Surface immunolocalisation of HPr in the equine pathogen Streptococcus equi.
We have investigated the surface localisation of the phosphotransferase system protein HPr in the equine pathogen Streptococcus equi subsp. equi using immunogold localisation and transmission electron microscopy. Like the LppC acid phosphatase lipoprotein, a reference surface antigen, the S. equi HPR could be clearly detected on the surfaces of intact cells. This study is consistent with previous reports that some streptococcal HPr is cell surface associated and suggests that the extracytoplasmic mobilisation and transfer of phosphate groups by streptococci warrant further investigation.
Dixon
S
S
School of Sciences, University of Sunderland, UK.
Haswell
M
M
Harrington
D
D
Sutcliffe
I C
IC
D001426:Bacterial Proteins / Q000378:metabolism*; D007150:Immunohistochemistry; D008854:Microscopy, Electron; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000378:metabolism*; D018502:Streptococcus equi / Q000378:metabolism*
D001426:Bacterial Proteins; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C030182:phosphocarrier protein HPr