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Research Support, Non-U.S. Gov't
Two Forms of Vibrio vulnificus Metalloprotease VvpE are Secreted via the Type II General Secretion System
Jong Park , So-Yeon Ryu , Choon-Mee Kim , Sung-Heui Shin
J. Microbiol. 2008;46(3):338-343.   Published online July 5, 2008
DOI: https://doi.org/10.1007/s12275-008-0058-6
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AbstractAbstract
Vibrio vulnificus has been known to secrete one form of metalloprotease VvpE (45 kDa) that is cleaved to 34 kDa-VvpE and 11 kDa-C-terminal propeptide via extracellular autoproteolysis. However, we found that extracellular secretion of both the 34 and 45 kDa forms of VvpE began in the early growth phase; moreover, 34 kDa-VvpE existed as the major form in V. vulnificus cell lysates and culture supernatants. In addition, extracellular secretion of both 34 and 45 kDa-VvpE was blocked by mutation of the pilD gene, which encodes for the type IV leader peptidase/N-methyltransferase of the type II general secretion system, and the blocked VvpE secretion was recovered by in trans-complementation of the wild-type pilD gene. These results indicate that 34 kDa-VvpE is the major form secreted along with 45 kDa-VvpE from the early growth phase via the PilD-mediated type II general secretion system.

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