Abstract
The HlyX, a putative hemolysin identified from the Leptospira genomes, was cloned, expressed in Escherichia coli, purified, and its hemolytic activity was confirmed. Mouse polyclonal antiserum against the recombinant HlyX recognized HlyX-related antigens in a panel of Leptospira species extracts and it was also able to abolish the hemolytic activity of HlyX. A mixture of HlyX and LipL32, a known hemolysin from Leptospira, induced hemolysis in a synergistic way that was fully inhibited by antiserum against either protein. Moreover, sera from patients with leptospirosis also recognized the recombinant HlyX, showing that it is presented to the host immune system during Leptospira infection.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Bacterial Outer Membrane Proteins / pharmacology*
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Bacterial Proteins / pharmacology*
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Cells, Cultured
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Drug Synergism
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Erythrocytes / drug effects
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Erythrocytes / pathology
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Female
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Hemolysin Proteins / chemistry*
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Hemolysin Proteins / genetics
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Hemolysin Proteins / metabolism
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Hemolysin Proteins / pharmacology*
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Hemolysis / drug effects*
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Hemolysis / physiology*
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Humans
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Leptospira interrogans / classification
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Leptospira interrogans / metabolism*
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Lipoproteins / pharmacology*
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Mice
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Mice, Inbred BALB C
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Molecular Sequence Data
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Recombinant Proteins / analysis
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Recombinant Proteins / pharmacology
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Species Specificity
Substances
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Bacterial Outer Membrane Proteins
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Bacterial Proteins
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Hemolysin Proteins
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LipL32 protein, Leptospira
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Lipoproteins
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Recombinant Proteins
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hemolysin hlx protein, bacteria