Abstract
Thiol-activated cytolysins share a conserved hydrophobic, Trp-rich undecapeptide that is suggested to be involved in membrane binding and intercalation. The neutralizing monoclonal antibody PLY-5 recognizes all members of this toxin family and peptide mapping assigned its epitope to the undecapeptide motif. This antibody inhibited binding of the toxins to host cell membranes and the epitope was no longer available for binding when a preformed toxin/membrane complex was tested. These results confirm the model of cytolysin binding suggested by structural data.
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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Antibodies, Monoclonal / immunology
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Bacteria
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Bacterial Proteins
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Cell Membrane / metabolism*
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Conserved Sequence / immunology*
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Cytotoxins / immunology*
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Cytotoxins / metabolism
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Epitope Mapping
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Erythrocyte Membrane / metabolism
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Molecular Sequence Data
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Sequence Homology, Amino Acid
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Sheep
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Streptolysins / immunology
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Sulfhydryl Compounds / metabolism
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Tryptophan / immunology
Substances
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Antibodies, Monoclonal
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Bacterial Proteins
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Cytotoxins
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Streptolysins
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Sulfhydryl Compounds
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plY protein, Streptococcus pneumoniae
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Tryptophan