Abridged region from Escherichia coli periplasmic stress sensor DegS acts as plasminogen activator in vitro.
It is well known that the Escherichia coli inner membrane-bound protease DegS is a periplasmic stress sensor for unfolded outer membrane proteins (OMPs). Previous studies have also shown that the outer membrane protease OmpT activates plasminogen in vitro and this may be exploited by bacteria in the course of pathogenesis. However, there has been no research on the plasminogen activation ability of the important periplasmic protein DegS. Accordingly, in this study, the whole-length and truncated degS genes were separately overexpressed in Escherichia coli, the recombinant proteins purified by affinity chromatography, and their plasminogen activator role tested in vitro. The results suggested that the whole-length DegS was able to activate plasminogen on a plasma plate. The truncated form of DegS (residues 80-345), designated delta DegS, also acted as a plasminogen activator, as confirmed by different assays. The serine protease property of delta DegS was verified based on the complete inhibition of its enzyme activity by PMSF (phenylmethanesulfonyl fluoride). Therefore, the present results indicate that DegS is a plasminogen activator in vitro.
State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, P R China, 430072.
Junpeng
J
Yan
Juho
J
Ko
Yipeng
Y
Qi
D029968:Escherichia coli Proteins / Q000737:chemistry / Q000494:pharmacology*; D006801:Humans; D010446:Peptide Fragments / Q000494:pharmacology*; D010960:Plasminogen Activators / Q000494:pharmacology*
D029968:Escherichia coli Proteins; D010446:Peptide Fragments; C489349:degS protein, Escherichia coli; D010960:Plasminogen Activators