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2601848 
Journal Article 
Penaeus monodon caspase is targeted by a white spot syndrome virus anti-apoptosis protein 
Leu, JH; Wang, H; Kou, GH; Lo, C 
2008 
Yes 
Developmental and Comparative Immunology
ISSN: 0145-305X 
32 
476-486 
English 
Caspases play a central and evolutionarily conserved role in mediating and executing apoptosis. Here, we report the cloning and characterization of a caspase from Penaeus monodon, Pm caspase. The full-length Pm caspase cDNA is 1386 bp, encoding a polypeptide of 304 amino acids with a calculated molecular mass of 34.3 kDa. BLASTP analysis against the NCBI nr database showed that Pm caspase is similar to insect effector caspases. RT-PCR analysis showed that Pm caspase mRNA is expressed in all examined tissues. When Pm caspase was overexpressed in SF-9 cells, the cells showed apoptotic morphological features including the formation of apoptotic bodies and DNA ladders. The caspase-3 activity of Pm caspase was determined using the recombinant protein purified from Escherichia coli. Both RT-PCR and qRT-PCR analyses showed that the RNA levels of Pm caspase and P monodon inhibitor of apoptosis protein (PmIAP) remained unchanged after white spot syndrome virus (WSSV) infection. We also used Pm caspase to show that WSSV449, an anti-apoptosis protein encoded by WSSV, is a direct caspase inhibitor. (c) 2007 Elsevier Ltd. All rights reserved. 
Penaeus monodon; capase; inhibitor of apoptosis protein; IAP; white spot syndrome virus; WSSV; apoptosis; WSSV449