Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein.
The recruitment of plasminogen endows the bacterial cell surface of Streptococcus pneumoniae with proteolytic activity. In this study we demonstrate specific plasmin- and plasminogen-binding activity for the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH), which is located in the cytoplasm as well as on the surface of pneumococci. GAPDH exhibits a high affinity for plasmin and a significantly lower affinity for plasminogen.
Bergmann
Simone
S
Research Center for Infectious Diseases, University of Würzburg, Wuerzburg, Germany.
Rohde
Manfred
M
Hammerschmidt
Sven
S
D001483:Base Sequence; D005341:Fibrinolysin / Q000378:metabolism*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D010958:Plasminogen / Q000378:metabolism*; D013296:Streptococcus pneumoniae / Q000201:enzymology* / Q000235:genetics; D020349:Surface Plasmon Resonance
D010958:Plasminogen; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D005341:Fibrinolysin