Title Two Forms of Vibrio vulnificus Metalloprotease VvpE are Secreted via the Type II General Secretion System
Author Jong Park1,2, So-Yeon Ryu1,2, Choon-Mee Kim1, and Sung-Heui Shin1,3*
Address 1Research Center for Resistant Cells, Chosun University Medical School, Gwangju 501-759, Republic of Korea, 2Department of Preventive Medicine, Chosun University Medical School, Gwangju 501-759, Republic of Korea, 3Department of Microbiology, Chosun University Medical School, Gwangju 501-759, Republic of Korea
Bibliography Journal of Microbiology, 46(3),338-343, 2008,
DOI
Key Words Vibrio vulnificus, metalloprotease, general secretion system
Abstract 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.