Functional characterization of chitinase from Cydia pomonella granulovirus.
Baculovirus chitinases (V-CHIAs) play a crucial role in the terminal liquefaction of virus-infected larvae after death. Although v-chiAs from nucleopolyhedroviruses (NPVs) have been well characterized, little is known about v-chiAs from granuloviruses (GVs). We characterized the v-chiA of Cydia pomonella GV (CpGV) by constructing a recombinant Bombyx mori NPV (BmNPV) in which BmNPV v-chiA was replaced by CpGV v-chiA (103CpGV virus). CpGV v-chiA encoded an approximately 70-kDa chitinase with an exo-type substrate preference. CpGV V-CHIA lacked a C-terminal KDEL endoplasmic reticulum retention motif and was suggested to be a secretory protein. Terminal host liquefaction of B. mori larvae and proper folding of BmNPV-encoded cysteine protease (BmNPV V-CATH) were observed following infection with 103CpGV, indicating that CpGV v-chiA is able to compensate for the absence of its BmNPV counterpart. Our data suggest that the molecular interaction between V-CHIA and V-CATH may be conserved across a broad range of lepidopteran GVs and NPVs.
Daimon
T
T
Graduate School of Agricultural and Life Sciences, Department of Agricultural and Environmental Biology, The University of Tokyo, Tokyo, Japan.
Katsuma
S
S
Kang
W K
WK
Shimada
T
T
D000818:Animals; D002460:Cell Line; D002688:Chitinases / Q000235:genetics*; D003546:Cysteine Endopeptidases / Q000235:genetics; D004279:DNA, Viral / Q000235:genetics; D005814:Genes, Viral; D025722:Granulovirus / Q000201:enzymology* / Q000235:genetics*; D007814:Larva / Q000821:virology; D009036:Moths / Q000821:virology*
D004279:DNA, Viral; D002688:Chitinases; D003546:Cysteine Endopeptidases