棉铃虫核型多角体病毒侵染机制的研究
摘要
棉铃虫核型多角体病毒(Heliothis armigera Nuleopolyhedrovirus, HaNPV)是棉铃虫的天然病原体，对棉铃虫有特异的致死效应，不危害人畜及环境，是进行棉铃虫生物防治的好材料。国内外已广泛应用棉铃虫核型多角体病毒防治棉铃虫。棉铃虫核型多角体病毒是我国最早注册的杆状病毒杀虫剂，到1999年，约有100，000公顷棉田用棉铃虫核型多角体病毒的生物制剂防治害虫。国内已对HaNPV进行了多方面的研究，包括病毒株的分离鉴定、形态特征、病毒生物活性测定、离体细胞感染和复制、测序和功能基因研究，基因工程病毒杀虫剂的构建等；但对其复制侵染与宿主细胞互作的分子机理，目前仍缺乏足够且深入的了解。
Chariton C A & Volkman L Z于1993年研究了AcMNPV感染Sf21细胞过程中肌动蛋白的变化情况，他们发现在病毒侵染的早期(3hr p.i)，即使用放线菌酮抑制细胞蛋白合成，细胞中原有的肌动蛋白也可被脱去囊膜而进入细胞的核衣壳诱导形成缆索(cable)结构。在病毒感染的迟早期，即病毒复制DNA以前(3-6hr p.i)，细胞变园，肌动蛋白在整个细胞中都出现凝集，这种凝集可被放线菌酮(抑制细胞和病毒蛋白合成)抑制而对蚜栖菌素(抑制细胞而不抑制病毒蛋白合成)不敏感，这表明病毒早期蛋白合成有利于这种凝集而与细胞蛋白无关，并且这种凝集与细胞变园无相关性，细胞变园也可通过其他途径如秋水仙素处理而实现，但此时并无肌动蛋白凝集现象。在病毒形成对数期(6-12hr p.i)，病毒核衣壳与肌动蛋白纤丝同时存在于核内病毒发生基质中。于是他们认为核衣壳导致细胞内肌动蛋白形成缆索结构，这种结构与病毒的胞内运输及其后在核内的装配以及装配后的细胞液化、病毒释放是相关的。
以上是AcMNPV在侵染过程中其核衣壳与细胞肌动蛋白的互作关系，但研究者并没有在分子水平揭示这种互作关系的机制，即并不知道核衣壳中哪种成分、哪个基因起了作用，推测AcMNPV衣壳蛋白的最主要成分VP39的作用可能很重要。VP39蛋白是杆状病毒代表种——AcMNPV衣壳的主要组成成分，Miller等1989首先鉴定AcMNPV的晚期必需基因——编码分子量为39kD的核衣壳蛋白基因vp39，许多学者对其进行了深入的研究。VP39蛋白是杆状病毒核衣壳结构最主要成分，几乎是均匀的分布在核衣壳表面。新合成的VP39蛋白几乎全部分散在细胞质中，但经过一段时间以后(大约12小时)，大部分VP39蛋白被转移到细胞核中。最近的研究发现，AcMNPV的vp39基因与侵染密切相关。
其它众多的杆状病毒的侵染过程是否也象AcMNPV那样，存在病毒衣壳与宿主
细胞ACtin的互作呢?至今的报道很少，对ljaNPV这方面的知识更是空白。为
此，我们借鉴前人的资料，开展了!laNPV侵染机制的研究。
本文首先用TR工201试剂从约10日个棉铃虫细胞Hz一AM 111“提取了1 .68mg
总RNA，用0119。(dT)纤维素柱从总RNA中分离mRNA，然后用superscript翔
Ch。iCe System for cDNA Synthesis kit试剂盒合成棉铃虫细胞Hz一AMI的
eDNA:用01190(dT)，2一l，作引物，用除去了RNaseH活胜的Supersciptll RT
从mRNA逆转录出cDNA的第一链，再以原有的mRNA作引物，以新合成的cDNA
第一链作模板，利用￡。olj DNA Polymerase工的nick translation合成
cDNA的第二链，在合成第二链的同时加入丑co了了RNasell消化fnRNA，并加入
E.Coli DNA ligase将各个片段连接起来，最后用T4 DNA polymerase将双链
cDNA的末端补平。用T4 DNA ligase将去磷酸化的EcoRI adaPter连接到双
链cDNA的末端，并用p。lynucleotide kinase使adapter磷酸化。并用CDNA
SIZe fractionati()nC。lumns筛选出大一犷500}〕p的CDNA片段。最后将大一于
SOObp的CDNA片段克隆到去磷酸化的载体质粒pGAD424的ECoR工位点，转化
大肠杆菌DHSQ，构建成棉铃虫细胞HZ一AMI的cDNA文库。质粒pGAD424是大
肠杆菌一酵母菌穿梭质粒载体，pGAD424上含有酵母菌转录激活因子GAL4蛋
白激活域的编码区(GAL4一AD)。该文库中有1/6重组质粒可在酵母中表达酵
母蛋白Ga14一AD与棉铃虫蛋白的融合蛋白。通过在合成cDNA第一链时参入。
32PdCTP，显示出合成的CDNA为6. OKb以下的连续区带，测得文库的滴度为
1.5火1。‘，可以代表亲本细胞的全部编码蛋白质的基因序列，即该文库具有
代表性(representativity)。
在成功构建棉铃虫细胞Hz一AMICDNA文库的基础上，本文接着将棉铃虫核
型多角体病毒衣壳蛋白VP39(HaNPV一VP39)基因克隆到酵母双杂交系统(yeast
two一hybrid system)中的质粒pGBTg上。pGBTg上含有酵母菌转录激活因子
GAL4 DNA结合域的编码区(GAL4一DBD)，使克隆到质粒pGBTg上的HaNPV一vp39
基因与GAL4一DBD基因融合，在酵母菌中表达DBD一vp39融合蛋白，该融合蛋
白即为酵母双杂交系统中的诱饵蛋白。然后通过酵母双杂交系统，在棉铃虫
细胞CDNA文库中钓取VP39的相互作用因子基因。按CDNA文库转化法将
Hz一AMI细胞cDNA文库质粒转化入酵母受体菌HF7C中。转化效率显示含有
pGBT39质粒和cDNA文库质粒DNA的转化子约有1.8x10卜个。7一10d后，从
SD产LeU一Trp一HIS平板上挑取1000个直径Zlnln以上的菌落划线培养于另一个
新鲜的三缺SD产TrP一Leu一HI
Heliothis armigera nuclear polyhedrosis virus (HaNPV), due to its special pestiferous effect on Heliothis armigera and being innocent to human, livestock and environment, has been a commercial bioinsecticide widely in the world for years. HaNPV is the earliest commercial baculovirus insecticide in China and about 100,000 hectare cotton farmland had been used such insecticide to prevent Heliothis armigera by the end of 1999. Many aspects of HaNPV such as the isolation and identification of different virus strains, bioassay of their toxicity, infectivity and duplication in culture cells, genome sequencing and some functional genes have been researched. But there is little understanding of the virus-host interaction.
Chariton C A &Volkman L Z researched the change of Actin in Sf21 cells during the AcMNPV infection process in 1991. They found that the original Actin can been induced to form the cable structure by the nucleocapsid just escaped from its envelope about 3hr p.i., even though the cellular protein synthesis was inhibited by aphidicolin. At the late-early phase of infection (3-6hr p.i.) and before the viral DNA replication, host cells became round and ventral aggregates of actin were observed. This precess were sensitive to cychoheximide but not to aphidicolin indicating that an early viral protein mediated this Actin rearrangement. Howerever, ventral aggregates itself did not result in
the rounding process, because uninfected cells becoming round pretreated with colchicine did not form ventral aggregates of Actin. During the viral infection login phase (6-12hr p.i.), viral nucleocapsid and filamentous Actin were found to coexisted in nucleoplasm. So nucleocapsid might induce Actin to form cable structure and this structure might associate with such viral infectious courses as the viral transportation in host cells, viral assembly in nucleus, host cells' liquefaction and viruses' release from the host cells.
Because VP39 is the major component of AcMNPV nucleocapsid, it was speculated that VP39 might play an important role in the aggregation of host cell Actin caused by AcMNPV nucleocapsid. But the researchers hadn't revealed the molecular mechanism for the interaction of AcMNPV nucleocapsid and the host Actin, i.e., which component of the nuleocapsid actually interacted with the host actin and induced it to form cable structure? vp39 gene of AcMNPV was first identified by Miller et al. in 1989, which codes a 39kD nucleocapsid protein(VP39), the main component of AcMNPV's capsid. Almost all the newly synthesized VP39 were dispersed in the cytoplasm, but most of them were then transferred to the nucleus after about 12hr and distributed on the surface of nucleocapsid equably. Recent study has shown that VP39 is associated tightly with the infectious course of AcMNPV. Does the interaction of AcMNPV nucleocapsid and Actin also exist in other kinds of baculoviruses such as HaNPV? Little has been reported by far. So we explored the infection process of HaNPV deeply in this thesis.
Using the Oligo(dT) cellulose column , 1.68mg mRNA was purified from total RNA that was isolated from 1 X 108Hz-AMl cells with TRIzol reagent. Then, cDNA of Hz-AMl cell (Ha-cDNA) was synthesized with "SuperScrip?choice system for the cDNA to synthesis kit": using Oligo(dT)12-18 as the primers, the first strains of cDNA were retrotranscripted from mRNA with SuperScripII RT
without RNaseH activity, then using original mRNA as primers and the newly synthesized first strains of cDNA as templates, the second strain of cDNA was synthesized through the nick translation function of E.coli DNA polymerase I, at the same time E.coli RNaseH was added to digest the original mRNA and the newly synthesized DNA fragments were ligated by THE addition of E.coli DNA ligase. Finally, the terminal of the newly synthesized double strain cDNA was blunted by T4 DNA polymerase. Dephosphorylated EcoRI adapter was ligated to the newly blunted terminal of cDNA with T4 DNA ligase and then was phosphorylated by polynucleotide kinase. cDNA fragments that molecular
Chariton C A & Volkman L Z于1993年研究了AcMNPV感染Sf21细胞过程中肌动蛋白的变化情况，他们发现在病毒侵染的早期(3hr p.i)，即使用放线菌酮抑制细胞蛋白合成，细胞中原有的肌动蛋白也可被脱去囊膜而进入细胞的核衣壳诱导形成缆索(cable)结构。在病毒感染的迟早期，即病毒复制DNA以前(3-6hr p.i)，细胞变园，肌动蛋白在整个细胞中都出现凝集，这种凝集可被放线菌酮(抑制细胞和病毒蛋白合成)抑制而对蚜栖菌素(抑制细胞而不抑制病毒蛋白合成)不敏感，这表明病毒早期蛋白合成有利于这种凝集而与细胞蛋白无关，并且这种凝集与细胞变园无相关性，细胞变园也可通过其他途径如秋水仙素处理而实现，但此时并无肌动蛋白凝集现象。在病毒形成对数期(6-12hr p.i)，病毒核衣壳与肌动蛋白纤丝同时存在于核内病毒发生基质中。于是他们认为核衣壳导致细胞内肌动蛋白形成缆索结构，这种结构与病毒的胞内运输及其后在核内的装配以及装配后的细胞液化、病毒释放是相关的。
以上是AcMNPV在侵染过程中其核衣壳与细胞肌动蛋白的互作关系，但研究者并没有在分子水平揭示这种互作关系的机制，即并不知道核衣壳中哪种成分、哪个基因起了作用，推测AcMNPV衣壳蛋白的最主要成分VP39的作用可能很重要。VP39蛋白是杆状病毒代表种——AcMNPV衣壳的主要组成成分，Miller等1989首先鉴定AcMNPV的晚期必需基因——编码分子量为39kD的核衣壳蛋白基因vp39，许多学者对其进行了深入的研究。VP39蛋白是杆状病毒核衣壳结构最主要成分，几乎是均匀的分布在核衣壳表面。新合成的VP39蛋白几乎全部分散在细胞质中，但经过一段时间以后(大约12小时)，大部分VP39蛋白被转移到细胞核中。最近的研究发现，AcMNPV的vp39基因与侵染密切相关。
其它众多的杆状病毒的侵染过程是否也象AcMNPV那样，存在病毒衣壳与宿主
细胞ACtin的互作呢?至今的报道很少，对ljaNPV这方面的知识更是空白。为
此，我们借鉴前人的资料，开展了!laNPV侵染机制的研究。
本文首先用TR工201试剂从约10日个棉铃虫细胞Hz一AM 111“提取了1 .68mg
总RNA，用0119。(dT)纤维素柱从总RNA中分离mRNA，然后用superscript翔
Ch。iCe System for cDNA Synthesis kit试剂盒合成棉铃虫细胞Hz一AMI的
eDNA:用01190(dT)，2一l，作引物，用除去了RNaseH活胜的Supersciptll RT
从mRNA逆转录出cDNA的第一链，再以原有的mRNA作引物，以新合成的cDNA
第一链作模板，利用￡。olj DNA Polymerase工的nick translation合成
cDNA的第二链，在合成第二链的同时加入丑co了了RNasell消化fnRNA，并加入
E.Coli DNA ligase将各个片段连接起来，最后用T4 DNA polymerase将双链
cDNA的末端补平。用T4 DNA ligase将去磷酸化的EcoRI adaPter连接到双
链cDNA的末端，并用p。lynucleotide kinase使adapter磷酸化。并用CDNA
SIZe fractionati()nC。lumns筛选出大一犷500}〕p的CDNA片段。最后将大一于
SOObp的CDNA片段克隆到去磷酸化的载体质粒pGAD424的ECoR工位点，转化
大肠杆菌DHSQ，构建成棉铃虫细胞HZ一AMI的cDNA文库。质粒pGAD424是大
肠杆菌一酵母菌穿梭质粒载体，pGAD424上含有酵母菌转录激活因子GAL4蛋
白激活域的编码区(GAL4一AD)。该文库中有1/6重组质粒可在酵母中表达酵
母蛋白Ga14一AD与棉铃虫蛋白的融合蛋白。通过在合成cDNA第一链时参入。
32PdCTP，显示出合成的CDNA为6. OKb以下的连续区带，测得文库的滴度为
1.5火1。‘，可以代表亲本细胞的全部编码蛋白质的基因序列，即该文库具有
代表性(representativity)。
在成功构建棉铃虫细胞Hz一AMICDNA文库的基础上，本文接着将棉铃虫核
型多角体病毒衣壳蛋白VP39(HaNPV一VP39)基因克隆到酵母双杂交系统(yeast
two一hybrid system)中的质粒pGBTg上。pGBTg上含有酵母菌转录激活因子
GAL4 DNA结合域的编码区(GAL4一DBD)，使克隆到质粒pGBTg上的HaNPV一vp39
基因与GAL4一DBD基因融合，在酵母菌中表达DBD一vp39融合蛋白，该融合蛋
白即为酵母双杂交系统中的诱饵蛋白。然后通过酵母双杂交系统，在棉铃虫
细胞CDNA文库中钓取VP39的相互作用因子基因。按CDNA文库转化法将
Hz一AMI细胞cDNA文库质粒转化入酵母受体菌HF7C中。转化效率显示含有
pGBT39质粒和cDNA文库质粒DNA的转化子约有1.8x10卜个。7一10d后，从
SD产LeU一Trp一HIS平板上挑取1000个直径Zlnln以上的菌落划线培养于另一个
新鲜的三缺SD产TrP一Leu一HI
Heliothis armigera nuclear polyhedrosis virus (HaNPV), due to its special pestiferous effect on Heliothis armigera and being innocent to human, livestock and environment, has been a commercial bioinsecticide widely in the world for years. HaNPV is the earliest commercial baculovirus insecticide in China and about 100,000 hectare cotton farmland had been used such insecticide to prevent Heliothis armigera by the end of 1999. Many aspects of HaNPV such as the isolation and identification of different virus strains, bioassay of their toxicity, infectivity and duplication in culture cells, genome sequencing and some functional genes have been researched. But there is little understanding of the virus-host interaction.
Chariton C A &Volkman L Z researched the change of Actin in Sf21 cells during the AcMNPV infection process in 1991. They found that the original Actin can been induced to form the cable structure by the nucleocapsid just escaped from its envelope about 3hr p.i., even though the cellular protein synthesis was inhibited by aphidicolin. At the late-early phase of infection (3-6hr p.i.) and before the viral DNA replication, host cells became round and ventral aggregates of actin were observed. This precess were sensitive to cychoheximide but not to aphidicolin indicating that an early viral protein mediated this Actin rearrangement. Howerever, ventral aggregates itself did not result in
the rounding process, because uninfected cells becoming round pretreated with colchicine did not form ventral aggregates of Actin. During the viral infection login phase (6-12hr p.i.), viral nucleocapsid and filamentous Actin were found to coexisted in nucleoplasm. So nucleocapsid might induce Actin to form cable structure and this structure might associate with such viral infectious courses as the viral transportation in host cells, viral assembly in nucleus, host cells' liquefaction and viruses' release from the host cells.
Because VP39 is the major component of AcMNPV nucleocapsid, it was speculated that VP39 might play an important role in the aggregation of host cell Actin caused by AcMNPV nucleocapsid. But the researchers hadn't revealed the molecular mechanism for the interaction of AcMNPV nucleocapsid and the host Actin, i.e., which component of the nuleocapsid actually interacted with the host actin and induced it to form cable structure? vp39 gene of AcMNPV was first identified by Miller et al. in 1989, which codes a 39kD nucleocapsid protein(VP39), the main component of AcMNPV's capsid. Almost all the newly synthesized VP39 were dispersed in the cytoplasm, but most of them were then transferred to the nucleus after about 12hr and distributed on the surface of nucleocapsid equably. Recent study has shown that VP39 is associated tightly with the infectious course of AcMNPV. Does the interaction of AcMNPV nucleocapsid and Actin also exist in other kinds of baculoviruses such as HaNPV? Little has been reported by far. So we explored the infection process of HaNPV deeply in this thesis.
Using the Oligo(dT) cellulose column , 1.68mg mRNA was purified from total RNA that was isolated from 1 X 108Hz-AMl cells with TRIzol reagent. Then, cDNA of Hz-AMl cell (Ha-cDNA) was synthesized with "SuperScrip?choice system for the cDNA to synthesis kit": using Oligo(dT)12-18 as the primers, the first strains of cDNA were retrotranscripted from mRNA with SuperScripII RT
without RNaseH activity, then using original mRNA as primers and the newly synthesized first strains of cDNA as templates, the second strain of cDNA was synthesized through the nick translation function of E.coli DNA polymerase I, at the same time E.coli RNaseH was added to digest the original mRNA and the newly synthesized DNA fragments were ligated by THE addition of E.coli DNA ligase. Finally, the terminal of the newly synthesized double strain cDNA was blunted by T4 DNA polymerase. Dephosphorylated EcoRI adapter was ligated to the newly blunted terminal of cDNA with T4 DNA ligase and then was phosphorylated by polynucleotide kinase. cDNA fragments that molecular
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