Analysis of expression of a cytosolic enzyme on the surface of Streptococcus pyogenes.
The normally cytosolic glycolytic enzyme, glyceraldehyde-3-phosphate dehydrogenase, (GAPDH) has been reported to be expressed on the surface of Streptococcus pyogenes, group A, where it can act as a plasmin binding protein (Plr), and potentially a signaling molecule. In studies of wild-type and isogenic mutants, an association between surface expression of antigenic GAPDH/Plr and M and M-related fibrinogen-binding proteins was identified. Inactivation of the mga gene, whose product controls expression of M and M-related proteins also influenced expression of surface GAPDH/Plr. Revertants or pseudorevertants of mga mutants led to concomitant re-expression of surface GAPDH/Plr and M and M-related proteins. Using surface enhanced laser desorption ionization (SELDI) mass spectroscopy, a physical association between GAPDH/Plr and streptococcal fibrinogen-binding proteins was demonstrated. These studies support the hypothesis that surface M and M-related proteins are involved in anchoring GAPDH/Plr on the surface of group A streptococci.
D'Costa
S S
SS
Department of Microbiology and Immunology, Medical College of Ohio, Toledo, Ohio, USA.
Romer
T G
TG
Boyle
M D
MD
D001426:Bacterial Proteins / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism / Q000648:ultrastructure; D003600:Cytosol / Q000201:enzymology; D005340:Fibrinogen / Q000378:metabolism; D005341:Fibrinolysin / Q000378:metabolism; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D013058:Mass Spectrometry; D018000:Receptors, Peptide / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D013297:Streptococcus pyogenes / Q000201:enzymology* / Q000235:genetics / Q000648:ultrastructure
D001426:Bacterial Proteins; C101055:Plr protein, Streptococcus; D018000:Receptors, Peptide; D011994:Recombinant Proteins; D005340:Fibrinogen; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D005341:Fibrinolysin