Identification of an Amsacta spheroidin-like protein within the occlusion bodies of Choristoneura entomopoxviruses.
Identification of an Amsacta spheroidin-like protein within the occlusion bodies of Choristoneura entomopoxviruses.
复制标题
Choristoneura 昆虫痘病毒包涵体内 Amsacta 河豚精蛋白样蛋白的鉴定。
DOI：
10.1006/viro.1993.1020
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发表时间：
1993
期刊：
影响因子：
3.7
通讯作者：
Moyer,RW
中科院分区：
文献类型：
--
作者：
Hall,RL;Moyer,RW
与杆状病毒一样，昆虫痘病毒的一个特征是病毒粒子在环境稳定的包涵体内融合。病毒的这种封闭形式是传播给其他昆虫的主要原因。虽然杆状病毒包涵体的主要蛋白（多角体蛋白）在病毒之间非常相似，但据报道，两种B组昆虫痘病毒Amsacta moorei（AmEPV）和Choristoneura biennis（CbEPV）的主要包涵体蛋白（河豚精蛋白）在氨基酸序列和相应河豚精蛋白基因的编码能力（115和47 kDa）方面都有很大差异。分别为 AmEPV 和 CbEPV）。我们报告在 CbEPV 和第二种 Choristoneuravirus Choristoneura fumiferana (CfEPV) 中发现了 AmEPV 河豚精蛋白基因同源物。针对 AmEPV 115-kDa 河豚精蛋白的抗体与两种 Choristoneuraviruses 包涵体制剂中发现的~115 kDa 主要蛋白质发生反应。对来自 CbEPV 的 115 kDa 蛋白质的一小部分进行直接蛋白质微测序，得到了与 AmEPV 河豚精蛋白基因相应区域相同的肽序列。我们推测正是这个 Choristoneura 基因编码河豚精蛋白。然而，所有在 AmEPV 中寻找先前报道的 CbEPV 河豚精蛋白基因同源物的尝试均未成功。我们还表明，这个新鉴定的 AmEPV 河豚精蛋白基因的 Choristoneura 同源物以及 AmEPV 河豚精蛋白基因本身都位于 NPH I 基因的 3' 端，并且在所有三种病毒中高度同源，表明这三种病毒的基因组区域是共线的。这些结果和其他结果表明，虽然昆虫病毒缺乏在脊椎动物痘病毒中观察到的保守基因的传统中央核心，但昆虫痘病毒也可能进化出了无脊椎动物痘病毒所独有的保守基因的替代中央核心。
Like baculoviruses, a characteristic feature of entomopoxviruses is the amalgamation of virions within environmentally stable occlusion bodies. It is this occluded form of the virus that is primarily responsible for dissemination to other insects. While the major protein (polyhedrin) of baculovirus occlusions is quite similar between viruses, it has been reported that the major occlusion body protein (spheroidin) of two group B entomopoxviruses,Amsacta moorei(AmEPV) andChoristoneura biennis(CbEPV) is quite different both in terms of amine acid sequence and coding capacity of the corresponding spheroidin genes (115 and 47 kDa for AmEPV and CbEPV, respectively). We report the discovery of a AmEPV spheroidin gene homolog in both CbEPV and a secondChoristoneuravirus,Choristoneura fumiferana(CfEPV). Antibodies directed against the AmEPV 115-kDa spheroidin reacted with the major protein of ∼115 kDa found within the occlusion body preparation from bothChoristoneuraviruses. Direct protein microsequencing of small portions of the 115-kDa protein from CbEPV has resulted in peptide sequences identical to those of corresponding regions of the AmEPV spheroidin gene. We suggest that it is thisChoristoneuragene which encodes spheroidin. All attempts, however, to find a homolog of the previously reported CbEPV spheroidin gene within AmEPV have been unsuccessful. We also show this newly identifiedChoristoneurahomolog of the AmEPV spheroidin gene as well as the AmEPV spheroidin gene itself are both located at the 3′ end of an NPH I gene and are highly homologous in all three viruses, indicating that this region of the genome in the three viruses is co-linear. These results and others suggest that while the insect viruses lack the traditional central core of conserved genes observed for the vertebrate poxviruses, the insect poxviruses may have also evolved an alternative central core of conserved genes, unique to the invertebrate poxviruses.