomics based approach utilized in the present study appears to be a suitable tool for identification of novel S. pneumoniae vaccine candidates.

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Section: Discussionsupporting

confidence: 53%

Glycolytic enzymes associated with the cell surface of Streptococcus pneumoniae are antigenic in humans and elicit protective immune responses in the mouse

Ling

Feldman

Portnoi

et al. 2004

Clinical and Experimental Immunology

181

156

View full text Add to dashboard Cite

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“…association may allow Plr to indirectly acquire plasmin generated by the M-protein-fibrinogen-mediated fibrinolytic complex (13,14). In the present study, we have shown for the first time that SEN, a ubiquitously found surface protein of GAS, binds to both Lys-and Glu-plasminogen.…”

Section: Vol 72 2004 Sen-mediated Plasmin(ogen) Binding Of Gas 103mentioning

confidence: 49%

Role of the C-Terminal Lysine Residues of Streptococcal Surface Enolase in Glu- and Lys-Plasminogen-Binding Activities of Group A Streptococci

et al. 2004

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Streptococcal surface enolase (SEN) is a major plasminogen-binding protein of group A streptococci. Our earlier biochemical studies have suggested that the region responsible for this property is likely located at the C-terminal end of the SEN molecule. In the present study, the gene encoding SEN was cloned from group A streptococci M6 isolate D471. A series of mutations in the sen gene corresponding to the C-terminal region ( 428 KSFYNLKK 435 ) of the SEN molecule were created by either deleting one or more terminal lysine residues or replacing them with leucine. All purified recombinant SEN proteins with altered C-terminal ends were found to be enzymatically active and were analyzed for their Glu-and Lys-plasminogen-binding activities. Wild-type SEN bound to Lys-plasminogen with almost three times more affinity than to Glu-plasminogen. However, the recombinant mutant SEN proteins with a deletion of Lys434-435 or with K435L and K434-435L replacements showed a significant decrease in Glu-and Lys-plasminogen-binding activities. Accordingly, a streptococcal mutant expressing SEN-K434-435L showed a significant decrease in Glu-and Lys-plasminogen-binding activities. Biochemical and functional analyses of the isogenic mutant strain revealed a significant decrease in its abilities to cleave a chromogenic tripeptide substrate, acquire plasminogen from human plasma, and penetrate the extracellular matrix. Together, these data indicate that the last two C-terminal lysine residues of surfaceexposed SEN contribute significantly to the plasminogen-binding activity of intact group A streptococci and hence to their ability to exploit host properties to their own advantage in tissue invasion.

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“…The modifications provoked by respiration growth therefore suggest a new role for GapB in L. lactis physiology other than in glycolysis. In this regard, GAPDH has recently been implicated as having a secondary role on the cell surface in bacterial adhesion (1,10). Moreover, several isoforms of this enzyme were already reported in other Streptococcaceae related to L. lactis, e.g., Streptococcus pneumoniae (8), Enterococcus faecalis (A. Hartke, personal communication), and Streptococcus pyogenes (38).…”

Section: Discussionmentioning

confidence: 93%

Proteome Analyses of Heme-Dependent Respiration inLactococcus lactis: Involvement of the Proteolytic System

Vido

Bars²,

Mistou³

et al. 2004

J Bacteriol

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Sugar fermentation was long considered the sole means of energy metabolism available to lactic acid bacteria. We recently showed that metabolism of Lactococcus lactis shifts progressively from fermentation to respiration during growth when oxygen and heme are available. To provide insights into this phenomenon, we compared the proteomic profiles of L. lactis under fermentative and respiratory growth conditions in rich medium. We identified 21 proteins whose levels differed significantly between these conditions. Two major groups of proteins were distinguished, one involved in carbon metabolism and the second in nitrogen metabolism. Unexpectedly, enzymes of the proteolytic system (PepO1 and PepC) which are repressed in rich medium in fermentation growth were induced under respiratory conditions despite the availability of free amino acids. A triple mutant (dtpT dtpP oppA) deficient in oligopeptide transport displayed normal respiration, showing that increased proteolytic activity is not an absolute requirement for respiratory metabolism. Transcriptional analysis confirmed that pepO1 is induced under respiration-permissive conditions. This induction was independent of CodY, the major regulator of proteolytic functions in L. lactis. We also observed that pepO1 induction is redox sensitive. In a codY mutant, pepO1 expression was increased twofold in aeration and eightfold in respiration-permissive conditions compared to static conditions. These observations suggest that new regulators activate proteolysis in L. lactis, which help to maintain the energetic needs of L. lactis during respiration.

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Analysis of Expression of a Cytosolic Enzyme on the Surface of Streptococcus pyogenes

Cited by 32 publications

References 35 publications

Glycolytic enzymes associated with the cell surface of Streptococcus pneumoniae are antigenic in humans and elicit protective immune responses in the mouse

Glycolytic enzymes associated with the cell surface of Streptococcus pneumoniae are antigenic in humans and elicit protective immune responses in the mouse

Role of the C-Terminal Lysine Residues of Streptococcal Surface Enolase in Glu- and Lys-Plasminogen-Binding Activities of Group A Streptococci

Proteome Analyses of Heme-Dependent Respiration inLactococcus lactis: Involvement of the Proteolytic System

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