Cellular location of polyamine transport protein PotD in Streptococcus pneumoniae

FEMS Microbiol Lett. 2006 Aug;261(2):235-7. doi: 10.1111/j.1574-6968.2006.00352.x.

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

  • Antibodies, Bacterial / immunology
  • Bacterial Capsules / chemistry
  • Bacterial Proteins / analysis
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / immunology
  • Cell Fractionation
  • Cell Membrane / chemistry*
  • Flow Cytometry
  • Immunoblotting
  • Membrane Transport Proteins / analysis*
  • Membrane Transport Proteins / chemistry
  • Membrane Transport Proteins / immunology
  • Polyamines / metabolism*
  • Protein Sorting Signals
  • Protein Structure, Tertiary
  • Streptococcus pneumoniae / chemistry*

Substances

  • Antibodies, Bacterial
  • Bacterial Proteins
  • Membrane Transport Proteins
  • Polyamines
  • Protein Sorting Signals