SARS冠状病毒S蛋白抗原表位分析与定位研究
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摘要
严重急性呼吸综合症(Severe acute respiratory syndrome, SARS)是由SARS冠状病毒(SARS-CoV)引起的人类新发传染病,S、M、N、E蛋白是SARS-CoV病毒粒子的几种主要结构蛋白。用Lasergene软件系统分析SARS病毒结构蛋白S、M、N蛋白,预测了12个抗原表位,用这些预测表位序列设计组合成四个嵌合基因SSCV-A、SSCV-B、SSCV-C、SSCV-D。人工合成后插入pGEX-6p-1的BamHI和XhoI位点间,构建成融合表达质粒,转化宿主菌BL21经IPTG诱导后嵌合基因表达产物为可溶性蛋白。经免疫印迹试验表明嵌合基因表达产物可被SARS康复患者血清所识别,表明重组融合蛋白具有免疫反应性,提示预测表位中含有SARS-CoV结构蛋白的抗原表位。用纯化的重组融合蛋白GST-SSCV-D和GST-SSCV-A为抗原制备了一系列单克隆抗体。抗SSCV-D的单抗有两株,分别为D3D1和D3C5。将6个S蛋白预测表位分别与GST融合表达。在这6个融合蛋白中,GST-S5可以和单克隆抗体D3C5反应,GST-S2可以和单抗D3D1反应。Western blot分析表明两个单抗所识别的表位均为线性表位。两个表位分别位于SARS-CoV纤突蛋白的第447至458氨基酸残基和789至799氨基酸残基。D3D1表位(447～458)正位于S蛋白与受体结合的结构域中。
2C5是一株SARS-CoV S蛋白特异的有中和活性的单克隆抗体。以2C5为筛选靶分子,筛选噬菌体展示随机7肽库。经三轮淘洗后随机挑选20个噬菌体克隆进行ELISA分析和序列测定。在10个ELISA OD值大于0.2的阳性噬菌体克隆中,有8个噬菌体克隆展示有共同的7肽序列TPEQQFT。展示有该序列的噬菌体克隆能竞争抑制SARS-CoV S蛋白抗原与单抗2C5的结合。与SARS-CoV S蛋白序列比对分析发现该7肽序列散布于S蛋白的第539位到第559位氨基酸上。将S蛋白T_(539)PSSKRFQPFQQFGRDVSDFT_(559)的21肽与GST进行融合表达,得到了可溶解的融合蛋白。该融合蛋白能不能被单抗2C5识别,但经Western blot分析表明该融合蛋白能被灭活SARS冠状病毒免疫鸡血清识别。表明T_(539)PSSKRFQPFQQFGRDVSDFT_(559)是S蛋白的一个线性表位,而TPEQQFT为单克隆抗体2C5的模拟表位。
SARS冠状病毒S蛋白在病毒与宿主细胞受体结合、细胞膜融合及入侵、诱导机体产生中和抗体中起重要作用。S蛋白受体结合结构域的核心区域为318～510片段。克隆并融合表达了S蛋白318～510片段,分析表明原核表达的受体结合结构域融合蛋白能被SARS康复患者清和高免动物血清所识别。进一步设计了一套23个覆盖整个该受体结合结构域的长为16氨基酸残基的部分重叠的短肽,并进行了融合表达。用23个融合蛋白对受体结合结构域进行抗原表位作图。结果鉴定出两个抗原表位SRBD3(F_(334)PSVYAWERKKISNCV_(349))和表位D3D1(K_(447)LRPFERDI_(455))。
SARS冠状病毒S蛋白S1部分在与细胞受体结合以及诱导机体产生保护性中和抗体中发挥重要作用。用PCR扩增S1(12～672)及S1N(12～510),S1C(318～672)和SRBD(318～510)四个片段。PCR产物分别克隆到表达载体pGEX-6p-1中,经诱导各融合蛋白均以包涵体形式表达。Western
Severe acute respiratory syndrome (SARS) is a newly emerged human infectious disease caused by the severe acute respiratory syndrome coronavirus (SARS-CoV). And the S, M, N and E protein are four main structural proteins of SARS-CoV. The spike (S) protein of SARS-CoV is a major virion structural protein. It plays an important role in the interaction with receptors and neutralizing antibodies. In the study, six epitopes (S1 S2 S3 S4 S5 S6) of the spike protein of SARS-CoV were predicted by bioinformatics analysis. Firstly, a multi-epitopes chimeric antigen gene was constructed and synthesized. The chimeric antigen gene then fused to downstream GST gene in pGEX-6p-1. The western blot assay demonstrated that SARS patient convalescent serum could recognize the recombinant fusion protein. And six predicted epitopes gene fused to GST expressed in E.coli BL21 respectively. Among six fusion proteins, GST-S5 reacted with monoclonal antibody D3C5 and GST-S2 reacted with monoclonal antibody D3D1 against spike protein of SARS-CoV. The results indicated that the epitopes recognized by monoclonal antibody D3C5 and D3D1 are all lineal epitopes. The two epitopes correspond the sequence of 447 to 458 and 789-799 amino acid of spike protein of SARS-CoV respectively.2C5 is a SARS-CoV spike protein specific neutralizing monoclonal antibody. Based 2C5 as the target molecular, C7C? phage display peptide library were screened. After the third panning 20 phage clones were analyzed and sequenced. Among these 20 clones, there are 7 get the same sequence TPEQQFT and their OD value in ELISA are all over 0.2. And the phages displayed this peptide could inhibit and compete with SARS-CoV spike protein in binding with monoclonal antibody 2C5. Align the peptide with spike protein sequence, we found it may located in amino acid 539 to 559 of spike protein. In further step S539-559 was fused with GST and expressed and purified. But the followed analysis demonstrated that 2C5 did not binding with S539-559. However, this fusion protein could be recognized by immunized chicken sera. So S539-559 is a lineal epitope of spike protein, but not the epitope of 2C5. And the sequence TPEQQFT is a mimic epitope of monoclonal antibody 2C5.Amino acid 318 to 510 is the receptor binding domain of SARS-CoV spike protein. To map the antigenic epitope of this region, a set of 23 partially overlapping fragments spanning the fragment were fused with GST and expressed. With Western blot and ELISA analysis, two antigenic epitopes SRBD3 (334-349) and epitope D3D1 (447-455) were identified. Immunization of mice with each of the two antigenic epitope-fused proteins revealed that all four proteins could elicit spike protein specific antisera.
2C5是一株SARS-CoV S蛋白特异的有中和活性的单克隆抗体。以2C5为筛选靶分子,筛选噬菌体展示随机7肽库。经三轮淘洗后随机挑选20个噬菌体克隆进行ELISA分析和序列测定。在10个ELISA OD值大于0.2的阳性噬菌体克隆中,有8个噬菌体克隆展示有共同的7肽序列TPEQQFT。展示有该序列的噬菌体克隆能竞争抑制SARS-CoV S蛋白抗原与单抗2C5的结合。与SARS-CoV S蛋白序列比对分析发现该7肽序列散布于S蛋白的第539位到第559位氨基酸上。将S蛋白T_(539)PSSKRFQPFQQFGRDVSDFT_(559)的21肽与GST进行融合表达,得到了可溶解的融合蛋白。该融合蛋白能不能被单抗2C5识别,但经Western blot分析表明该融合蛋白能被灭活SARS冠状病毒免疫鸡血清识别。表明T_(539)PSSKRFQPFQQFGRDVSDFT_(559)是S蛋白的一个线性表位,而TPEQQFT为单克隆抗体2C5的模拟表位。
SARS冠状病毒S蛋白在病毒与宿主细胞受体结合、细胞膜融合及入侵、诱导机体产生中和抗体中起重要作用。S蛋白受体结合结构域的核心区域为318～510片段。克隆并融合表达了S蛋白318～510片段,分析表明原核表达的受体结合结构域融合蛋白能被SARS康复患者清和高免动物血清所识别。进一步设计了一套23个覆盖整个该受体结合结构域的长为16氨基酸残基的部分重叠的短肽,并进行了融合表达。用23个融合蛋白对受体结合结构域进行抗原表位作图。结果鉴定出两个抗原表位SRBD3(F_(334)PSVYAWERKKISNCV_(349))和表位D3D1(K_(447)LRPFERDI_(455))。
SARS冠状病毒S蛋白S1部分在与细胞受体结合以及诱导机体产生保护性中和抗体中发挥重要作用。用PCR扩增S1(12～672)及S1N(12～510),S1C(318～672)和SRBD(318～510)四个片段。PCR产物分别克隆到表达载体pGEX-6p-1中,经诱导各融合蛋白均以包涵体形式表达。Western
Severe acute respiratory syndrome (SARS) is a newly emerged human infectious disease caused by the severe acute respiratory syndrome coronavirus (SARS-CoV). And the S, M, N and E protein are four main structural proteins of SARS-CoV. The spike (S) protein of SARS-CoV is a major virion structural protein. It plays an important role in the interaction with receptors and neutralizing antibodies. In the study, six epitopes (S1 S2 S3 S4 S5 S6) of the spike protein of SARS-CoV were predicted by bioinformatics analysis. Firstly, a multi-epitopes chimeric antigen gene was constructed and synthesized. The chimeric antigen gene then fused to downstream GST gene in pGEX-6p-1. The western blot assay demonstrated that SARS patient convalescent serum could recognize the recombinant fusion protein. And six predicted epitopes gene fused to GST expressed in E.coli BL21 respectively. Among six fusion proteins, GST-S5 reacted with monoclonal antibody D3C5 and GST-S2 reacted with monoclonal antibody D3D1 against spike protein of SARS-CoV. The results indicated that the epitopes recognized by monoclonal antibody D3C5 and D3D1 are all lineal epitopes. The two epitopes correspond the sequence of 447 to 458 and 789-799 amino acid of spike protein of SARS-CoV respectively.2C5 is a SARS-CoV spike protein specific neutralizing monoclonal antibody. Based 2C5 as the target molecular, C7C? phage display peptide library were screened. After the third panning 20 phage clones were analyzed and sequenced. Among these 20 clones, there are 7 get the same sequence TPEQQFT and their OD value in ELISA are all over 0.2. And the phages displayed this peptide could inhibit and compete with SARS-CoV spike protein in binding with monoclonal antibody 2C5. Align the peptide with spike protein sequence, we found it may located in amino acid 539 to 559 of spike protein. In further step S539-559 was fused with GST and expressed and purified. But the followed analysis demonstrated that 2C5 did not binding with S539-559. However, this fusion protein could be recognized by immunized chicken sera. So S539-559 is a lineal epitope of spike protein, but not the epitope of 2C5. And the sequence TPEQQFT is a mimic epitope of monoclonal antibody 2C5.Amino acid 318 to 510 is the receptor binding domain of SARS-CoV spike protein. To map the antigenic epitope of this region, a set of 23 partially overlapping fragments spanning the fragment were fused with GST and expressed. With Western blot and ELISA analysis, two antigenic epitopes SRBD3 (334-349) and epitope D3D1 (447-455) were identified. Immunization of mice with each of the two antigenic epitope-fused proteins revealed that all four proteins could elicit spike protein specific antisera.
引文
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