Abstract
Enolase occurs as a cytoplasmic and a surface-associated protein in bacteria. Enolases of the bacterial pathogens Streptococcus pyogenes, Streptococcus pneumoniae and Staphylococcus aureus, as well as of the commensal lactic acid bacteria, Lactobacillus crispatus and Lactobacillus johnsonii, were purified as His(6)-fusion proteins from recombinant Escherichia coli. The fusion proteins were compared for putative virulence-associated functions, i.e., binding of human plasminogen, enhancement of plasminogen activation by human plasminogen activators, as well as binding to immobilized laminin, fibronectin and collagens. The individual enolases showed varying efficiencies in these functions. In particular, highly and equally effective interactions with plasminogen and laminin were seen with lactobacillar and staphylococcal enolases.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Child
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Cloning, Molecular
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Collagen / metabolism
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DNA, Bacterial / chemistry
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DNA, Bacterial / genetics
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Fibronectins / metabolism
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Gram-Positive Bacterial Infections / microbiology
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Humans
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Lactobacillus / enzymology*
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Lactobacillus / genetics
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Laminin / metabolism
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Male
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Molecular Sequence Data
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Phosphopyruvate Hydratase / genetics
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Phosphopyruvate Hydratase / isolation & purification*
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Phosphopyruvate Hydratase / metabolism*
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Phylogeny
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Plasminogen / metabolism
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Plasminogen Activators / metabolism
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Protein Binding
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Sequence Analysis, DNA
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Staphylococcus aureus / enzymology*
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Staphylococcus aureus / genetics
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Streptococcus pneumoniae / enzymology*
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Streptococcus pneumoniae / genetics
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Streptococcus pyogenes / enzymology*
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Streptococcus pyogenes / genetics
Substances
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DNA, Bacterial
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Fibronectins
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Laminin
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Recombinant Proteins
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Plasminogen
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Collagen
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Plasminogen Activators
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Phosphopyruvate Hydratase
Associated data
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GENBANK/EF362410
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GENBANK/EF362411
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GENBANK/EF362412
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GENBANK/EF362413