CN113493494B - Eb病毒balf3蛋白的抗原表位 - Google Patents
Eb病毒balf3蛋白的抗原表位 Download PDFInfo
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- CN113493494B CN113493494B CN202010205009.1A CN202010205009A CN113493494B CN 113493494 B CN113493494 B CN 113493494B CN 202010205009 A CN202010205009 A CN 202010205009A CN 113493494 B CN113493494 B CN 113493494B
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Abstract
本发明涉及分子生物学与免疫学技术领域，尤其涉及EB病毒BALF3蛋白的抗原表位。本发明提供了EB病毒BALF3蛋白的抗原表位，其如SEQ ID NO：1所示，并提供了编码该表位的核酸分子，还提供了其抗原蛋白、特异性抗体及其应用。本发明所述的抗原表位具有良好的保守性、敏感性及特异性，所制得的抗体效价较高，能够应用于临床诊断及分子机制的研究。
Description
技术领域
本发明涉及分子生物学与免疫学技术领域，尤其涉及EB病毒BALF3蛋白的抗原表位。
背景技术
EB病毒(Epstein-Barr virus，EBV)是疱疹病毒科嗜淋巴细胞病毒属的成员，基因组为DNA。EB病毒具有在体内外专一性地感染人类及某些灵长类B细胞的生物学特性。人是EB病毒感染的宿主，主要通过唾液传播。无症状感染多发生在幼儿，3～5岁幼儿90％以上曾感染EB病毒，90％以上的成人都有病毒抗体。EB病毒是传染性单核细胞增多症的病原体，此外EB病毒与鼻咽癌、儿童淋巴瘤的发生有密切相关性，被列为可能致癌的人类肿瘤病毒之一。目前所测EB病毒抗体，主要有针对病毒的衣壳抗原(CA)、早期抗原(EA)和核抗原(EBNA)。
BALF3是EB病毒裂解期蛋白，已有文献报道表明其促进病毒自身成熟(PMID：24554665)，参与病毒在宿主人体内免疫逃逸(PMID：30133498)，诱导宿主细胞基因组不稳定性、遗传学异常及恶性转化(PMID：29108278，25261366)。因此，检测BALF3蛋白的表达情况对于研究其致病机制等方面存在非常重要的意义。然而，EB病毒基因组存在的高度可变异性，尽管BALF3的序列已经与NCBI数据库中登录，但仍难以确定高保守性和高度特异性的抗原结构域，因此，目前还上缺乏可供临床检测及科学研究使用的BALF3抗体，也因此，对于BALF3在肿瘤组织中表达检测及其致病机制研究等均受到极大的限制。
发明内容
有鉴于此，本发明要解决的技术问题在于提供EB病毒BALF3蛋白的抗原表位，该表位制备抗体能够用于特异性检测BALF3的表达，可满足包括免疫印迹、免疫组化、免疫共沉淀、染色质共沉淀等实验需要，有助于相关临床检验及科学研究的开展以明确EB病毒与肿瘤致病的相关性及其分子机制。
本发明提供的EB病毒BALF3蛋白的抗原表位，其如SEQ ID NO：1所示。
本发明从31例EBV感染的肿瘤组织中，获得了EB病毒BALF3蛋白的保守序列，该序列如SEQ ID NO：3所示，通过对该蛋白序列进行可表达性和抗原性进行预测筛选，最终确定抗原表位为SEQ ID NO：3所示氨基酸序列的510～700位氨基酸，即SEQ ID NO：1所示的多肽。该区段不含突变氨基酸位点，免疫原性较好，二级结构稳定，易于表达。
本发明还提供了编码SEQ ID NO：1所示抗原表位的核酸分子。
肿瘤组织中编码BALF3蛋白的DNA分子的核酸序列如SEQ ID NO：4所示。其中编码SEQ ID NO：1所示抗原表位的核酸分子共计573bp。为了使该抗原表位能够顺利的在原核系统中进行表达，对编码其的核酸分子进行密码子优化，优化后的序列如SEQ ID NO：2所示。
本发明还提供了一种核酸载体，其包含编码SEQ ID NO：1所示抗原表位的核酸分子。
本发明所述的核酸载体中，所述编码SEQ ID NO：1所示抗原表位的核酸分子的序列如SEQ ID NO：2所示。该载体的骨架载体为pGEX4T-AB1。
本发明还提供了一种重组宿主，其包含本发明所述的核酸载体。
本发明所述的核酸载体能够在宿主体内表达SEQ ID NO：1所示抗原表位，该宿主在本发明中称为重组宿主。所述的宿主细胞选自大肠杆菌、酵母菌、昆虫细胞或哺乳动物细胞。为了实现表位的更高效的表达，采用原核表达系统。在本发明的实施例中，所述重组宿主的宿主细胞为大肠杆菌。具体采用E.coli Rosetta。
所述重组宿主经诱导后表达，分离纯化可获得表达的抗原蛋白。因此，本发明还提供了表达本发明所述重组宿主获得的抗原蛋白。
本发明提供的抗原蛋白能够刺激受体产生抗体，所述抗体可用于制备EB病毒BALF3蛋白检测试剂。
本发明还要求保护EB病毒BALF3蛋白的特异性抗体，其由本发明所述的抗原表位或融合蛋白免疫动物制得。作为优选，所述的特异性抗体可以为单克隆抗体，也可以为多克隆抗体。在本发明实施例中，所述抗体由本发明所述的抗原表位或融合蛋白免疫兔制得。免疫后的抗血清用pGEX-4T-AB1-BALF3蛋白作抗原亲和纯化后，得到浓缩后的抗体。
本发明所述的抗原表位、抗原蛋白或特异性抗体，在制备EB病毒BALF3蛋白检测试剂中的应用。
本发明提供的抗原表位、抗原蛋白或特异性抗体能够应用于EB病毒BALF3蛋白的免疫学的检测方法，例如：酶联免疫吸附测定法、免疫印迹、免疫组化、免疫共沉淀、染色质共沉淀等。其检测可包括直接法或间接法。
本发明还提供了一种试剂，其包含本发明所述的抗原表位、本发明抗原蛋白和/或本发明所述的特异性抗体。
本发明提供的试剂能够应用于免疫学检测，除包含本发明所述的抗原表位、本发明抗原蛋白和/或本发明所述的特异性抗体外，还包括检测所需的缓冲液、二抗和固相支持物。
本发明提供的抗原蛋白能够刺激受体产生抗体，所述抗体具有良好的特异性，也可用于保护受体抵抗EB病毒的感染。
本发明所述的抗原蛋白在制备防治EB病毒引起疾病的治疗性抗体和/或疫苗中的应用。
一种治疗性抗体和/或疫苗，其由本发明所述的抗原蛋白制得。
本发明提供的治疗性抗体包括由本发明所述抗原蛋白刺激受体产生的抗体。其中还可以包括要学上可接受的辅料，根据实际应用的需要，其剂型包括注射剂或口服制剂。
本发明还提供了一种疫苗，其包括本发明所述的抗原蛋白和佐剂。
作为优选，佐剂为氢氧化铝佐剂、弗氏完全佐剂或弗氏不完全佐剂。
所述疫苗中还包括稳定剂、pH调节剂、防腐剂等。也可包括免疫应答的调节剂。
所述EB病毒引起的疾病包括因感染EB病毒引起的咽炎、发热和淋巴结病，还包括传染性单核细胞增多症、鼻咽癌、儿童淋巴瘤。
本发明提供了EB病毒BALF3蛋白的抗原表位，其如SEQ ID NO：1所示，并提供了编码该表位的核酸分子，还提供了其抗原蛋白、特异性抗体及其应用。本发明所述的抗原表位具有良好的特异性，所制得的抗体效价较高，能够应用于临床诊断及分子机制的研究。
附图说明
图1示31例EB病毒阳性的NK/T细胞淋巴瘤患者的BALF3蛋白序列与B95-8参考序列进行比对，其中，BALF3_temp为参考序列，BALF3_SNV代表我们完成的31例EBV阳性的NKT细胞淋巴瘤样本实际测序数据；
图2示BALF3_SNV的保守结构域；
图3示BALF3_SNV的二级结构预测；
图4示BALF3_SNV的抗原表位预测；
图5示抗原表达质粒的验证；
图6示构建的重组宿主所表达的融合蛋白纯化前(左)及纯化后(右)；
图7示免疫获得两株抗体进行抗血清ELISA检测；
图8示抗体(E11797、E11798)的抗原western blot检测结果；
图9示抗体特异性检测结果(即对于不含病毒蛋白样本检测结果为阴性)。
具体实施方式
本发明提供了EB病毒BALF3蛋白的抗原表位，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。
本发明中所述“抗原表位”(epitope)又称抗原决定簇或抗原决定基，是指抗原分子中决定抗原特异性的特殊化学基团。本发明的抗原表位是一段包含191个氨基酸残基的多肽片段，因此，在本发明中，所述抗原表位、表位、多肽交替使用。
本发明中，所述“核酸分子”是指有多个核苷酸聚合形成的生物大分子化合物，所述核苷酸可为核糖核酸或脱氧核糖核酸以及它们的修饰物，包括双链或单链的DNA、cDNA、RNA、mRNA等，其可为环状也可为线性，也可为环状载体中的一部分或基因组中的一个片段。
本发明中，所述“核酸载体”是指重组DNA分子，其包含期望的编码序列和对可操作连接的编码基因在具体宿主生物内的表达所必不可少的合适的核酸序列。对原核细胞中的表达必需的核酸序列包括启动子，任选包括操纵基因序列，核糖体结合位点及可能的其它序列。已知原核细胞利用启动子，增强子以及终止和多腺苷酸化信号。一经转化进入合适的宿主，载体可以独立于宿主基因组进行复制和发挥作用，或者，在一些情况下，自己整合进入基因组。在本说明书中，“质粒”和“载体”有时可以交换通用，因为质粒是当前最普遍使用的载体形式。然而，本发明意图包括表达载体的这样的其它形式，其发挥等价作用，其在本领域是已知的或将变为已知的，包括但不限于：质粒，噬菌体颗粒，病毒载体和/或仅为潜在的基因组插入物。
本发明中，“宿主细胞”一般为含有核酸载体和/或感兴趣基因的原核或真核宿主。用使用重组DNA技术构建的载体转化或转染宿主细胞。这样的转化宿主细胞有能力复制编码蛋白质的载体或表达期望蛋白质。
本发明中，所述治疗性抗体是指能够通过中和作用、示踪或导向作用、竞争性抑制作用/拮抗作用、抗体依赖性细胞街道的细胞毒效应及补体依赖性细胞溶解作用、通过内影像作用模拟抗原等机制发挥治疗作用的抗体。
本发明中，所述免疫学检测是应用免疫学基本原理——抗原抗体反应，即抗原与抗体特异性结合的原理，通过化学反应使标记抗体的显色剂(荧光素、酶、金属离子、同位素)显色，来对定性、定量或定位研究细胞内抗原(多肽和蛋白质)，或抗体的技术，这样的技术包括但不限于酶联免疫分析法、免疫荧光、放射免疫分析法、免疫印迹、免疫组化、免疫共沉淀、染色质共沉淀等。
本发明中，所述固相支持物是指本文所述的抗原表位、特异性抗体和/或抗原蛋白能够附着至其上的任何支持物，包括但不限于硝酸纤维素膜、聚偏二氟乙烯(PVDF)膜、iPDMS芯片、微孔板、微粒、微载体、凝胶等。
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
一、本发明通过对31例EBV感染的肿瘤组织进行全基因组测序，检测其中EBV病毒片段。从NCBI库中120余株病毒中选取一株作为参考核酸序列，通过序列比对，确定病毒保守序列(核酸序列如SEQ ID NO：4所示，蛋白序列如SEQ ID NO：3所示)，
2、比较不同EB病毒株之间BALF3基因碱基序列及氨基酸序列的保守性(图1)，结果表明，在Human gamma herpesvirus 4中，分析基因的特异性不同病毒株BALF3序列与上述参考序列间相似性高达99％，考虑到病毒基因组具有较高的可变性，本申请基于相对保守的全外显子序列，筛选BALF3抗原区段。以该区段序列为基础设计制备的抗体具有较可靠的检测效力，可避免因感染病毒株亚型不同引起的假阴性结果。
3、比较临床样本中EB病毒株序列与上述参考序列间的保守性(图2)：NK/T细胞淋巴瘤发病与EB病毒感染密切相关。通过对31例EB病毒阳性的NK/T细胞淋巴瘤患者的WGS数据进行分析检测其中EB病毒序列，提取BALF3的序列信息，标识单个核苷酸变异位点及氨基酸变异位点，与B95-8参考序列进行比对，标识变化氨基酸。
二、蛋白可表达性分析
(1)跨膜结构分析：无跨膜结构
(2)翻译后修饰：暂无
(3)保守结构域(图2)
(4)二级结构预测(图3)
三、蛋白抗原性分析
(1)抗原表位预测(图4)
(2)抗原区域选择
-510-700aa(SEQ ID NO：1)：该区段不含突变氨基酸位点，免疫原性较好二级结构稳定易于表达，构到pGEX4T-AB1载体，采用大肠杆菌原核系统表达蛋白制备抗原。
四、抗体合成和功效验证
(1)抗原表达质粒制备
BALF3(510-700aa)PCR产物电泳鉴定大小正确(图5)，成功克隆到pGEX-4T-AB1载体上，并测序鉴定正确。
(2)抗原蛋白表达
重组质粒转化入表达菌株E.coli Rosetta，表达诱导条件：培养到OD600nm 0.5-0.6加入0.8mM IPTG 37℃诱导4小时
结果鉴定(图6)：
1.pGEX-4T-AB1-BALF3(510-700aa)表达在包涵体中。
2.包涵体纯化后蛋白浓度为0.6mg/mL，纯度达到免疫要求。
(3)兔免疫
流程如表1：
表1免疫流程
| 免疫次数 | 免疫周期 | 免疫剂量 | 免疫佐剂 | 免疫动物状态 |
| 第一次免疫 | 1天 | 0.3mg | 完全弗氏佐剂 | 良好 |
| 第二次免疫 | 12天 | 0.15mg | 不完全弗氏佐剂 | 良好 |
| 第三次免疫 | 26天 | 0.15mg | 不完全弗氏佐剂 | 良好 |
| 第四次免疫 | 40天 | 0.15mg | 不完全弗氏佐剂 | 良好 |
| 免疫动物采血 | 52天 | 采血正常 |
(4)抗血清ELISA检查，设置不添加抗体或血清的空白对照组，以及添加抗体但不添加血清的阴性对照，以及添加血清以及不同浓度抗体的实验组。实验采用上述构建获得的两株抗体，分别记为BALF3-E11787、BALF3-E11788，检测结果如图7。结果表明，两株抗体皆表现出良好效价。
(5)抗血清纯化
-亲和纯化用pGEX-4T-AB1-BALF3蛋白经检测，浓度为0.5mg/ml，与破菌纯化后浓度和纯度差异不大，可进行抗原亲和纯化。
-抗血清用pGEX-4T-AB1-BALF3蛋白作抗原亲和纯化后，得到浓缩后的抗体：E11797浓度为2.65mg/ml、E11798浓度为2.78mg/ml
(6)抗原western blot检测
利用纯化后的抗体对抗原进行检测，结果如图8，结果表明：
①、E11797、E11798抗体检测抗原条带大小在49KD左右；
②、E11797、E11798抗体1∶1000稀释可检测到500pg抗原；
③、E11797、E11798抗体浓度正常。
如上结果表明，本发明设计获得的抗原表位能够特异性的检测BALF3蛋白，且抗体具有良好的效价。
(7)特异性验证
以上述抗体对于人类细胞株裂解蛋白样本进行检测，检测结果为阴性(图9)，如图所示，BALF3理论大小为74,764Da，红色方框中所示应为目的蛋白的印记。B95-8为可分泌EBV的细胞株，可检测到内源性表达BALF3(阳性对照)，SNK6无EBV成分细胞株未检测到BALF3(阴性对照)。
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。
序列表
<110> 上海交通大学医学院附属瑞金医院
<120> EB病毒BALF3蛋白的抗原表位
<130> MP1914455
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Claims (6)
1.EB病毒BALF3蛋白的抗原表位肽，其如SEQ ID NO:1所示。
2.编码权利要求1所述抗原表位的核酸分子。
3.一种核酸载体，其包含权利要求2所述的核酸分子。
4.一种重组宿主，其包含权利要求3所述的核酸载体。
5.表达权利要求4所述重组宿主获得的抗原蛋白。
6.权利要求5所述的抗原蛋白在制备防治EB病毒引起疾病的治疗性抗体和/或疫苗中的应用。
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| WO2018187356A2 (en) * | 2017-04-03 | 2018-10-11 | Neon Therapeutics, Inc. | Protein antigens and uses thereof |
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