CN114163524B - 抗体及其在a蛋白检测中的应用 - Google Patents
抗体及其在a蛋白检测中的应用 Download PDFInfo
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- CN114163524B CN114163524B CN202111478482.8A CN202111478482A CN114163524B CN 114163524 B CN114163524 B CN 114163524B CN 202111478482 A CN202111478482 A CN 202111478482A CN 114163524 B CN114163524 B CN 114163524B
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Abstract
本发明涉及生物检测技术领域,尤其涉及抗体及其在A蛋白检测中的应用。本发明提供的包被抗体和标记抗体与SPA蛋白有着高度的亲合力,将其用于SPA残留的检测。其中包被抗体包被与磁微粒,标记抗体以辣根过氧化物酶标记,通过一步夹心检测法,实现对SPA进行准确快速检测。
Description
技术领域
本发明涉及生物检测技术领域,尤其涉及抗体及其在A蛋白检测中的应用。
背景技术
金黄色葡萄球菌(Staphylococcus aureus)是一类极其常见的革兰氏阳性菌,属于葡萄球菌属(Staphy-lococcus)。金黄色葡萄球菌蛋白A(Staphylococcus aureus,proteinA,SPA)是金黄色葡萄球菌膜表面的一种蛋白质,约占整个细胞壁蛋白质成分的6.7%,通过COOH端与细胞壁肽聚糖呈共价连接,分子质量为42Kda,几乎90%的金黄色葡萄球菌细胞壁表面都含有SPA。
因此,对SPA的检测可以反映出金黄色葡萄球菌的存在情况,目前制药行业监测SPA残留多采用商品化试剂盒。目前,商业化的SPA检测试剂盒多采用双抗体夹心法,所用抗体为针对SPA的抗体。
SPA是一种高度稳定的I型膜细胞表面受体,能够与单克隆抗体的Fc片段特异性结合。SPA多肽链由E、D、A、B、C五个同源区组成,每个同源区都能与人及某些哺乳动物血清中IgG的Fc片段结合,且不影响抗体分子Fab片段与抗原结合位点的活性。
针对SPA的特性,研发新的检测方法,从而进一步的提高检测的效率,具有重要的意义。
发明内容
有鉴于此,本发明要解决的技术问题在于提供一对与SPA蛋白有着高度的亲合力的抗体及其在SPA蛋白检测中的应用。
本发明提供的抗体包括包被抗体和标记抗体两种。
本发明提供的包被抗体,
其重链的三个CDR区的氨基酸序列分别具有如SEQ ID NO:1、2和3所示的氨基酸序列;
其轻链的三个CDR区的氨基酸序列分别具有如SEQ ID NO:4、5和6所示的氨基酸序列。
一些实施例中,所述包被抗体重链的氨基酸序列如SEQ ID NO:7所示。
一些实施例中,所述包被抗体轻链的氨基酸序列如SEQ ID NO:8所示。
本发明还提供了包被抗体与介质偶联制得的偶联物。
本发明中,所述与包被抗体偶联的介质为固体或非固体。具体实施例中,所述介质为磁珠。
本发明提供的标记抗体,
其重链的三个CDR区的氨基酸序列分别具有如SEQ ID NO:9、10和11所示的氨基酸序列;
其轻链的三个CDR区的氨基酸序列分别具有如SEQ ID NO:12、13和14所示的氨基酸序列。
一些实施例中,所述标记抗体重链的氨基酸序列如SEQ ID NO:15所示;
一些实施例中,所述标记抗体轻链的氨基酸序列如SEQ ID NO:16所示。
本发明还提供了所述标记抗体经标记物修饰制得的结合物。
本发明中,所述标记为化学标记或生物标记,一些实施例中,所述标记物为辣根过氧化物酶。
本发明所述的包被抗体、偶联物,标记抗体,结合物,在制备SPA蛋白检测的试剂中的应用。
本发明提供了一种检测SPA蛋白的试剂,其包括本发明所述的偶联物和所述的结合物。
本发明所述的试剂,还包括洗液、底物A和底物B;
所述洗液为PBST缓冲液;
所述底物A包括鲁米诺;
所述底物B包括双氧水。
本发明还提供了一种检测SPA蛋白的方法,其以本发明所述的试剂对样品进行检测。
体外诊断检测中,特别是针对双抗夹心检测模式,如果包被和标记抗体中SPA均有残留,将会导致二者夹心产生高本底或者假阳性的情况。因此,本发明所述试剂的功能之一是对需要进行抗体的SPA残留检测的样品进行检测。一些实施例中,所述待测样品为经SPA亲和层析纯化获得抗体。
本发明中,所述检测采用一步夹心法。
本发明提供的包被抗体和标记抗体与SPA蛋白有着高度的亲合力,将其用于SPA残留的检测。其中包被抗体包被与磁微粒,标记抗体以辣根过氧化物酶标记,通过一步夹心检测法,实现对SPA进行准确快速检测。
具体实施方式
本发明提供了抗体及其在A蛋白检测中的应用,本领域技术人员可以借鉴本文内容,适当改进工艺参数实现。特别需要指出的是,所有类似的替换和改动对本领域技术人员来说是显而易见的,它们都被视为包括在本发明。本发明的方法及应用已经通过较佳实施例进行了描述,相关人员明显能在不脱离本发明内容、精神和范围内对本文的方法和应用进行改动或适当变更与组合,来实现和应用本发明技术。
除非另有定义,本文使用的所有科技术语具有本领域普通技术人员所理解的相同含义。关于本领域的定义及术语,专业人员具体可参考Current Protocols in MolecularBiology(Ausubel)。氨基酸残基的缩写是本领域中所用的指代20个常用L-氨基酸之一的标准3字母和/或1字母代码。
“抗体”是指由能特异结合抗原的一种或多种多肽构成的蛋白质。抗体的一种形式构成了抗体的基本结构单元。这种形式是四聚物,它由两对完全相同的抗体链构成,每一对都有一个轻链和一个重链。在每对抗体链中,轻链和重链的可变区联合在一起共同负责结合抗原,而恒定区则负责抗体的效应器功能。
抗体重链或轻链的“可变区”是该链的N端成熟区域。目前已知的抗体类型包括κ和λ轻链,以及α,γ(IgG1,IgG2,IgG3,IgG4),δ,ε和μ重链或它们的其它类型等价物。全长的免疫球蛋白“轻链”(大约25kDa或大约214个氨基酸)包含一个由NH2-末端上大约110个氨基酸形成的可变区,以及一个COOH-末端上的κ或λ恒定区。全长的免疫球蛋白“重链”(大约50kDa或大约446个氨基酸),同样包含一个可变区(大约116个氨基酸),以及重链恒定区之一,例如γ(大约330个氨基酸)。
本文使用的“CDR区”或“CDR”是指免疫球蛋白的重链和轻链的高变区,如Kabat etal.所定义(Kabat et al.,Sequences of proteins of immunological interest,5thEd.,U.S.Department of Health and Human Services,NIH,1991,以及以后版本)。存在三个重链CDR和三个轻链CDR。根据情况,本文所用术语CDR或CDRs是为了指示这些区域之一、或者这些区域的几个或者甚至全部,所述区域包含通过抗体对抗原或其识别表位的亲和力而负责结合的大部分氨基酸残基。
本发明提供的抗体包括标记抗体和包被抗体,这对抗体并非特异性的SPA蛋白的抗体,但这对抗体的Fc区与SPA蛋白有着高度的亲合力。
本发明所述包被抗体轻链的三个CDR区依次为:KSLLHSNGFTY、QMS、QHHFGTPWT。具体的包被抗体轻链氨基酸序列为:DIVMTQAAFSNPVTLGTSASISCRSSKSLLHSNGFTYLNWYLQKPGQSPQLLIYQMSNLASGVPDRFSSSGSGTDFTLRISRVEAEDVGVYYCQHHFGTPWTFGGGTKLEIK。
包被抗体重链的三个CDR区依次为:GYSFTNYW、IDPANDNA、ALYYYGPTY,包被抗体重链的氨基酸序列为:EVQLQQSGTVLARPGASVKISCKASGYSFTNYWMNWIEQRPGQGLEWIGTIDPANDNANFNQNFKGKAKLTAVTSTSTAYMELSSLTNEDSAVYYCALYYYGPTYWGQGTLVTVSA。
标记抗体重链的三个CDR区依次为:ENIYSY、NAI、AQNLELPWT。标记抗体轻链氨基酸序列为:DIQMTQSPASLSASVGKSVTITCRASENIYSYLAWYQQKQGESPHLLVYNAITLAEGVPSRFRGSGSGTQFSLRINSLQPEDLGSYYCAQNLELPWTFGGGTKLEIK。
标记抗体重链的三个CDR区依次为:GFNIIDTY、IYPGNQNA、STYYRYDVGWFAS。标记抗体重链氨基酸序列为:EVQLKQSGAELVKPGASVKLSCTASGFNIIDTYIHWVKQRPEQGLEWIGKIYPGNQN AEYDPKFRGKATVTSDTSSNTAFLQLSSLTSEDTAVYYCSTYYRYDVGWFASWGQGTLVTVSA。
“抗体”包括任何同型体的抗体或免疫球蛋白,或保持与抗原特异结合的抗体片段,包括但不限于Fab,Fv,scFv和Fd片段、嵌合抗体、人源化抗体、单链抗体以及包含抗体的抗原结合部分和非抗体蛋白质的融合蛋白质。
抗体可以被标记和检测,本发明中,所述标记包括化学标记或生物标记。标记抗体通过放射性同位素、能产生可检测物的酶、荧光蛋白质、生物素进行标记后可被检测。所述化学标记为同位素、免疫毒素和/或化学药物;一些实施例中,所述生物标记为生物素、亲和素或酶标记。所述酶标记优选为辣根过氧化物酶或碱性磷酸酶。所述免疫毒素优选为黄曲霉毒素、白喉毒素、绿脓杆菌外毒素、蓖麻毒蛋白、相思子毒蛋白、槲寄生凝集素、蒴莲根毒素、PAP、造草素、白树毒素或丝瓜毒素。本发明实施例中,所述标记抗体被生物酶标记。一些具体实施例中,所述标记抗体被辣根辣根过氧化物酶。
抗体还可以包被于固相或非固相载体。所述固体介质或非固体介质选自胶体金、聚苯乙烯平板或珠粒。本发明中,所述包被抗体包被于磁微粒。
本发明提供的包被抗体和标记抗体与SPA蛋白有着高度的亲合力,将其用于SPA残留的检测。其中包被抗体包被与磁微粒,标记抗体以辣根过氧化物酶标记,通过一步夹心检测法,实现对SPA进行准确快速检测。而对实验中获得的其他抗体组合制备成试剂盒,以相同的方法对SPA进行检测,结果表明,准确性和灵敏度都不及本发明制备获得的试剂盒。
本发明所述的两个抗体的筛选方法包括:包被SPA蛋白,加入抗体,对照不加解离剂,检测抗体加解离剂(6M尿素、1M盐酸胍或者1.5M NaSCN),解离后洗板,加入HRP标记的羊抗鼠二抗。检测OD450,解离孔/不加解离剂。值越高,亲合力越高。筛选到亲合力>60%的,然后进行配对筛选。筛选到可以夹心检测SPA蛋白的配对抗体。
本发明中,所述包被抗体包被于磁微粒的制备方法包括:磁微粒与包被抗体偶联采用羧基两步法,制备过程中,EDC浓度10mg/ml;NHS浓度10mg/ml(摩尔比EDC:NHS:抗体=50:50:1),磁微粒包被浓度0.2~0.5μg/T。
所述标记抗体被辣根过氧化物酶标记的步骤包括:酶标抗体制备采用过碘酸钠法标记。酶标抗体使用工作浓度1/4K-1/5K。
本发明中,所述SPA蛋白的制备采用重组大肠杆菌表达法,表达后的粗蛋白经金属螯合层析结合离子交换层析获得。
本发明检测方法中,以重组SPA蛋白为标准品。所述标准品的浓度为0、10pg/ml、40pg/ml、100pg/ml、200pg/ml、400pg/ml。
本发明所述一步夹心法检测方法,其特征在于,反应原理为:
①加入包被抗体的磁微粒20μl、加入待检样品50μl;加入酶标抗体50μl,反应15min;②加入洗液,洗6次,加入发光底物A和B各50μl,检测。洗液成分:PBST(PBS+Tween20);底物A成分:鲁米诺;底物B成分:双氧水。
本发明采用的试材皆为普通市售品,皆可于市场购得。下面结合实施例,进一步阐述本发明:
实施例1高亲合力抗体筛选
1、SPA蛋白包被:
1)SPA蛋白采用pH9.6 0.01M碳酸盐缓冲液进行稀释,稀释至5μg/ml,50ul/孔,加入至96孔酶免板中,37℃12h。
2)用PBST缓冲液洗5遍,在吸水纸上拍干孔内残留液体,加入50μl封闭液(5%的Casein缓冲液),37℃2h。
3)在吸水纸上拍干孔内残留液体,烘干,真空包装袋密封保存备用。
2、抗体筛选:
1)待筛选抗体,采用0.01M磷酸盐缓冲液稀释至5μg/ml;
2)取出包被酶免板,A1和B1孔中各加入100μl稀释过的待测抗体,其他待测样本也以同样方式复孔加样;
3)在微型振荡器上震荡30秒使孔内液体混合均匀,37℃温育30min;
4)洗板5次,在吸水纸上拍干孔内残留液体;
5)其中一孔加入100μl对照缓冲液(pH9.6 0.01M Tris缓冲液)(如A1、C1、E1、G1),另外一孔加入100μl解离液(pH9.6 0.01M Tris缓冲液+6M尿素)(如B1、D1、F1、H1);
6)重复操作步骤3,37℃温育10min;
7)重复操作步骤4;
8)每孔分别加入酶结合物100μl(HRP标记的羊抗鼠二抗,1/3K稀释);
9)重复操作步骤3、4;
10)每孔加入底物液和显色剂各50μl,37℃避光反应10min;
11)每孔加入终止液50μl,震荡混匀后,立即测试结果;
12)用酶标仪450nm波长检测各孔的吸光值(OD值)。
13)结果计算:
IgG抗体亲合力=解离缓冲液孔OD值/对照缓冲液孔OD值×100%。
3、抗体配对建立:
1)筛选到亲合力>60%的抗体,然后再进行配对筛选。
2)筛选到高亲合力抗体,均采用过碘酸钠法进行HRP标记。
3)包被和酶标抗体交叉配对采用酶联免疫法筛选,5μg/ml的包被浓度,酶标1/4K-1/5K。
4)大肠杆菌重组SPA蛋白稀释梯度,夹心检测。
5)最终筛选到一对抗体,作为SPA蛋白检测的配对抗体,经ELISA检测该对抗体对SPA蛋白的亲和力显著优于其他抗体。
经测序,
包被抗体轻链氨基酸序列为:
DIVMTQAAFSNPVTLGTSASISCRSSKSLLHSNGFTYLNWYLQKPGQSPQLLIYQMSNLASGVPDRFSSSGSGTDFTLRISRVEAEDVGVYYCQHHFGTPWTFGGGTKLEIK
包被抗体重链氨基酸序列为:
EVQLQQSGTVLARPGASVKISCKASGYSFTNYWMNWIEQRPGQGLEWIGTIDPANDNANFNQNFKGKAKLTAVTSTSTAYMELSSLTNEDSAVYYCALYYYGPTYWGQGTLVTVSA
标记抗体轻链氨基酸序列为:
DIQMTQSPASLSASVGKSVTITCRASENIYSYLAWYQQKQGESPHLLVYNAITLAEGVPSRFRGSGSGTQFSLRINSLQPEDLGSYYCAQNLELPWTFGGGTKLEIK
标记抗体重链氨基酸序列为:
EVQLKQSGAELVKPGASVKLSCTASGFNIIDTYIHWVKQRPEQGLEWIGKIYPGNQNAEYDPKFRGKATVTSDTSSNTAFLQLSSLTSEDTAVYYCSTYYRYDVGWFASWGQGTLVTVSA
实施例2试剂盒制备
1、抗体包被磁微粒:
1)磁微粒与包被抗体采用羧基两步法进行包被,磁微粒包被浓度为0.2μg/T;
2)将磁珠原液进行混匀,取30μl磁珠原液+300μlpH7.4 0.01M磷酸盐缓冲液,洗涤5次,加入10mg/mlEDC 50μl(pH4.7 0.01M醋酸缓冲液配制)+10mg/ml NHS 50μl(pH4.70.01M醋酸缓冲液配制),混匀后振荡反应1h;
3)300μl B液洗涤2次,100μl(定量抗体用pH4.7 0.01M醋酸缓冲液\稀释),混匀后振荡反应2h;(其中摩尔比EDC:NHS:抗体=50:50:1)
4)加入1mol/L300μl乙醇胺终止反应30min;
5)弃上清,加入300μl封闭液同洗涤方法封闭4次;
6)加入保护液(封闭液)3ml存于2~8℃。
封闭液包括:0.01M PBS pH7.4(含1%BSA+10%甘油)。
2、HRP修饰标记抗体
酶标抗体制备采用过碘酸钠法标记,步骤包括:HRP的活化,活化后的HRP与抗体反应,终止反应,透析,加入50%的甘油,获得HRP标记抗体。
3、洗液:配制PBST缓冲液,包括:取300μl Tween-20加入PBS 100ml中,现配现用。
4、底物A:鲁米诺溶液。
5、底物B:双氧水溶液。
6、标准品:大肠杆菌表达重组SPA蛋白(GI:1442983453),经金属螯合层析结合离子交换层析获得,梯度稀释,浓度依次为0pg/mL、10pg/mL、40pg/mL、100pg/mL、200pg/mL、400pg/mL。
实施例3一步夹心法检测SPA残留
1、待测样品为:
2、检测试剂:实施例2制备:
3、检测步骤包括:
3.1在反应容器中依次加入标准品和待检样品,加样量为50μl/孔
3.2每孔加入包被抗体的磁微粒混悬液20μl;
3.3加入酶标抗体50μl(用工作浓度1/5K);
3.4混匀后,37℃温育15min;
3.5加入洗液,洗6次;
3.6每孔加入发光底物A液和发光底物B液各50μl;
3.7混匀后1-5min,检测发光强度。
4、结果分析:
标准品检测结果:
待测品检测结果:
如上表所示,在样本中SPA的含量大于0.2ng/ml时,本发明试剂盒与商品化SPA检测试剂盒结果一致性较高,说明本发明试剂盒具有良好的准确性。在含量低于0.2ng/ml,市售试剂盒无法有效检测获得结果,说明本发明试剂盒的灵敏度高于市售试剂盒。
以上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。
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Thr Phe Gly Gly Gly Thr Lys Leu Glu Ile Lys
100 105
Claims (13)
1.包被抗体,其特征在于,
其重链的三个CDR区的氨基酸序列分别如SEQ ID NO:1、2和3所示;
其轻链的三个CDR区的氨基酸序列分别如SEQ ID NO:4、5和6所示。
2.根据权利要求1所述的包被抗体,其特征在于,
其重链的氨基酸序列如SEQ ID NO:7所示;
其轻链的氨基酸序列如SEQ ID NO:8所示。
3.权利要求1或2所述包被抗体与介质偶联制得的偶联物。
4.根据权利要求3所述的偶联物,其特征在于,所述介质为磁珠。
5.权利要求1或2所述的包被抗体、权利要求3或4所述的偶联物在制备SPA蛋白检测的试剂中的应用。
6.一种检测SPA蛋白的试剂,其特征在于,包括权利要求3或4所述的偶联物。
7.根据权利要求6所述的试剂,其特征在于,还包括标记抗体经标记物修饰制得的结合物,其中:
标记抗体重链的三个CDR区的氨基酸序列分别如SEQ ID NO:9、10和11所示;
标记抗体轻链的三个CDR区的氨基酸序列分别如SEQ ID NO:12、13和14所示。
8.根据权利要求7所述的试剂,其特征在于,
标记抗体重链的氨基酸序列如SEQ ID NO:15所示;
标记抗体轻链的氨基酸序列如SEQ ID NO:16所示。
9.根据权利要求7所述的试剂,其特征在于,所述标记物为辣根过氧化物酶。
10.根据权利要求9所述的试剂,其特征在于,还包括洗液、底物A和底物B;
所述洗液为PBST缓冲液;
所述底物A包括鲁米诺;
所述底物B包括双氧水。
11.一种检测SPA蛋白的方法,其特征在于,以权利要求6~10任一项所述的试剂对样品进行检测。
12.根据权利要求11所述的方法,其特征在于,所述待测样品为经SPA亲和层析纯化获得抗体。
13.根据权利要求11或12所述的方法,其特征在于,所述检测采用一步夹心法。
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