Abstract
Streptococcus pneumoniae encodes a transporter for polyamines that contributes to virulence in an animal model. The putative polyamine-binding protein, PotD, has an amino-terminal secretory peptide but no other domains known to be involved in anchoring proteins to the surface of Gram-positive bacteria. Cell fractionation and immunoblotting, along with flow cytometry, suggest that PotD is surface-exposed and anchored to the cytoplasmic membrane by a potentially novel mechanism.
MeSH terms
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Antibodies, Bacterial / immunology
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Bacterial Capsules / chemistry
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Bacterial Proteins / analysis
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Bacterial Proteins / chemistry
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Bacterial Proteins / immunology
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Cell Fractionation
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Cell Membrane / chemistry*
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Flow Cytometry
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Immunoblotting
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Membrane Transport Proteins / analysis*
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Membrane Transport Proteins / chemistry
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Membrane Transport Proteins / immunology
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Polyamines / metabolism*
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Protein Sorting Signals
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Protein Structure, Tertiary
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Streptococcus pneumoniae / chemistry*
Substances
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Antibodies, Bacterial
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Bacterial Proteins
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Membrane Transport Proteins
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Polyamines
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Protein Sorting Signals