Controllable Production Profile of Vibrio vulnificus Metalloprotease VvpE

Vibrio vulnificus produces the metalloprotease VvpE with the molecular size of 45 kDa, which was reported to form VvpE with 34 kDa via extracellular autoproteolysis. However, our previous study revealed that two forms of VvpE were simultaneously produced and 34 kDa-VvpE was the main form in cell lysates as well as culture supernatants. Moreover, this study showed conditions that 45 kDa-VvpE was produced in the main form. This VvpE production profile was inverted by a mutation in crp encoding cAMP-receptor protein and recovered by in trans complementing the wild-type crp. Accordingly, these results suggest that the proteolytic cleavage of VvpE may be a controllable reaction rather than a spontaneous reaction.