A novel slow-tight binding serine protease inhibitor from eastern oyster (Crassostrea virginica) plasma inhibits perkinsin, the major extracellular protease of the oyster protozoan parasite Perkinsus marinus

Author(s):  
Qing-Gang Xue ◽  
Grover L. Waldrop ◽  
Kevin L. Schey ◽  
Naoki Itoh ◽  
Masahiro Ogawa ◽  
...  
1999 ◽  
Vol 65 (9) ◽  
pp. 4261-4263 ◽  
Author(s):  
B. D. Tall ◽  
J. F. La Peyre ◽  
J. W. Bier ◽  
M. D. Miliotis ◽  
D. E. Hanes ◽  
...  

ABSTRACT The in vitro effects of the Perkinsus marinus serine protease on the intracellular survival of Vibrio vulnificusin oyster hemocytes were examined by using a time-course gentamicin internalization assay. Results showed that protease-treated hemocytes were initially slower to internalize V. vulnificus than untreated hemocytes. After 1 h, the elimination of V. vulnificus by treated hemocytes was significantly suppressed compared with hemocytes infected with invasive and noninvasive controls. Our data suggest that the serine protease produced byP. marinus suppresses the vibriocidal activity of oyster hemocytes to effectively eliminate V. vulnificus, potentially leading to conditions favoring higher numbers of vibrios in oyster tissues.


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