Open AccessCellular location of polyamine transport protein PotD in Streptococcus pneumoniae
Author(s) -
Shah Pratik,
Marquart Mary,
Quin Lisa R.,
Swiatlo Edwin
Publication year - 2006
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2006.00352.x
Subject(s) - streptococcus pneumoniae , flow cytometry , virulence , bacteria , biology , cytoplasm , polyamine , microbiology and biotechnology , transport protein , biochemistry , gene , genetics
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.