CN108450467A - FoF1-ATPaseβ蛋白在促进或降低细胞吸收凋亡小体中的应用 - Google Patents
FoF1-ATPaseβ蛋白在促进或降低细胞吸收凋亡小体中的应用 Download PDFInfo
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Abstract
本申请提供了FoF1‑ATPaseβ蛋白在促进细胞吸收凋亡小体中的应用，其中，所述FoF1‑ATPaseβ蛋白的氨基酸序列中含有WalK A模序和WalK B模序。
Description
技术领域
本申请涉及FoF1-ATPaseβ蛋白在促进细胞吸收凋亡小体中的应用。特别是FoF1-ATPaseβ蛋白在用于控制害虫中的应用，或在制备用于控制动物或人由于凋亡小体积累引起的炎症和/或自身免疫疾病的药物中的应用；此外本申请还涉及一种鉴定候选细胞内源蛋白是否影响细胞吸收凋亡小体的方法。
背景技术
凋亡小体是最大的一种胞囊，直径为1-5μm，凋亡小体内含有DNA，microRNA和蛋白质。
对于昆虫等体型较小的动物来说，一般认为细胞凋亡在10％以下(例如7％)为正常现象，但是当凋亡在生物体内累积在10％以上时，则会影响其生长发育；严重时，例如凋亡在生物体内累积在20％左右时可以导致其死亡。
对于人或哺乳动物，凋亡在生物体内累积，虽然不会引起死亡，但也会引发例如炎症或自身免疫疾病等方面的病变，为害生物体的健康状况。
然而，到目前为止，一直未能解决控制凋亡小体积累的方法。
发明内容
本申请之一提供了FoF1-ATPaseβ蛋白在促进或降低细胞吸收凋亡小体中的应用，其中，所述FoF1-ATPaseβ蛋白的氨基酸序列中含有Walk A模序和WalK B模序。
在一个具体实施方式中，所述Walk A模序为如SEQ ID No.1或SEQ ID No.2所示的氨基酸序列，所述Walk B模序为如Arg Xaa Xaa Xaa Gly Xaa Xaa Xaa Leu Jaa Jaa JaaAsp所示的氨基酸序列或如Lys Xaa Xaa Xaa Gly Xaa Xaa Xaa Leu Jaa Jaa Jaa Asp所示的氨基酸序列；其中如SEQ ID No.1所示的氨基酸序列、SEQ ID No.2所示的氨基酸序列、如Arg Xaa Xaa Xaa Gly Xaa Xaa Xaa Leu Jaa Jaa Jaa Asp所示的氨基酸序列或如LysXaa Xaa Xaa Gly Xaa Xaa Xaa Leu Jaa Jaa Jaa Asp所示的氨基酸序列中的Xaa独立地为甘氨酸、丙氨酸、缬氨酸、亮氨酸、异亮氨酸、苯丙氨酸、脯氨酸、色氨酸、丝氨酸、酪氨酸、半胱氨酸、蛋氨酸、天冬酰胺、谷氨酰胺、苏氨酸、天冬氨酸、谷氨酸、赖氨酸、精氨酸和组氨酸中的任意一种氨基酸，如Arg Xaa Xaa Xaa Gly Xaa Xaa Xaa Leu Jaa Jaa Jaa Asp的氨基酸序列或如Lys Xaa Xaa Xaa Gly Xaa Xaa Xaa Leu Jaa Jaa Jaa Asp所示的氨基酸序列中的Jaa为疏水性氨基酸。需要强调的是在同一个序列中存在多个Xaa时，该序列中的每个Xaa独立地为甘氨酸、丙氨酸、缬氨酸、亮氨酸、异亮氨酸、苯丙氨酸、脯氨酸、色氨酸、丝氨酸、酪氨酸、半胱氨酸、蛋氨酸、天冬酰胺、谷氨酰胺、苏氨酸、天冬氨酸、谷氨酸、赖氨酸、精氨酸和组氨酸中的任意一种氨基酸。例如SEQ ID No.1中的四个Xaa，可以彼此相同，也可以彼此不同。同一个序列中存在多个Jaa时，该序列中的每个Jaa独立地为疏水性氨基酸。例如如Arg Xaa Xaa Xaa Gly Xaa Xaa Xaa Leu Jaa Jaa Jaa Asp所示的氨基酸序列中的三个Jaa，可以彼此相同，也可以彼此不同。
在一个具体实施方式中，所述疏水性氨基酸选自酪氨酸、色氨酸、苯丙氨酸、缬氨酸、亮氨酸、异亮氨酸、和丙氨酸中的一种。
在一个具体实施方式中，所述Walk A模序为如SEQ ID No.3所示的氨基酸序列，所述Walk B模序为如SEQ ID No.4所示的氨基酸序列。
在一个具体实施方式中，所述FoF1-ATPaseβ蛋白的氨基酸序列为来源于昆虫纲中的任意一种昆虫的FoF1-ATPaseβ蛋白；优选所述FoF1-ATPaseβ蛋白的氨基酸序列为来源于鳞翅目中的任意一种昆虫的FoF1-ATPaseβ蛋白。
在一个具体实施方式中，所述FoF1-ATPaseβ蛋白的氨基酸序列如SEQ ID No.6所示。
本申请之二提供了如本申请之一任意一项所述的应用中的所述FoF1-ATPaseβ蛋白在用于控制害虫中的应用。
在一个具体实施方式中，优选所述害虫为昆虫纲中的任意一种昆虫。
在一个具体实施方式中，更优选所述害虫为来源于鳞翅目中的任意一种昆虫。
本申请之三如本申请之一中所述的应用中的所述FoF1-ATPaseβ蛋白在制备用于控制动物或人由于凋亡小体积累引起的炎症和/或自身免疫疾病的药物中的应用。其中，所述FoF1-ATPaseβ蛋白在控制动物或人由于凋亡小体积累引起的炎症时，其最好为来自于该动物或人的FoF1-ATPaseβ蛋白，即用于控制疾病的FoF1-ATPaseβ蛋白的氨基酸序列与其该物种自身的内源FoF1-ATPaseβ蛋白的氨基酸序相同，或者为其该物种自身的内源FoF1-ATPaseβ蛋白的氨基酸序的截短序列。
在一个具体实施方式中，所述动物可以为宠物、牲畜、禽类等，例如狗、猫、兔、猪、牛、羊、鸡、鸭和鹅等。
本申请之四提供了一种鉴定候选细胞内源蛋白是否影响细胞吸收凋亡小体的方法，所述方法选自下列方案之一：
方案一：步骤1)、步骤3)、步骤4)和步骤5)；
方案二：步骤1)、步骤2)、步骤6)、步骤7)和步骤8)；
方案三：步骤1)、步骤2)、步骤3)、步骤4)、步骤5)、步骤6)、步骤7)和步骤8)；
其中，
1)将定位于细胞表面的第一蛋白与第一标签在第一细胞中融合表达，得到表达有所述第一蛋白与所述第一标签的融合产物的第二细胞；并且所述第一蛋白与所述第一标签在所述第一细胞中融合表达后，使所述第二细胞形成凋亡小体；其中，所述第一标签为所述第一细胞中不能内源表达的蛋白质或多肽；形成凋亡小体后，第一蛋白与第一标签的融合产物会位于凋亡小体的表面，并且所述第一蛋白越稳定越好(即不容易被降解)；
2)将所述候选细胞内源蛋白在第三细胞中过表达，得到过表达所述候选细胞内源蛋白的第四细胞；
3)对于第一处理组：在用所述候选细胞内源蛋白的抗体处理所述第三细胞后，与步骤1)中形成的凋亡小体混合后进行培养，得到第一处理细胞；
对于第一对照组：将步骤1)中形成的凋亡小体与所述第三细胞混合后进行培养，得到第一对照细胞；
4)分别提取第一处理细胞和第一对照细胞的总蛋白，依次得到第一处理蛋白和第一对照蛋白；
5)将所述第一标签的抗体与所述第一处理蛋白进行定量或半定量抗原/抗体反应；将所述第一标签的抗体与所述第一对照蛋白进行定量或半定量抗原/抗体反应；根据第一处理组和第一对照组分别得到的定量或半定量抗原/抗体反应结果确定所述候选细胞内源蛋白是否影响细胞吸收凋亡小体；
6)对于第二处理组：将步骤1)中形成的凋亡小体与步骤2)中的第四细胞混合后进行培养，得到第二处理细胞；
对于第二对照组：将步骤1)中形成的凋亡小体与第五细胞与混合后进行培养，得到第二对照细胞；其中所述第五细胞与所述第四细胞的不同之处仅在于，所述第五细胞中不含有外加的编码所述候选细胞内源蛋白的DNA或RNA，也不含有外加的所述候选细胞内源蛋白；例如，当编码候选细胞内源蛋白的核苷酸克隆到pIZT/V5-His质粒载体上后再转染第三细胞得到第四细胞时，那么就利用没有克隆编码候选细胞内源蛋白的核苷酸的pIZT/V5-His空载体转染第三细胞得到第五细胞。
7)分别提取第二处理细胞和第二对照细胞的总蛋白，依次得到第二处理蛋白和第二对照蛋白；
8)将所述第一标签的抗体与所述第二处理蛋白进行定量或半定量抗原/抗体反应；将所述第一标签的抗体与所述第二对照蛋白进行定量或半定量抗原/抗体反应；根据第二处理组和第二对照组分别得到的定量或半定量抗原/抗体反应结果确定所述候选细胞内源蛋白是否影响细胞吸收凋亡小体。
在一个具体实施方式中，编码所述第一蛋白和编码第一标签的核苷酸连接到昆虫杆状病毒表达系统的Bacmid上。
在一个具体实施方式中，编码所述候选细胞内源蛋白的核苷酸连接到pIZT/V5-His或pIB-V5/His表达载体上；
在一个具体实施方式中，所述第一蛋白为SpliInx3蛋白。
在一个具体实施方式中，所述第一蛋白的氨基酸序列如SEQ ID No.10所示；和/或
在一个具体实施方式中，所述第一标签最好选自有相应商业化抗体的标签序列，例如其可以选自组氨酸标签(例如由六个组氨酸形成的标签)、Flag标签(其氨基酸序列为DYKDDDDK)、V5标签(其氨基酸序列为GKPIPNPLLGLDST)、HA标签(其氨基酸序列为YPYDVPDYA)中的至少一种。所述第一标签可以位于所述第一蛋白的N端，也可以位于所述第一蛋白的C端。
在一个具体实施方式中，所述第一细胞和所述第三细胞独立地选自Sf9昆虫细胞或High five昆虫细胞、BmN昆虫细胞和Spli221昆虫细胞中的一种。
在一个具体实施方式中，在步骤3)中，培养70h-75h时间得到第一处理细胞；培养70h-75h时间得到第一对照细胞；和/或在步骤6)中，培养70h-75h时间得到第二处理细胞；培养70h-75h时间得到第二对照细胞。
在一个具体实施方式中，通过提取目标生物的RNA，例如目标昆虫(例如斜纹夜蛾)的3-10日龄幼虫的RNA，然后逆转录合成cDNA；再利用能够扩增编码第一蛋白的核苷酸的上下游引物以及所述cDNA为模板进行PCR扩增，进一步将所述PCR产物克隆到表达载体(例如Bacmid，一般带有第一标签核苷酸，如果表达载体上不自在标签，也可以自行选择标签进行与第一蛋白融合表达的克隆)上；将克隆有编码第一蛋白的核苷酸的带有第一标签核苷酸的表达载体感染(或转染)第一细胞(宿主细胞)，获得能够表达第一蛋白和第一标签的第二细胞，然后使所述第二细胞形成凋亡小体。其中，使第二细胞形成凋亡小体可以为例如紫外线照射、或以脂多糖(LPS)作为药物处理等方法获得。
在一个具体实施方式中，在一定的用量下(例如Bacmid病毒与第一细胞的体积比例为1：4，其中，Bacmid病毒的MOI约为4，第一细胞在培养液中的浓度约为1×106个细胞/毫升)克隆有N端带有组氨酸标签和氨基酸酶切位点(例如能够被烟草蚀纹病毒(TobaccoEtch Virus,TEV)的半胱氨酸蛋白酶所特异识别的七肽序列Glu-Asn-Leu-Tyr-Phe-Gln-Gly)的SpliInx3基因的Bacmid病毒能使感染其的细胞形成凋亡小体。
在一个具体实施方式中，候选细胞内源蛋白的过表达，其可以与标签融合，也可以不用与标签融合。
在一个具体实施方式中，在步骤5)中，如果第一处理组得到的定量或半定量抗原/抗体反应结果大于和第一对照组得到的定量或半定量抗原/抗体反应结果，则确定所述候选细胞内源蛋白能够降低细胞吸收凋亡小体的能力。
在一个具体实施方式中，在步骤5)中，如果第一处理组得到的定量或半定量抗原/抗体反应结果小于和第一对照组得到的定量或半定量抗原/抗体反应结果，则确定所述候选细胞内源蛋白能够促进细胞吸收凋亡小体的能力。
在一个具体实施方式中，在步骤5)中，如果第一处理组得到的定量或半定量抗原/抗体反应结果与第一对照组得到的定量或半定量抗原/抗体反应结果相当，则确定所述候选细胞内源蛋白不影响细胞吸收凋亡小体的能力。
在一个具体实施方式中，在步骤8)中，如果第二处理组得到的定量或半定量抗原/抗体反应结果大于和第二对照组得到的定量或半定量抗原/抗体反应结果，则确定所述候选细胞内源蛋白能够促进细胞吸收凋亡小体的能力。
在一个具体实施方式中，在步骤8)中，如果第二处理组得到的定量或半定量抗原/抗体反应结果小于和第二对照组得到的定量或半定量抗原/抗体反应结果，则确定所述候选细胞内源蛋白能够降低细胞吸收凋亡小体的能力。
在一个具体实施方式中，在步骤8)中，如果第二处理组得到的定量或半定量抗原/抗体反应结果与第二对照组得到的定量或半定量抗原/抗体反应结果相当，则确定所述候选细胞内源蛋白不影响细胞吸收凋亡小体的能力。
在本申请中，术语“内源蛋白”意指细胞自身DNA转录翻译所表达的蛋白质。
在本申请中，术语“过表达”意指例如通过将内源性的靶标基因克隆到表达质粒载体上，然后将克隆有靶标基因的表达质粒载体转入到天然存在该内源性靶标基因的目标细胞中，从而使内源性的靶标基因的表达水平高于未转入该表达载体时的表达水平。
本申请的有益效果：
本申请首次发现了作为主要负责合成生物生命活动所需的大部分ATP的FoF1-ATPaseβ蛋白能够正向条件正常细胞吸收凋亡小体的量，即FoF1-ATPaseβ蛋白的含量与正常细胞吸收凋亡小体的量呈正相关。据此，可以通过调节FoF1-ATPaseβ蛋白的含量的方法来控制凋亡小体积累。
众所周知，对于昆虫等体型较小的动物来说，一般认为细胞凋亡在10％以下为正常现象，但是当凋亡在生物体内累积在10％以上时，则会影响其生长发育；严重时，例如凋亡在生物体内累积在20％左右时可以导致其死亡。因此，对于昆虫，特别是有害昆虫，我们希望将其种群密度控制在人类接受的范围内，因此大部分有害昆虫需要人为地采取机械、物理、化学、生物防治的方式来控制。FoF1-ATPaseβ蛋白新功能的发现，为害虫的治理提供了一条新的路径，例如可以通过FoF1-ATPaseβ的RNAi来降低FoF1-ATPaseβ蛋白，从而引发有害昆虫体内凋亡小体的积累，进而直至其死亡。
对于人或哺乳动物(例如鼠类、猪、牛、羊)，凋亡小体在生物体内累积，虽然不会引起死亡，但也会引发例如炎症或自身免疫等方面的病变，为害生物体的健康状况。因此，如果适当增加该患病生物体内的FoF1-ATPaseβ蛋白的量，则可以加快凋亡小体的清除，降低凋亡小体对生物体产生的为害。
附图说明
图1为凋亡小体吸收荧光图。由图可知细胞可以吸收凋亡小体。其中，明场为微分干涉相差(differentia interference contrast，DIC)图；荧光为在575nm的波长下的图片。
图2为FoF1-ATPaseβ抗体(简称ATPaseβ抗体)孵育后凋亡小体吸收量变化示意图。由图可知FoF1-ATPaseβ抗体孵育后凋亡小体吸收量减少。其中第一行“+”表示加入凋亡小体；第二行“+”表示加入了FoF1-ATPaseβ抗体进行孵育；“-”表示没有加入FoF1-ATPaseβ抗体孵育。
图3为FoF1-ATPaseβ过表达后凋亡小体吸收量变化示意图及结果。由图可知FoF1-ATPaseβ过表达后凋亡小体吸收量增多。其中“+”表示加入凋亡小体。
图4为不同物种FoF1-ATPaseβ的WalkerA和WalkerB保守序列比对。由图可知FoF1-ATPaseβ的WalkerA和WalkerB具有高度保守性。
图5为FoF1-ATPaseβ突变后凋亡小体吸收量变化示意图及结果。由图可知FoF1-ATPaseβ突变后凋亡小体吸收量减少。其中“+”表示加入凋亡小体。
具体实施方式
下面结合实施例对本发明作进一步说明，但本发明实施例仅为示例性的说明，该实施方式无论在任何情况下均不构成对本发明的限定。
在没有特别说明的情况下，本申请使用的试剂均可商业购买获得。
实施例1
1.FoF1-ATPaseβ的引物设计
从斜纹夜蛾转录组数据(Li M,Pang Z,Xiao W,Liu X,Zhang Y,et al.(2014)ATranscriptome Analysis Suggests Apoptosis-Related Signaling Pathways inHemocytes of Spodoptera litura After Parasitization by Microplitisbicoloratus.PLoS ONE 9(10):e110967.doi:10.1371/journal.pone.0110967)中选取FoF1-ATPaseβ基因序列，FoF1-ATPaseβ基因序列(如SEQ ID No.5所示)大小为1551bp，共编码516个氨基酸(SEQ ID No.6)。采用引物设计软件Primer Premier 5设计特异引物。上游引物FoF1-ATPaseβ-F(SEQ ID No.7)和下游引物FoF1-ATPaseβ-R(SEQ ID No.8)。
2.斜纹夜蛾幼虫总RNA的提取及cDNA的合成
本实验采用实验室方案提取斜纹夜蛾幼虫总RNA，具体步骤如下：
1)取10头3日龄幼虫，放置于加入少量RNAisoTM Plus裂解液的EP管中，充分捣碎研磨，继续加入RNAisoTM Plus裂解液至总体积达到1ml，涡旋混匀后，室温静置6min；
2)将上述处理好的样品，12000rpm，4℃离心5min；
3)取上清，转移至新的EP管中，加入氯仿200μL，剧烈振荡10-15s，充分混匀后，室温静置5min；
4)12000rpm，4℃离心15min；离心后的溶液分为三层：无色的上清液、中间的白色蛋白层及带有颜色的下层有机相,吸取上清液转移至另一新的离心管中；
5)向上清中加入等体积的异丙醇，混匀后室温静置10min；12000rpm，4℃离心10min；轻轻弃去上清，缓慢地沿离心管壁加入75％的乙醇1ml(0.1％DEPC水配制)；12000rpm，4℃离心5min；
6)弃去乙醇，室温干燥5min，加入50μL的RNase-free H2O溶解沉淀，标记好后，-80℃保存，取5μL马上进行琼脂糖凝胶电泳检测。
本实验用PrimeScriptTM RT reagent Kit反转录试剂盒(货号6210A)来反转录，具体步骤如下：
1)在离心管(EP管)中配置下列反应混合液(10μL)
Oligo dT引物1μL；dNTP混合物1μL；模板RNA 8μL；65℃，5min，冰上骤冷。
2)在上述EP管中加入下列反转录反应液：
5×PrimeScrip缓冲液4μL；PrimeScrip逆转录酶(200U/μL)4μL；核糖核酸酶抑制因子(40U/μL)2μL；总体积15μL，45℃保温45min。然后，95℃反应5min，冰上骤冷；-80℃保存。
3.FoF1-ATPaseβ基因片段的克隆
1)以上述所得的cDNA为模板，用FoF1-ATPaseβ的特异引物FoF1-ATPaseβ-F(SEQ IDNo.7)和FoF1-ATPaseβ-R(SEQ ID No.8)进行PCR扩增。
扩增体系：10×Ex Taq缓冲液1.25μL；dNTP混合物5μL；上游引物0.5μL；下游引物0.5μL；cDNA 1.0μL；Ex Taq聚合酶0.125μL；dd H2O至15μL总体积：15μL
2)PCR程序：94℃5min；94℃30s，55℃30s，72℃1min 30s，30个循环；72℃10min；10℃保存。
3)将上述PCR产物进行电泳，回收1563bp的PCR产物，并连接到克隆载体pMD19-T载体(Takara提供)上，经测序确定正确，得到含有靶标片段的pMD19-ATPaseβ质粒。
4.pIZT-ATPaseβ的连接
1)将pMD19-ATPaseβ质粒和pIZT/V5-His质粒分别用EcoR I和Not I进行双酶切。取测序成功的pMD19-ATPaseβ菌液，加入氨苄青霉素过夜培养，用普通质粒提取试剂盒提取质粒，根据设计的相应酶切位点对质粒进行双酶切(EcoR I/Not I)，用同样的限制性内切酶对pIZT/V5-His载体(Thermo fisher提供，包含6个组氨酸的编码序列)进行双酶切。将FoF1-ATPaseβ基因片段和pIZT/V5-His载体片段进行回收，T4连接酶连接。经测序确定正确，得到含有靶标片段的pIZT-ATPaseβ质粒。通过该质粒，6个组氨酸(6×His)标签的编码序列与FoF1-ATPaseβ基因可以融合表达。
5.SpliInx3的引物的设计
从斜纹夜蛾转录组数据(Li M,Pang Z,Xiao W,Liu X,Zhang Y,et al.(2014)ATranscriptome Analysis Suggests Apoptosis-Related Signaling Pathways inHemocytes of Spodoptera litura After Parasitization by Microplitisbicoloratus.PLoS ONE 9(10):e110967.doi:10.1371/journal.pone.0110967)中选取SpliInx3基因序列，SpliInx3基因序列(如SEQ ID No.9所示)大小为1161bp，共编码386个氨基酸(SEQ ID No.10)。采用引物设计软件Primer Premier 5设计特异引物。上游引物Inx3-F(SEQ ID No.11)和下游引物Inx3-R(SEQ ID No.12)。
6.Inx3基因片段的克隆
1)以上述第2小节所得的cDNA为模板，用SpliInx3特异引物Inx3-F(SEQ IDNo.11)和Inx3-R(SEQ ID No.12)进行PCR扩增。
扩增体系：10×Ex Taq缓冲液1.25μL；dNTP混合物5μL；上游引物0.5μL；下游引物0.5μL；cDNA 1.0μL；Ex Taq聚合酶0.125μL；dd H2O至15μL总体积：15μL。
2)PCR程序：94℃5min；94℃30s，55℃30s，72℃1min，30个循环；72℃10min；10℃保存。
3)将上述PCR产物进行电泳，回收1161bp的PCR产物，并连接到克隆载体pMD19-T载体(Takara提供)上，经测序确定正确，得到含有靶标片段的pMD19-Inx3质粒。
7.pFastBacHTA-Inx3质粒构建以及转座
1)pFastBacHTA-Inx3的获取
对于取测序成功的pMD19-Inx3菌液，加氨苄青霉素过夜培养，用普通质粒提取试剂盒提取质粒，根据设计的相应酶切位点对质粒进行双酶切(EcoR I/Not I)，用同样的限制性内切酶对pFastBacHTA载体(Thermo fisher提供)进行双酶切。将Inx3基因片段和pFastBacHTA载体片段进行回收，T4连接酶连接。经测序确定正确，得到含有靶标片段的pFastBacHTA-Inx3质粒。
2)转座
将pFastBacHTA-Inx3质粒转化到带有Bacmid(Thermo fisher提供)和helper质粒(Thermo fisher提供)的大肠杆菌DH10Bac(Thermo fisher提供)中进行转座，得到质粒Bacmid-Inx3。分别用引物M13-F(SEQ ID No.13)与M13-R(SEQ ID No.14)、引物M13-F(SEQID No.13)与Inx3-R(SEQ ID No.12)、引物Inx3-F(SEQ ID No.11)与M13-R(SEQ IDNo.14)、以及引物Inx3-F(SEQ ID No.11)与Inx3-R(SEQ ID No.12)对重组质粒Bacmid-Inx3进行鉴定，PCR产物片段大小与预期符合，分别为3500bp、2800bp、1700bp和1161bp。
8.重组杆状病毒的制备
1)P1代病毒的获取
将Bacmid-Inx3质粒采用脂质体转染法转染Sf9细胞(每孔8×105个细胞)，细胞出现裂解后(大概72h后)500g，5min离心取上清即为P1代病毒。
2)P2代病毒的获取
①向25cm的细胞培养瓶中加入5ml Sf9细胞悬浮液(约1×106个细胞/ml)，贴壁培养30min；
②向培养瓶中加入5％(即250μl)的P1代病毒上清进行细胞感染；
③每隔24h对细胞进行计数，持续至72h止；
④细胞数量应该在24h时增加一倍(约2×106个细胞/ml))，然后停止分裂；
a.如果细胞在24h时未增加一倍，则P2病毒使用过多，应减少P2代病毒的使用量至0.05％来感染细胞；
b.如果细胞在48h时未停止分裂，则P2病毒使用过少，应增加P2代病毒的使用量至10％来感染细胞；
⑤持续培养72h后低速500g，5min，离心收集上清液，上清液即为P2代病毒，避光4℃保存。
3)P3代病毒的获取
①向25cm2的细胞培养瓶中加入5ml Sf9细胞悬浮液(约1×106个细胞/ml)，贴壁培养30min；
②向培养瓶中加入0.1％(即5μl)的P2代病毒上清进行细胞感染；
③每隔24h对细胞进行计数，持续至72h止；
④细胞数量应该在24h时增加一倍(约2×106个细胞/ml)，然后停止分裂；
a.如果细胞在24h时未增加一倍，则P2病毒使用过多，应减少P2代病毒的使用量至0.05％来感染细胞
b.如果细胞在48h时未停止分裂，则P2病毒使用过少，应增加P2代病毒的使用量至0.5％来感染细胞
⑤持续培养72h后低速500g，离心5min，收集上清液，上清液即为P3代病毒，P3代病毒可直接用于蛋白的制备。避光4℃保存；
9.凋亡小体的制备
向6孔板以20％的量加入P3代病毒(每孔2×105Sf9细胞)，在活细胞工作站观察到细胞会逐渐凋亡形成凋亡小体。72h后，500g，离心5min，收集上清液；再3000g，离心20min，去除上清；用PBS 3000g，离心20min，洗2遍，底部沉淀即为凋亡小体。
10.凋亡小体吸收处理
设置处理组和对照组。分别向处理组和对照组的6孔板每孔加入2×106个Highfive细胞，其中处理组加入10μl FoF1-ATPaseβ的抗体(将SEQ ID No.6所示的氨基序列送至贝尔生化(上海)有限公司制备其多克隆抗体)进行孵育；不做处理的作为对照组。24h后处理组和对照组都加入用5μl Annexin V-PE(碧云天Annexin V-PE细胞凋亡检测试剂盒C1065)染色的凋亡小体(4×105个Sf9细胞形成的凋亡小体)。72h后用荧光显微镜拍照如图1，细胞表面有红色荧光说明凋亡小体被High five细胞吸收。但是荧光呈块状聚集，一方面无法统计吸收凋亡小体的High five细胞的数量，另一方面也无法统计单个High five细胞能够吸收凋亡小体的数量。即无法用荧光强度进行定量或半定量的差异性分析。
11.凋亡小体吸收量检测
1)总蛋白的提取
第一组：设置处理组和对照组。向处理组和对照组的6孔板每孔加入1×106个Highfive细胞，处理组加入10μl FoF1-ATPaseβ的抗体进行孵育；不做处理的作为对照组。24h后处理组和对照组都加入等量凋亡小体(4×105Sf9细胞形成的凋亡小体)。
第二组：设置处理组和对照组。向处理组和对照组的6孔板每孔加入1×106个Highfive细胞，对照组转染pIZT/V5-His质粒，处理组转染pIZT-ATPaseβ。72h后处理组和对照组都换新的培养基并加入等量凋亡小体(4×105Sf9细胞形成的凋亡小体)。
72h后两组实验分别进行如下操作：弃培养基，用PBS洗2次每次5min，收集Highfive细胞蛋白。具体如下：①加入1×PBS 1ml，6000r/min，4℃离心5min，去上清。②加入50-80μl RIPA混合液(RIPA：PMSF＝100：1)，13000r/min，4℃离心10min③用BCA法测蛋白浓度④计算需要样品蛋白、SDS以及水的量⑤按计算的量将蛋白、SDS以及水加入到新的200μlEP管中，涡旋，离心⑥将上述蛋白混合液92℃煮10min⑦将煮好的蛋白冷却后离心放入-80℃备用。
2)Western bolt的检测
①清洗玻璃板并擦干组装为制胶器。
②按照SDS-PAGE凝胶配方配制分离胶，
A.分离胶配置体系(15ml)
B.浓缩胶配置体系(8ml)
③每个胶板灌入7ml分离胶，再加入1ml无水乙醇隔绝空气并压平分离胶。待分离胶凝结后(大约20min)倒掉无水乙醇，倾斜制胶器用滤纸吸干参与的无水乙醇。加入2.5ml的浓缩胶，快速插入梳子，等待浓缩胶凝结(大约15min)。
④将胶板放入电泳槽中，加入电泳缓冲液，拔去梳子，蛋白上样。
⑤先用80V进行电泳，待蛋白样品压成一条线时，改用100V电压，继续电泳至蛋白样品距离分离胶的下边缘1cm左右停止电泳。
⑥取与蛋白样品所在的分离胶同样大小的PVDF膜，在甲醛中浸湿1min。用转膜缓冲液浸湿海绵和滤纸，按照夹板负极面，海绵，滤纸，胶，PVDF膜，滤纸，海绵，夹板正极面的顺序夹起夹板，按正负极放入转膜槽中，加入转膜缓冲液。将电泳槽放入冰水中，以100V的恒压电泳90min。
⑦转膜结束后，取出PVDF膜，放入5％脱脂奶粉的TBST缓冲液中室温封闭1h。封闭结束后，倒掉5％脱脂奶粉的TBST缓冲液，用PBST洗膜3次，每次5min，弃去PBST。
⑧向5％脱脂奶粉的TBST缓冲液中加入组氨酸标签(6×His)抗体(购自北京索爱宝科技有限公司，鼠抗)在4℃下孵育膜8-10小时，其中，6×His抗体与5％脱脂奶粉的TBST缓冲液的体积比为1:2000。
⑨移除含有6×His抗体的5％脱脂奶粉的TBST缓冲液然后用PBST洗膜3次，每次5min，弃去PBST。
⑩向5％脱脂奶粉的TBST缓冲液中加入辣根过氧化物酶(HRP)标记山羊抗小鼠IgG(H+L)(二抗，购自上海碧云天生物技术有限公司，二抗与5％脱脂奶粉的TBST缓冲液的体积比为1:5000)，室温孵育1h。孵育结束后，弃去含有二抗的5％脱脂奶粉的TBST缓冲液，用PBST洗膜3次，每次5min，弃去PBST。
将PVDF膜放到Tanon5200化学发光仪的发光板上，在膜上均匀滴加0.2ml的Luminata Forte Western HRP Substrate，用软件GelCap曝光成像。用PBST洗膜3次，每次10min，弃去PBST。
向5％脱脂奶粉的TBST缓冲液中加入内参蛋白的抗体(购自北京索爱宝科技有限公司，鼠抗)在4℃下孵育膜8-10小时，其中，内参蛋白的抗体与5％脱脂奶粉的TBST缓冲液的体积比为1:2000，重复步骤⑨-。
3)显著性差异分析
凋亡小体吸收量的Western bolt结果用GraphPad Prism 6进行分析。
4)结果
图2为该小节1)中第一组的Western bolt结果，其使用的内参蛋白为微管蛋白(tubulin)。由图2可知FoF1-ATPaseβ抗体孵育后细胞对凋亡小体的吸收明显减少，说明FoF1-ATPaseβ蛋白在细胞表面的量降低导致细胞吸收凋亡小体的能力下降。
图3为该小节1)中第二组的Western bolt结果，其使用的内参蛋白为甘油醛-3-磷酸脱氢酶(GAPDH)。由图3可知FoF1-ATPaseβ过表达后细胞对凋亡小体的吸收明显增加，说明FoF1-ATPaseβ蛋白在细胞的量的增加促进了细胞吸收凋亡小体的能力。通过正反两个方面的实验可以得出结论：FoF1-ATPaseβ蛋白与细胞吸收凋亡小体的能力成正相关。据此，如果需要降低细胞吸收凋亡小体的能力，则可以降低FoF1-ATPaseβ蛋白的表达量；如果需要增加细胞吸收凋亡小体的能力，则可以增加FoF1-ATPaseβ蛋白的表达量。
实施例2
酿酒酵母(Saccharomyces cerevisiae)FoF1-ATPaseβ的genebank登录号为AAA34444.1、秀丽隐杆线虫(Caenorhabditis elegans)FoF1-ATPaseβ的genebank登录号为P46561.2、黑腹果蝇(Drosophila melanogaster)FoF1-ATPaseβ的genebank登录号为CAA50332.1、斜纹夜蛾(Spodoptera litura)FoF1-ATPaseβ的genebank登录号为AFY62978.1、非洲爪蟾(Xenopus laevis)FoF1-ATPaseβ的genebank登录号为NP_001080126.1、智人(Homo sapiens)FoF1-ATPaseβ的genebank登录号为NP_001677.2。对从低等到高等各种代表性物种FoF1-AT Paseβ的氨基酸序列进行Walk A模序和Walk B模序的序列比对，见图4。由图4可知，FoF1-ATPaseβ的WalkerA和WalkerB在各个物种都有极高的保守性。
实施例3
仅将pIZT-ATPaseβ替换为pIZT-ATPaseβ(K202-A)，pIZT-ATPaseβ(K202-A)与pIZT-ATPaseβ的不同在于表达出来FoF1-ATPaseβ的202位氨基酸由原来的赖氨酸(K)突变为丙氨酸(A)，即将Walker A模序中的保守氨基酸赖氨酸(K)突变为丙氨酸(A)。
总蛋白的提取、Western bolt的检测、显著性差异分析的操作方法同实施例1。在本实施例中以甘油醛-3-磷酸脱氢酶为内参。
结果见图5。由图5可知突变后质粒pIZT-ATPaseβ(K202-A)过表达的细胞与pIZT-ATPaseβ质粒过表达的细胞相比，对凋亡小体的吸收明显减少，说明FoF1-ATPaseβ中至少Walker A的赖氨酸(K)在凋亡小体吸收过程中有重要作用。
虽然本申请已经参照具体实施方式进行了描述，但是本领域的技术人员应该理解在没有脱离本申请的真正的精神和范围的情况下，可以进行的各种改变。此外，可以对本申请的主体、精神和范围进行多种改变以适应特定的情形、材料、材料组合物和方法。所有的这些改变均包括在本申请的权利要求的范围内。
序列表
<110> 云南大学
<120> FoF1-ATPase β蛋白在促进或降低细胞吸收凋亡小体中的应用
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Claims (10)
1.FoF1-ATPaseβ蛋白在促进或降低细胞吸收凋亡小体中的应用，其中，所述FoF1-ATPaseβ蛋白的氨基酸序列中含有Walk A模序和Walk B模序。
2.根据权利要求1所述的应用，其特征在于，所述Walk A模序为如SEQ ID No.1或SEQID No.2所示的氨基酸序列，所述Walk B模序为如Arg Xaa Xaa Xaa Gly Xaa Xaa Xaa LeuJaa Jaa Jaa Asp所示的氨基酸序列或如Lys Xaa Xaa Xaa Gly Xaa Xaa Xaa Leu JaaJaa Jaa Asp所示的氨基酸序列；其中如SEQ ID No.1所示的氨基酸序列、SEQ ID No.2所示的氨基酸序列、如Arg Xaa Xaa Xaa Gly Xaa Xaa Xaa Leu Jaa Jaa Jaa Asp所示的氨基酸序列或如Lys Xaa Xaa Xaa Gly Xaa Xaa Xaa Leu Jaa Jaa Jaa Asp所示的氨基酸序列中的Xaa独立地为甘氨酸、丙氨酸、缬氨酸、亮氨酸、异亮氨酸、苯丙氨酸、脯氨酸、色氨酸、丝氨酸、酪氨酸、半胱氨酸、蛋氨酸、天冬酰胺、谷氨酰胺、苏氨酸、天冬氨酸、谷氨酸、赖氨酸、精氨酸和组氨酸中的任意一种氨基酸，如Arg Xaa Xaa Xaa Gly Xaa Xaa Xaa Leu JaaJaa Jaa Asp的氨基酸序列或如Lys Xaa Xaa Xaa Gly Xaa Xaa Xaa Leu Jaa Jaa JaaAsp所示的氨基酸序列中的Jaa独立地为疏水性氨基酸。
3.根据权利要求2所述的应用，其特征在于，所述Walk A模序为如SEQ ID No.3所示的氨基酸序列，所述Walk B模序为如SEQ ID No.4所示的氨基酸序列。
4.根据权利要求1-3中任意一项所述的应用，其特征在于，所述FoF1-ATPaseβ蛋白的氨基酸序列为来源于昆虫纲中的任意一种昆虫的FoF1-ATPaseβ蛋白；优选所述FoF1-ATPaseβ蛋白的氨基酸序列为来源于鳞翅目中的任意一种昆虫的FoF1-ATPaseβ蛋白。
5.根据权利要求1所述的应用，其特征在于，所述FoF1-ATPaseβ蛋白的氨基酸序列如SEQID No.6所示。
6.如权利要求1至5中任意一项所述的应用中的所述FoF1-ATPaseβ蛋白在用于控制害虫中的应用，优选所述害虫为昆虫纲中的任意一种昆虫；更优选所述害虫为来源于鳞翅目中的任意一种昆虫；或如权利要求1或2所述的应用中的所述FoF1-ATPaseβ蛋白在制备用于控制动物或人由于凋亡小体积累引起的炎症和/或自身免疫疾病的药物中的应用。
7.一种鉴定候选细胞内源蛋白是否影响细胞吸收凋亡小体的方法，所述方法选自下列方案之一：
方案一：步骤1)、步骤3)、步骤4)和步骤5)；
方案二：步骤1)、步骤2)、步骤6)、步骤7)和步骤8)；
方案三：步骤1)、步骤2)、步骤3)、步骤4)、步骤5)、步骤6)、步骤7)和步骤8)；
其中，
1)将定位于细胞表面的第一蛋白与第一标签在第一细胞中融合表达，得到表达有所述第一蛋白与所述第一标签的融合产物的第二细胞；并且所述第一蛋白与所述第一标签在所述第一细胞中融合表达后，使所述第二细胞形成凋亡小体；其中，所述第一标签为所述第一细胞中不能内源表达的蛋白质或多肽；
2)将所述候选细胞内源蛋白在第三细胞中过表达，得到过表达所述候选细胞内源蛋白的第四细胞；
3)对于第一处理组：在用所述候选细胞内源蛋白的抗体处理所述第三细胞后，与步骤1)中形成的凋亡小体混合后进行培养，得到第一处理细胞；
对于第一对照组：将步骤1)中形成的凋亡小体与所述第三细胞混合后进行培养，得到第一对照细胞；
4)分别提取第一处理细胞和第一对照细胞的总蛋白，依次得到第一处理蛋白和第一对照蛋白；
5)将所述第一标签的抗体与所述第一处理蛋白进行定量或半定量抗原/抗体反应；将所述第一标签的抗体与所述第一对照蛋白进行定量或半定量抗原/抗体反应；根据第一处理组和第一对照组分别得到的定量或半定量抗原/抗体反应结果确定所述候选细胞内源蛋白是否影响细胞吸收凋亡小体；
6)对于第二处理组：将步骤1)中形成的凋亡小体与步骤2)中的第四细胞混合后进行培养，得到第二处理细胞；
对于第二对照组：将步骤1)中形成的凋亡小体与第五细胞与混合后进行培养，得到第二对照细胞；其中所述第五细胞与所述第四细胞的不同之处仅在于，所述第五细胞中不含有外加的编码所述候选细胞内源蛋白的DNA或RNA，也不含有外加的所述候选细胞内源蛋白；
7)分别提取第二处理细胞和第二对照细胞的总蛋白，依次得到第二处理蛋白和第二对照蛋白；
8)将所述第一标签的抗体与所述第二处理蛋白进行定量或半定量抗原/抗体反应；将所述第一标签的抗体与所述第二对照蛋白进行定量或半定量抗原/抗体反应；根据第二处理组和第二对照组分别得到的定量或半定量抗原/抗体反应结果确定所述候选细胞内源蛋白是否影响细胞吸收凋亡小体。
8.根据权利要求7所述的方法，其特征在于，编码所述第一蛋白和编码第一标签的核苷酸连接到昆虫杆状病毒表达系统的Bacmid上；和/或编码所述候选细胞内源蛋白的核苷酸连接到pIZT/V5-His或pIB-V5/His表达载体上；
优选地，所述第一蛋白为SpliInx3蛋白，优选所述第一蛋白的氨基酸序列如SEQ IDNo.10所示；和/或优选地，所述第一标签选自组氨酸标签、Flag标签、V5标签、HA标签中的至少一种。
9.根据权利要求7或8所述的方法，其特征在于，所述第一细胞和所述第三细胞独立地选自Sf9昆虫细胞、High five昆虫细胞、BmN昆虫细胞和Spli221昆虫细胞中的一种。
10.根据权利要求7或8所述的方法，其特征在于，在步骤3)中，培养70h-75h时间得到第一处理细胞；培养70h-75h时间得到第一对照细胞；和/或
在步骤6)中，培养70h-75h时间得到第二处理细胞；培养70h-75h时间得到第二对照细胞。
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| CN114231551A (zh) * | 2021-12-24 | 2022-03-25 | 云南大学 | 蛋白在促进昆虫淋巴细胞凋亡和/或防治害虫中的应用 |
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| CN114231551A (zh) * | 2021-12-24 | 2022-03-25 | 云南大学 | 蛋白在促进昆虫淋巴细胞凋亡和/或防治害虫中的应用 |
| CN114231551B (zh) * | 2021-12-24 | 2023-09-29 | 云南大学 | 蛋白在促进昆虫淋巴细胞凋亡和/或防治害虫中的应用 |
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