Functional characterization of chitinase from Cydia pomonella granulovirus
Functional characterization of chitinase from Cydia pomonella granulovirus
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DOI：
10.1007/s00705-007-1000-7
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发表时间：
2007-09-01
影响因子：
2.7
通讯作者：
Shimada, T.
中科院分区：
文献类型：
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作者：
Daimon, T.;Katsuma, S.;Shimada, T.
杆状病毒几丁质酶(V-chias)在感染病毒的幼虫死亡后的最终液化过程中起着至关重要的作用。尽管核型多角体病毒(NPV)的V-CHIA已被很好地描述，但对粒病毒(GV)的V-CHIA却知之甚少。构建了用CpGV v-chia(103CpGV病毒)取代BmNPV v-chia的重组家蚕核型多角体病毒(BmNPV)，鉴定了CpGV的v-chia。CpGV v-chia编码约70 kDa的几丁质酶，具有外向型底物偏好。CpGV V-chia缺乏C端KDEL内质网滞留基序，被认为是一种分泌型蛋白。感染103CpGV后，家蚕幼虫的末端宿主液化和BmNPV编码的半胱氨酸蛋白酶(BmNPV V-Cath)正确折叠，表明CpGV v-chia能够弥补BmNPV V-Cath的缺失。我们的数据表明，V-Chia和V-Cath之间的分子相互作用在鳞翅目昆虫的GV和NPV中可能是保守的。
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.