two oyster shells - top one showing inside and bottom showing outside of the shell

 
Oyster Research and Restoration in U.S. Coastal Waters: Strategies for the Future
September 8-9, 2003 - Annapolis, Maryland

Abstracts
Workgroup: Frontiers in Disease Research

Identification of inhibitors against Perkinsus marinus proteases in oysters.

Principal Investigator(s):
Dr. Mohamed Faisal, Department of Environmental Sciences, School of Marine Science/Virginia Institute of Marine Science, The College of William and Mary

Co-Investigator(s):
Drs. S.L. Kaattari and J.F. La Peyre, Department of Environmental Sciences, School of Marine Science/Virginia Institute of Marine Science, The College of William and Mary

Funding Period: 1996

  • The plasma of eastern (Crassostrea virginica) and Pacific (Crassostrea gigas) oysters were compared for levels of inhibitory activities against a variety of serine, cysteine, metallo and aspartic proteases representing all protease mechanistic classes including extracellular proteases produced by two oyster-associated pathogens; Perkinsus marinus and Vibrio vulnificus.
  • In comparison to C. virginica, C. gigas plasma exhibited significantly higher specific inhibition levels (ng protease inhibited/ mu g plasma protein) for papain (P < 0.001), pepsin (P < 0.001), P. marinus protease (P < 0.001), trypsin (P = 0.015), and V. vulnificus protease (P < 0.001). Plasma of C. gigas did not inhibit the metalloprotease thermolysin.
  • Using substrate impregnated gel electrophoresis, it was possible to visualise oyster protease inhibitors against P. marinus protease (PMP). C. gigas possesses a number of protease inhibitors against PMP with significantly higher specific activities than those in C. virginica.

IMPACTS and/or BENEFITS:
Findings of this study demonstrated the presence of protease inhibitors in the plasma of Crassostrea spp., which may have an impact upon host defense mechanisms, in addition to other physiological roles. It was obvious that C. gigas, which is tolerant to P. marinus infection, is capable of mobilizing a larger number of protease inhibitors against PMP with much higher specific activities. This study also gives evidence for the presence of a broad spectrum of humoral host defenses (metalloproteases and their inhibitors) that is brought to bear on P. marinus infections by these two Crassostrea species.

This newly acquired knowledge is a cornerstone for further investigations on oysters and disease resistance.

PROJECT PUBLICATIONS:

Faisal, M., J.L. Oliver, and S.L. Kaattari (1999): Potential Role of Protease-Antiprotease Interactions in Perkinsus marinus infection in Crassostrea spp. Bull. Eur. Assoc. Fish Pathol. 19:269-276.

Faisal, M., E.A. MacIntyre, K.G. Adham, B.D. Tall, M.H. Kothary, and J.F. La Peyre (1998): Evidence for the presence of protease inhibitors in eastern (Crassostrea virgininca) and Pacific (Crassostrea gigas) oysters. Comparative Biochemistry and Physiology B 121:161-168.

Oliver, J.L., P.M. Gaffney, S.K. Allen, M. Faisal, S.L. Kaattari (2001): Protease inhibitory activity in selectively bred families of eastern oysters, Crassostrea virginica. Journal of Aquatic Animal Health 12:136-145.

Oliver, J.L., T. D. Lewis, M. Faisal, and S. L. Kaattari (2000): Analysis of the effects of Perkinsus marinus proteases on plasma proteins of the eastern oyster (Crassostrea virginica) and the Pacific oyster (Crassostrea gigas). J. Invertebr. Pathol. 74:173-183.



UM-SG-TS-2003-01 www.mdsg.umd.edu
   
This publication was supported by funds from
the NOAA National Sea Grant College Program and the
Maryland and Virginia Sea Grant College Programs

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