TY - JOUR
T1 - Penaeus monodon caspase is targeted by a white spot syndrome virus anti-apoptosis protein
AU - Leu, Jiann Horng
AU - Wang, Hao Ching
AU - Kou, Guang Hsiung
AU - Lo, Chu Fang
N1 - Funding Information:
This investigation was supported financially by the National Science Council grants (NSC96-2317-B-002-005, NSC95-2317-B-002-009 and NSC95-2317-B-002-010). Both Guang-Hsiung Kou and Chu-Fang Lo are corresponding authors for this work. We are indebted to Paul Barlow for his helpful criticism.
PY - 2008
Y1 - 2008
N2 - 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.
AB - 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.
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U2 - 10.1016/j.dci.2007.08.006
DO - 10.1016/j.dci.2007.08.006
M3 - Article
C2 - 17905432
AN - SCOPUS:38649105206
SN - 0145-305X
VL - 32
SP - 476
EP - 486
JO - Developmental and Comparative Immunology
JF - Developmental and Comparative Immunology
IS - 5
ER -