CN114989296B - 一种狂犬病毒的单克隆抗体2f2及通用型狂犬病毒抗体快速检测试纸 - Google Patents
一种狂犬病毒的单克隆抗体2f2及通用型狂犬病毒抗体快速检测试纸 Download PDFInfo
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Abstract
本发明提供了一种狂犬病毒的单克隆抗体2F2及通用型狂犬病毒抗体快速检测试纸,属于生物检测技术领域,所述单克隆抗体2F2的氨基酸序列如SEQ ID No.1所示。本发明提供的单克隆抗体2F2特异性结合狂犬病毒G蛋白,将单克隆抗体2F2制备成试纸条具有快速、准确、灵敏、特异和低成本优点。
Description
技术领域
本发明属于生物检测技术领域,尤其涉及一种狂犬病毒的单克隆抗体2F2及通用型狂犬病毒抗体快速检测试纸。
背景技术
狂犬病是人畜共患传染病,病死率接近100%。狂犬病病毒(Rabies virus,RV)属于弹状病毒科,与拉各斯蝙蝠病毒、Mokola病毒、Duvenhage病毒、欧洲蝙蝠狂犬病病毒1型、欧洲蝙蝠狂犬病病毒2型和澳大利亚蝙蝠狂犬病病毒同属于狂犬病毒属。RV为单股负链RNA病毒,一端圆凸;一端平凹,形如子弹,直径65~80nm,长约130~240nm。RV容易为日光、紫外线、甲醛、升汞季胺类化合物(如新洁尔灭)、脂溶剂、75%酒精等灭活,其悬液经56℃灭活30~60分钟或100℃灭活2分钟,病毒即可灭活。病毒于-70℃或冻干后置0~4℃中可保持活力数年。被感染的组织可保存于50%甘油内送验。RV主要包含5种蛋白,即糖蛋白(G)、核蛋白(N)、双聚酶(L)、磷蛋白(NS)及基质(M)。糖蛋白G为主要的保护性抗原,可诱导机体产生中和抗体,对抗病毒攻击。
预防狂犬病可以通过规范的暴露前和暴露后处置来实现,接种狂犬病疫苗是重要的处置手段,疫苗免疫后测定血清内的狂犬病病毒中和抗体滴度水平可以评价疫苗接种是否达到保护性水平。世界卫生组织推荐的检测狂犬病病毒中和抗体(Rabies virusneutralizing antibody,RVNA)的标准方法有快速荧光灶抑制试验(Rapid fluorescentfocus inhibition test,RFFIT)和小鼠脑内中和试验(Mouse neutralization test,MNT)。由于MNT需要使用动物,且操作繁琐、耗时长;RFFIT需要使用狂犬病固定毒株CVS-11,涉及活毒操作等原因,使这两种方法的普及使用受到了限制。
发明内容
有鉴于此,本发明的目的在于提供一种狂犬病毒的单克隆抗体2F2及通用型狂犬病毒抗体快速检测试纸,本发明提供的单克隆抗体2F2特异性结合狂犬病毒G蛋白,将单克隆抗体2F2制备成试纸条具有快速、准确、灵敏、特异和低成本优点。
为了实现上述发明目的,本发明提供了以下技术方案:
本发明提供了一种识别狂犬病毒G蛋白的单克隆抗体2F2,所述单克隆抗体2F2的氨基酸序列如SEQ ID No.1所示。
本发明还提供了上述技术方案所述的单克隆抗体2F2在制备检测狂犬病毒试剂中的应用。
本发明还提供了一种通用型狂犬病毒抗体快速检测试纸,包括:在支撑板上依次搭接样品垫、结合垫、检测膜和吸水垫,所述检测膜上喷涂检测线和质控线;
所述质控线上喷涂有权利要求1所述的单克隆抗体2F2。
优选的,所述单克隆抗体2F2以单克隆抗体2F2溶液形式进行喷涂,所述单克隆抗体2F2溶液的浓度为0.5mg/mL。
优选的,所述单克隆抗体2F2溶液以1μL/cm喷涂。
优选的,所述检测线上喷涂有SPA,所述SPA以SPA溶液形式进行喷涂,所述SPA溶液的浓度为0.5mg/mL;
所述SPA溶液以1μL/cm喷涂。
优选的,所述结合垫上喷涂有胶体金标记的狂犬病毒G蛋白。
优选的,所述狂犬病毒G蛋白以狂犬病毒G蛋白溶液形式进行喷涂,所述狂犬病毒G蛋白溶液的浓度为1mg/ml;
所述狂犬病毒G蛋白溶液以15μL/cm喷涂。
优选的,所述质控线与检测线的间距为0.5cm。
优选的,所述搭接的重叠距离为1~2mm。
本发明将单克隆抗体2F2制备成试纸条,试纸条的检测原理是:
狂犬病毒抗体的免疫层析检测试纸应用RV G重组蛋白及其单克隆抗体,根据现代免疫学技术和层析技术设计组装,待测血清样品在层析过程中,样品中的待检抗体与结合垫上的金标G重组蛋白结合,然后分别被检测线(T线)上的SPA捕获,多余的金标G重组蛋白与质控线(C线)上的2F2单抗捕获,从而出现两条线。
本发明提供的试纸检测狂犬病毒阳性血清的检测限可达1:12800;特异性检测结果显示该试纸与其它同属病毒阳性血清均不发生交叉反应。
附图说明
图1为慢病毒包装;
图2为稳定表达狂犬病毒G蛋白的CHO细胞系;
图3为纯化后的RV G重组蛋白;
图4为IFA结果;
图5为纯化单抗结果;
图6为狂犬病毒抗体的免疫层析快速检测试纸示意图;
图7为狂犬病毒抗体的免疫层析快速检测试纸检测限;1,1:400;2,1:800;;3,1:1600;4,1:3200;5,1:6400;6,1:12800;7,1:25600;8,1:51200;9,1:102400;N:PBS;
图8为狂犬病毒抗体的免疫层析快速检测试纸特异性;1:狂犬病病毒;2:拉各斯蝙蝠病毒;3:Mokola病毒;4:Duvenhage病毒;5:欧洲蝙蝠狂犬病病毒1型;6:欧洲蝙蝠狂犬病病毒2型;7:澳大利亚蝙蝠狂犬病病毒。
具体实施方式
本发明提供了一种识别狂犬病毒G蛋白的单克隆抗体2F2,所述单克隆抗体2F2的氨基酸序列如SEQ ID No.1所示,具体如下:
EAQSGAGLVASPQSVKLTCTATGFNITKDYHWVWIRQFPGEQLEWMGWIDSESGDISYNPSLKFQISITADTSWNTAFLDLNSVTSEDTAVYYCNAVSLGDQASISCRSSQSLLHSDGNTYLDWYLQKPGQSPKLLIYTSSFHR FSGVPDRFSGSGSGTDFTLKISRVEAEDLGIYFCSQSTLLPPTFGGGTKLEIKRI。加粗部分为重链可变区,下划线部分为轻链可变区。
本发明还提供了上述技术方案所述的单克隆抗体2F2在制备检测狂犬病毒试剂中的应用。本发明对将单克隆抗体2F2制备成试剂的种类没有特殊限定,本领域技术人员按照单克隆抗体2F2常规制备即可。
本发明还提供了一种通用型狂犬病毒抗体快速检测试纸,包括:在支撑板上依次搭接样品垫、结合垫、检测膜和吸水垫,所述检测膜上喷涂检测线和质控线;
所述质控线上喷涂有上述技术方案所述的单克隆抗体2F2。
在本发明中,所述单克隆抗体2F2优选以单克隆抗体2F2溶液形式进行喷涂,所述单克隆抗体2F2溶液的浓度优选为0.5mg/mL。在本发明中,所述单克隆抗体2F2溶液优选以1μL/cm喷涂。本发明优选使用PBS缓冲液制备单克隆抗体2F2溶液。
在本发明中,所述检测线上优选喷涂有SPA,所述SPA优选以SPA溶液形式进行喷涂,所述SPA溶液的浓度优选为0.5mg/mL。在本发明中,所述SPA溶液优选以1μL/cm喷涂。本发明优选使用PBS缓冲液制备SPA溶液。
在本发明中,所述结合垫上优选喷涂有胶体金标记的狂犬病毒G蛋白。本发明对胶体金标记狂犬病毒G蛋白的方法没有特殊限定,本领域技术人员依据常规技术操作即可。在本发明中,所述狂犬病毒G蛋白优选以狂犬病毒G蛋白溶液形式进行喷涂,所述狂犬病毒G蛋白溶液的浓度优选为1mg/ml;所述狂犬病毒G蛋白溶液优选以15μL/cm喷涂。在本发明中,所述质控线与检测线的间距优选为0.5cm。在本发明中,所述搭接的重叠距离优选为1~2mm。
下面结合实施例对本发明提供的技术方案进行详细的说明,但是不能把它们理解为对本发明保护范围的限定。
实施例1
RV G重组蛋白的表达及纯化
1、目的基因的合成
参考GenBank上发表的rabies virus毒株G-protein的序列信息(GenBank:E02022.1),优化成CHO偏爱的密码子后,由上海生物工程有限公司合成RV G蛋白的基因序列,并加入6×His标签基因序列,克隆到pLVX-IRES-ZsGreen1慢病毒载体中,构建真核重组表达pLVX-G-IRES-ZsGreen1,简称pLVX-G。包装慢病毒(如图1所示),转导CHO细胞并筛选CHO/G阳性细胞(如图2所示)。
2、G蛋白的表达及鉴定
(1)细胞的大量培养:将CHO/G细胞接种到50mL的摇瓶中,120rpm培养,通过细胞计数检测细胞的生长密度。当细胞培养密度保持不变时,将50mL摇瓶中的细胞扩大到500mL摇瓶中进行高密度培养,每天进行细胞计数,当细胞密度大于初始密度的1.5倍时开始加入SMS CHO-SUPI培养基添加液,按1.5%的量加入,每天加入,当细胞密度保持不变,或者细胞的死亡率开始升高时,停止加入SMS CHO-SUPI培养基添加液,收集细胞悬液,离心收取上清液体;
(2)取100μL上述细胞上清加入25μL 5×Loading buffer制备蛋白电泳样品,进行SDS-PAGE分析,检测RV G重组蛋白表达情况。SDS-PAGE结果显示:RV G重组蛋白在65KD有目的条带,说明RV G重组蛋白为可溶性表达。
(3)又将收集的细胞上清进行Western blot鉴定,具体步骤如下所示:将SDS-PAGE后的凝胶在转膜仪中15V电转至硝酸纤维素膜(NC膜)上;转印的NC膜用含5%脱脂奶粉的PBST封闭,4℃封闭过夜;一抗为His单抗,1:5000稀释后室温孵育1h;二抗为HRP标记的羊抗鼠IgG,1:5000稀释后室温孵育1h;避光条件下加入AEC显色液,观察显色结果。Westernblot结果显示RV G重组蛋白在65KD有条带,与预期结果一致。
3、RV G重组蛋白的纯化
由于RV G重组蛋白带有6×His标签,所以采用镍柱分别对其进行纯化。使用0.45μm滤器将培养上清过滤后,采用镍柱亲和层析法进行蛋白纯化,具体纯化步骤如下所示:
(1)用移液器分别吸取2mL镍柱填料加入安装好的蛋白纯化柱上,待填料沉降后,小心加入上垫片;打开控制阀,使20%乙醇流出,并继续用10mL去离子水清洗柱子;
(2)调节蛋白纯化装置的控制阀使其流速稳定,流速调节完毕后用10mL及以上体积的含20mM咪唑的平衡缓冲液(20mM磷酸盐缓冲液,PH 7.4,0.5M NaCL)以1mL/min的速度冲洗柱子;
(3)将滤膜过滤的超声后上清分批次滴加到上述平衡好的柱子中,每次5mL,调节控制阀使流速不超过1mL/min,迅速收集穿出液并重复上样2~3次,收集最后一次穿出液,放置-20℃备用;
(4)RV G重组蛋白的纯化是用含200mM咪唑的洗涤缓冲液(20mM磷酸盐缓冲液,PH7.4,0.5M NaCL)冲洗柱子,除去杂蛋白;
(5)最后向柱子中加入10mL含500mM咪唑的洗脱缓冲液,洗脱目的蛋白;调节控制阀,尽量降低液体流穿的速度;将洗脱的液体收集到1.5mL的EP管中,每管1mL,用酶标仪测出每管蛋白的浓度并做好标记,放置-20℃备用;
(6)纯化结束后,用20mL的ddw清洗镍柱,然后用NaOH溶液(1mol/L)再清洗一次柱子,用ddw又一次清洗镍柱,最后将镍柱存放在20%的乙醇中,4℃冰箱储存;
(7)向纯化后收集的洗脱液中加入5×Loading Buffer,并煮沸10min,经12%SDS-PAGE分析纯化结果;
(8)SDS-PAGE结果显示纯化后的RV G重组蛋白目的条带在65KD处,与预期结果一致,且能达到90%以上的纯度(如图3所示);
(9)用BCA法测定RV G重组蛋白的浓度分别为1.3mg/mL;将纯化后的蛋白分装后置于-80℃冰箱保存备用。
G蛋白核苷酸序列(SEQ ID No.2)具体如下:
ATGATCCCTCAGGTGCTGCTGTTTGTGCCTCTGCTGGTGTTCTCTTCTTGTTTTGGAAAGTTTCCTATCTACACCATCCCTGATAAGCTGGGCCCTTGGTCTCCTATCGATATCCACCACCTGAGCTGTCCTAACAACCTGGTGGTGGAGGATGAGGGCTGTACCAACCTGTCTGGCTTTTCTTACATGGAGCTGAAGGTGGGCTACATCTCCGCCATCAAGGTGAATGGCTTCACATGCACCGGCGTGGTGACAGAGGCCGAGACATACACCAACTTTGTGGGATACGTGACCACAACCTTCAAGAGGAAGCACTTTAGACCTATGCCTGATGCCTGTAGAGCCGCTTACAACTGGAAGATGGCCGGCGACCCAAGATACGAGGAGTCCCTGCACAACCCTTACCCTGATTACCACTGGCTGAGAACAGTGAAAACAACCAAGGAGTCTCTGGTCATCATCAGCCCTTCTGTGGCCGATCTGGACCCTTACGATAAGAGCCTGCACTCTAGAGTGTTTCCCGGCGGCAAGTGCTCTGGCATCACAGTGAGTTCTACCTGTTGTAGCACCAACCACGATTACACAATCTGGATGCCTGAGAACCCTAGACTGGGCACCAGCTGTGACATCTTCACAAACTCTAGGGGCAAGAGAGCTTCTAAGGGAGGAAAGACATGTGGCTTTGTGGATGAGAGGGGCCTGTATAAGTCTCTGAAGGGAGCTTGTAAGATGAAGCTGTGTGGAGTGCTGGGACTGAGACTGATGGATGGCACCTGGGTGGCTATCCAGACCTCTGATGAGATTAAGTGGTGTAGCCCTGACCAGCTGGTGAACCTGCACGACTTTCACAGCGATGAGATCGAGCACCTGGTGGTGGAGGAGCTGGTGAAGAAGAGAGAGGAGTGTCTGGATGCCCTGGAGACAATCATGACCACAAAGAGCGTGTCTTTTAGAAGATTGAGCCATCTGAGAAAGCTGGTGCCTGGATTTGGAAAGGCCTACACAATCTTCAACAAGACACTGATGGAGGCTGATGCCCACTACAAGAGCATCAGGACATGGAACGAGATCATTCCTTCTAAGGGCTGTCTGAGAGTGGGCGGCAGATGTCACCCTCACGTGAACGGCGTGTTCTTCAACGGCATCATCCTGGGACCTGATGGCCACGTGCTGATCCCTGAAATGCAGAGCTCTCTGCTGCACCAGCACATGGAGCTGCTGGAGTCCTCTGTGATCCCTCTGATGCATCCTCTGGCCGATCCTTCTACCGTGTTTAAGGATGGCGATGAGGCCGAGGATTTTGTGGAGGTGCACCTGCCTGATGTGCATAAGCAGATCTCTGGCGTGGATCTGGGCCTGCCTAACTGGGGAAAGTACCATCACCACCACCACCACTAA.
G蛋白氨基酸序列(SEQ ID No.3)具体如下:
MIPQVLLFVPLLVFSSCFGKFPIYTIPDKLGPWSPIDIHHLSCPNNLVVEDEGCTNLSGFSYMELKVGYISAIKVNGFTCTGVVTEAETYTNFVGYVTTTFKRKHFRPMPDACRAAYNWKMAGDPRYEESLHNPYPDYHWLRTVKTTKESLVIISPSVADLDPYDKSLHSRVFPGGKCSGITVSSTCCSTNHDYTIWMPENPRLGTSCDIFTNSRGKRASKGGKTCGFVDERGLYKSLKGACKMKLCGVLGLRLMDGTWVAIQTSDEIKWCSPDQLVNLHDFHSDEIEHLVVEELVKKREECLDALETIMTTKSVSFRRLSHLRKLVPGFGKAYTIFNKTLMEADAHYKSIRTWNEIIPSKGCLRVGGRCHPHVNGVFFNGIILGPDGHVLIPEMQSSLLHQHMELLESSVIPLMHPLADPSTVFKDGDEAEDFVEVHLPDVHKQISGVDLGLPNWGKYHHHHHH。
实施例2
单克隆抗体的制备
1、动物免疫
(1)分别将纯化后的RV G重组蛋白作为免疫原,与弗氏完全佐剂1:1混合后进行乳化,用于首次免疫;
(2)通过背部皮下多点注射的方法,2种免疫原分别免疫4~8周龄的雌性BALB/c小鼠3只,免疫剂量50μg/只;
(3)每隔2周用弗氏不完全佐剂与免疫抗原乳化后以相同的方法和剂量对BALB/c小鼠进行加强免疫,共进行4次免疫;
(4)4免后,分别尾静脉采血测定针对RV G重组蛋白的特异性抗体效价,分别选择效价较高的小鼠,于细胞融合前3~4天,通过腹腔注射的方法,分别用不含佐剂的RV G重组蛋白对BALB/c小鼠进行超强免疫,免疫剂量是100μg/只。
2、细胞融合及阳性克隆的筛选
采用聚乙二醇的方法,将免疫小鼠的脾细胞与小鼠骨髓瘤细胞SP2/0按细胞数量8:1的比例进行细胞融合,融合后的细胞用HAT选择培养基进行筛选;于融合后12天,以RV G重组蛋白作为包被抗原,通过间接ELISA法初步筛选阳性杂交瘤细胞;
间接ELISA法步骤如下所示:
(1)用CBS缓冲液将RV G重组蛋白稀释成浓度为2μg/mL的包被液,包被酶标板,100μl/孔,37℃孵育2h;
(2)弃去包被液,用PBST洗板拍干后,用5%脱脂奶封闭酶标板,200μl/孔,37℃孵育2h;
(3)弃去封闭液,用PBST洗板拍干后,将杂交瘤上清(一抗),加入酶标板中,100μl/孔,37℃孵育30min;
(4)弃去一抗,用PBST洗板7次,拍干;
(5)将稀释好的HRP标记的羊抗鼠IgG(二抗)加入反应孔中,100μl/孔,37℃孵育30min;
(6)弃去二抗,用PBST冲洗7次,拍干;
(7)每孔加入现配的TMB显色液100μl,暗室反应5min;
(8)每孔加入100μl H2SO4(2M)终止反应;
(9)酶标仪读取每孔的OD450值。
3、通过有限稀释法对杂交瘤细胞进行亚克隆
选取OD450值1.0以上的阳性孔,用含10%胎牛血清的1640培养基稀释上述阳性杂交瘤细胞至约10个细胞/ml,每孔100μl加入到预铺有100μl饲养细胞的96孔板中,置于37℃,5%CO2培养箱中培养一周;进一步通过间接ELISA法筛选阳性杂交瘤细胞;总共进行2~3次亚克隆,直至获得稳定分泌抗RV G重组蛋白单克隆抗体的杂交瘤细胞株2F2,将筛选得到的阳性单克隆细胞株扩大培养,细胞数按1~2×106/管进行冻存。
4、单克隆杂交瘤细胞株的鉴定
将所建立的单克隆杂交瘤细胞株连续培养3个月并反复从液氮冻存复苏,从而鉴定杂交瘤细胞的稳定性;结果显示获得的四株单克隆杂交瘤细胞株稳定性良好。
通过IFA的方法鉴定2F2单抗上清与RV G蛋白的反应性。将pcDNA3.1-RV G重组质粒转染293T细胞,瞬时表达RV G蛋白;经甲醇固定后,一抗孵育2F2单抗上清,37℃孵育1h,PBST洗板7次后拍干;二抗孵育FITC标记的羊抗鼠抗体,37℃孵育1h,PBST洗板7次后拍干;在倒置显微镜下观察荧光,结果显示2F2单抗(SEQ ID No.1)与RV G蛋白反应性良好(图4)。
5、体内诱生腹水法制备单抗
选择经产的雌性BALB/c小鼠,腹腔内注射500μl无菌的弗氏不完全佐剂,一周后,再次腹腔内注射获得的单克隆杂交瘤细胞2F2,注射量为1×106个细胞,再过一周后,待小鼠腹部膨大后抽取腹水,6000rpm离心10min后取上清,用辛酸硫酸铵法对腹水进行纯化,具体步骤如下所示:
(1)分别取上述腹水在4℃6000rpm离心20min后的中间层液体,并用乙酸乙酸钠(6mmol/L)将其5倍稀释;
(2)用5mol/L的NaOH调节步骤(1)中溶液的pH值至4.5左右,记录加入NaOH溶液的体积,室温条件下轻轻搅拌30min,
(3)室温滴加入正辛酸,边滴边搅拌,使其终浓度为25μL/mL,此时液体会变浑浊,继续室温搅拌30min,于4℃,6000rpm离心30min,取中间层液体;
(4)用PBS溶液润湿漏斗中的中速滤纸,将上一步中收集的上清液于滤纸中缓慢过滤,并收集滤液;
(5)将收集的滤液与10×PBS溶液按9:1的比例混合,调节pH值至7.4;
(6)将所得液体转移至4℃冰箱冷却,加入固体硫酸铵0.2778g/mL,边加边搅拌,可以在30min内分3次加完;
(7)将上一步中得到的溶液在4℃条件下,6000rpm离心20min,倒掉上清液体,加入600μL 1×PBS溶液,待沉淀完全溶解后装入透析袋中,4℃透析1-2d;
(8)透析结束后,将纯化后的腹水于4℃6000rpm离心10min,取上清液体分装成小管,放置-80℃备用。
实施例3
狂犬病毒抗体的免疫层析检测试纸的制备及应用
该实施例提供了一种检测狂犬病毒抗体的免疫层析试纸,该检测试纸包含本发明提供的RV G重组蛋白以及2F2单抗。
1、金标抗原的制备
(1)胶体金的制备
取100mL超纯水置于500mL洁净的锥形瓶,加入1mL 1%(w/v)氯金酸溶液煮沸;在搅拌状态下迅速加入新鲜配制的1mL 1%(w/v)柠檬酸钠溶液,煮沸约3min至溶液颜色由黄色变为***,继续煮沸2min;待溶液冷却至室温,补超纯水至100mL,以0.2mol/L K2CO3调pH至9.0,4℃避光保存备用。
(2)最适标记蛋白浓度测定
取待标记的G蛋白,在微孔板中以30μL超纯水1:2、1:4、1:8……分别倍比稀释;各孔加入125μL胶体金溶液,室温静置5min;加入125μL 1mol/L NaCl溶液;各孔颜色随蛋白浓度的降低而由红色变为蓝色。以颜色未变蓝的蛋白最高稀释度为胶体金最适标记浓度。
(3)蛋白的胶体金标记
取2mL最适蛋白浓度(12μg/ml)的待标记G蛋白,加入10mL胶体金溶液(pH 9.0),迅速混匀,室温作用10min~15min;加入混合液体积10%的含10%(w/v)牛血清白蛋白(BSA)的20mmol/L硼酸钠溶液,迅速混匀,室温作用10min~15min;4℃15000g离心30min,小心移去上清;以含1%(w/v)BSA的20mmol/L硼酸钠溶液重悬沉淀,同上离心,弃上清;重复洗涤1次,以1mL含1%(w/v)BSA的20mmol/L硼酸钠溶液重悬沉淀,4℃保存备用。
2、试纸的研制
(1)检测膜的制备
将硝酸纤维素检测膜(NC膜)置于XYZ 3000喷点仪平台上,并以压条固定;用PBS缓冲液分别将2F2单抗和SPA溶液稀释至0.5mg/mL,经0.22μm滤器过滤后,以1μL/cm分别将2F2单抗和SPA溶液喷点于硝酸纤维素检测膜中央,形成质控线(C线)和检测线(T线)印迹;检测线与检测线、检测线与质控线相距0.5cm;将检测膜置42℃干燥箱30min或室温自然干燥后,于4℃干燥密闭保存。
(2)结合垫的制备
将玻璃棉置于XYZ 3000喷点仪平台上,并以压条固定;取1mL金标蛋白加入2mL含2%(w/v)BSA、3%(w/v)蔗糖、0.6mol/L NaCl、0.2%Tween 20(v/v)和0.1%(w/v)叠氮钠的20mmol/L硼酸钠溶液(pH 8.0);以15μL/cm将金标G蛋白溶液(1mg/ml)喷点于玻璃棉;置50℃干燥箱30min干燥;将结合垫置于塑料袋中,加干燥剂4℃密闭保存备用。
(3)样品垫的制备
以含0.1mol/L NaCl、0.2%Tween 20(v/v)和0.1%(w/v)叠氮钠的PBS(pH 7.2)溶液浸泡玻璃棉条;置50℃干燥箱30min干燥;将样品垫置于塑料袋中,加干燥剂室温密闭保存备用。
(4)吸水垫的制备
将吸水垫置于塑料袋中,加干燥剂室温密闭保存备用。
(5)支撑板的制备
将双面胶贴于PVC支撑板,制备支撑板。
(6)试纸的组装
利用LM5000试纸装配仪或手工将上述材料装配成试纸板。先将检测膜粘贴于支撑板中央,然后将含有金标G蛋白的结合垫和样品垫依次粘贴于检测膜的样品端,各层间重叠1mm~2mm,再将吸水垫粘贴于检测膜的另一端,与检测膜重叠1mm~2mm(如图6)。
(7)检测原理
狂犬病毒抗体的免疫层析检测试纸应用RV G重组蛋白及其单克隆抗体,根据现代免疫学技术和层析技术设计组装,待测血清样品在层析过程中,样品中的待检抗体与结合垫上的金标G重组蛋白结合,然后分别被检测线(T线)上的SPA捕获,多余的金标G重组蛋白与质控线(C线)上的2F2单抗捕获,从而出现两条线。
3、检测临床样本
分别用本发明制备的狂犬病毒抗体检测免疫层析试纸同时检测狂犬病病毒、拉各斯蝙蝠病毒、Mokola病毒、Duvenhage病毒、欧洲蝙蝠狂犬病病毒1型、欧洲蝙蝠狂犬病病毒2型和澳大利亚蝙蝠狂犬病病毒的标准阳性血清。检测结果显示,本发明的狂犬病毒抗体检测免疫层析试纸检测狂犬病毒阳性血清的检测限可达1:12800(图7);特异性检测结果显示该试纸与其他同属病毒阳性血清均不发生交叉反应。以上结果表明本发明制备的狂犬病毒抗体检测免疫层析试纸具有较高的灵敏性和特异性(图8)。
以上所述仅是本发明的优选实施方式,应当指出,对于本技术领域的普通技术人员来说,在不脱离本发明原理的前提下,还可以做出若干改进和润饰,这些改进和润饰也应视为本发明的保护范围。
序列表
<110> 龙湖现代免疫实验室
郑州大学
<120> 一种狂犬病毒的单克隆抗体2F2及通用型狂犬病毒抗体快速检测试纸
<141> 2022-06-13
<160> 3
<170> SIPOSequenceListing 1.0
<210> 1
<211> 199
<212> PRT
<213> Artificial Sequence
<400> 1
Glu Ala Gln Ser Gly Ala Gly Leu Val Ala Ser Pro Gln Ser Val Lys
1 5 10 15
Leu Thr Cys Thr Ala Thr Gly Phe Asn Ile Thr Lys Asp Tyr His Trp
20 25 30
Val Trp Ile Arg Gln Phe Pro Gly Glu Gln Leu Glu Trp Met Gly Trp
35 40 45
Ile Asp Ser Glu Ser Gly Asp Ile Ser Tyr Asn Pro Ser Leu Lys Phe
50 55 60
Gln Ile Ser Ile Thr Ala Asp Thr Ser Trp Asn Thr Ala Phe Leu Asp
65 70 75 80
Leu Asn Ser Val Thr Ser Glu Asp Thr Ala Val Tyr Tyr Cys Asn Ala
85 90 95
Val Ser Leu Gly Asp Gln Ala Ser Ile Ser Cys Arg Ser Ser Gln Ser
100 105 110
Leu Leu His Ser Asp Gly Asn Thr Tyr Leu Asp Trp Tyr Leu Gln Lys
115 120 125
Pro Gly Gln Ser Pro Lys Leu Leu Ile Tyr Thr Ser Ser Phe His Arg
130 135 140
Phe Ser Gly Val Pro Asp Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp
145 150 155 160
Phe Thr Leu Lys Ile Ser Arg Val Glu Ala Glu Asp Leu Gly Ile Tyr
165 170 175
Phe Cys Ser Gln Ser Thr Leu Leu Pro Pro Thr Phe Gly Gly Gly Thr
180 185 190
Lys Leu Glu Ile Lys Arg Ile
195
<210> 2
<211> 1398
<212> DNA
<213> Artificial Sequence
<400> 2
atgatccctc aggtgctgct gtttgtgcct ctgctggtgt tctcttcttg ttttggaaag 60
tttcctatct acaccatccc tgataagctg ggcccttggt ctcctatcga tatccaccac 120
ctgagctgtc ctaacaacct ggtggtggag gatgagggct gtaccaacct gtctggcttt 180
tcttacatgg agctgaaggt gggctacatc tccgccatca aggtgaatgg cttcacatgc 240
accggcgtgg tgacagaggc cgagacatac accaactttg tgggatacgt gaccacaacc 300
ttcaagagga agcactttag acctatgcct gatgcctgta gagccgctta caactggaag 360
atggccggcg acccaagata cgaggagtcc ctgcacaacc cttaccctga ttaccactgg 420
ctgagaacag tgaaaacaac caaggagtct ctggtcatca tcagcccttc tgtggccgat 480
ctggaccctt acgataagag cctgcactct agagtgtttc ccggcggcaa gtgctctggc 540
atcacagtga gttctacctg ttgtagcacc aaccacgatt acacaatctg gatgcctgag 600
aaccctagac tgggcaccag ctgtgacatc ttcacaaact ctaggggcaa gagagcttct 660
aagggaggaa agacatgtgg ctttgtggat gagaggggcc tgtataagtc tctgaaggga 720
gcttgtaaga tgaagctgtg tggagtgctg ggactgagac tgatggatgg cacctgggtg 780
gctatccaga cctctgatga gattaagtgg tgtagccctg accagctggt gaacctgcac 840
gactttcaca gcgatgagat cgagcacctg gtggtggagg agctggtgaa gaagagagag 900
gagtgtctgg atgccctgga gacaatcatg accacaaaga gcgtgtcttt tagaagattg 960
agccatctga gaaagctggt gcctggattt ggaaaggcct acacaatctt caacaagaca 1020
ctgatggagg ctgatgccca ctacaagagc atcaggacat ggaacgagat cattccttct 1080
aagggctgtc tgagagtggg cggcagatgt caccctcacg tgaacggcgt gttcttcaac 1140
ggcatcatcc tgggacctga tggccacgtg ctgatccctg aaatgcagag ctctctgctg 1200
caccagcaca tggagctgct ggagtcctct gtgatccctc tgatgcatcc tctggccgat 1260
ccttctaccg tgtttaagga tggcgatgag gccgaggatt ttgtggaggt gcacctgcct 1320
gatgtgcata agcagatctc tggcgtggat ctgggcctgc ctaactgggg aaagtaccat 1380
caccaccacc accactaa 1398
<210> 3
<211> 465
<212> PRT
<213> Artificial Sequence
<400> 3
Met Ile Pro Gln Val Leu Leu Phe Val Pro Leu Leu Val Phe Ser Ser
1 5 10 15
Cys Phe Gly Lys Phe Pro Ile Tyr Thr Ile Pro Asp Lys Leu Gly Pro
20 25 30
Trp Ser Pro Ile Asp Ile His His Leu Ser Cys Pro Asn Asn Leu Val
35 40 45
Val Glu Asp Glu Gly Cys Thr Asn Leu Ser Gly Phe Ser Tyr Met Glu
50 55 60
Leu Lys Val Gly Tyr Ile Ser Ala Ile Lys Val Asn Gly Phe Thr Cys
65 70 75 80
Thr Gly Val Val Thr Glu Ala Glu Thr Tyr Thr Asn Phe Val Gly Tyr
85 90 95
Val Thr Thr Thr Phe Lys Arg Lys His Phe Arg Pro Met Pro Asp Ala
100 105 110
Cys Arg Ala Ala Tyr Asn Trp Lys Met Ala Gly Asp Pro Arg Tyr Glu
115 120 125
Glu Ser Leu His Asn Pro Tyr Pro Asp Tyr His Trp Leu Arg Thr Val
130 135 140
Lys Thr Thr Lys Glu Ser Leu Val Ile Ile Ser Pro Ser Val Ala Asp
145 150 155 160
Leu Asp Pro Tyr Asp Lys Ser Leu His Ser Arg Val Phe Pro Gly Gly
165 170 175
Lys Cys Ser Gly Ile Thr Val Ser Ser Thr Cys Cys Ser Thr Asn His
180 185 190
Asp Tyr Thr Ile Trp Met Pro Glu Asn Pro Arg Leu Gly Thr Ser Cys
195 200 205
Asp Ile Phe Thr Asn Ser Arg Gly Lys Arg Ala Ser Lys Gly Gly Lys
210 215 220
Thr Cys Gly Phe Val Asp Glu Arg Gly Leu Tyr Lys Ser Leu Lys Gly
225 230 235 240
Ala Cys Lys Met Lys Leu Cys Gly Val Leu Gly Leu Arg Leu Met Asp
245 250 255
Gly Thr Trp Val Ala Ile Gln Thr Ser Asp Glu Ile Lys Trp Cys Ser
260 265 270
Pro Asp Gln Leu Val Asn Leu His Asp Phe His Ser Asp Glu Ile Glu
275 280 285
His Leu Val Val Glu Glu Leu Val Lys Lys Arg Glu Glu Cys Leu Asp
290 295 300
Ala Leu Glu Thr Ile Met Thr Thr Lys Ser Val Ser Phe Arg Arg Leu
305 310 315 320
Ser His Leu Arg Lys Leu Val Pro Gly Phe Gly Lys Ala Tyr Thr Ile
325 330 335
Phe Asn Lys Thr Leu Met Glu Ala Asp Ala His Tyr Lys Ser Ile Arg
340 345 350
Thr Trp Asn Glu Ile Ile Pro Ser Lys Gly Cys Leu Arg Val Gly Gly
355 360 365
Arg Cys His Pro His Val Asn Gly Val Phe Phe Asn Gly Ile Ile Leu
370 375 380
Gly Pro Asp Gly His Val Leu Ile Pro Glu Met Gln Ser Ser Leu Leu
385 390 395 400
His Gln His Met Glu Leu Leu Glu Ser Ser Val Ile Pro Leu Met His
405 410 415
Pro Leu Ala Asp Pro Ser Thr Val Phe Lys Asp Gly Asp Glu Ala Glu
420 425 430
Asp Phe Val Glu Val His Leu Pro Asp Val His Lys Gln Ile Ser Gly
435 440 445
Val Asp Leu Gly Leu Pro Asn Trp Gly Lys Tyr His His His His His
450 455 460
His
465
Claims (10)
1.一种识别狂犬病毒G蛋白的单克隆抗体2F2,其特征在于,所述单克隆抗体2F2的氨基酸序列如SEQ ID No.1所示。
2.权利要求1所述的单克隆抗体2F2在制备检测狂犬病毒试剂中的应用。
3.一种通用型狂犬病毒抗体快速检测试纸条,包括:在支撑板上依次搭接样品垫、结合垫、检测膜和吸水垫,其特征在于,所述检测膜上喷涂检测线和质控线;
所述质控线上喷涂有权利要求1所述的单克隆抗体2F2。
4.根据权利要求3所述的试纸条,其特征在于,所述单克隆抗体2F2以单克隆抗体2F2溶液形式进行喷涂,所述单克隆抗体2F2溶液的浓度为0.5mg/mL。
5.根据权利要求4所述的试纸条,其特征在于,所述单克隆抗体2F2溶液以1µL/cm喷涂。
6.根据权利要求3所述的试纸条,其特征在于,所述检测线上喷涂有SPA,所述SPA以SPA溶液形式进行喷涂,所述SPA溶液的浓度为0.5mg/mL;
所述SPA溶液以1µL/cm喷涂。
7.根据权利要求3所述的试纸条,其特征在于,所述结合垫上喷涂有胶体金标记的狂犬病毒G蛋白。
8.根据权利要求7所述的试纸条,其特征在于,所述狂犬病毒G蛋白以狂犬病毒G蛋白溶液形式进行喷涂,所述狂犬病毒G蛋白溶液的浓度为1mg/ml;
所述狂犬病毒G蛋白溶液以15µL/cm喷涂。
9.根据权利要求3所述的试纸条,其特征在于,所述质控线与检测线的间距为0.5cm。
10.根据权利要求3所述的试纸条,其特征在于,所述搭接的重叠距离为1~2mm。
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WO1990011358A1 (fr) * | 1989-03-29 | 1990-10-04 | Institut Pasteur | Procede de detection et/ou d'identification des infections a lyssavirus, clonage et expression de genes codant pour des peptides et/ou des fragments de peptides du lyssavirus mokola, vaccin contre le virus mokola et/ou l'ensemble des lyssavirus ainsi que procede d'obtention dudit vaccin par genie genetique |
CN104928302A (zh) * | 2015-05-22 | 2015-09-23 | 华南农业大学 | 一株通过基因修饰以优化表达后的狂犬病病毒糖蛋白及其单克隆抗体和应用 |
CN110007080A (zh) * | 2019-04-12 | 2019-07-12 | 长春西诺生物科技有限公司 | 一种狂犬病毒抗体定量检测试剂盒及其制备方法与检测方法 |
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