SARS-CoV N蛋白功能的分子机制和作为抗原在SARS诊断上的应用
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摘要
PhD candidate: Khalid Amine Timani ID No. 2001193004 Academic Supervisor: ProfLinbai Ye Sate Key lab of Virology, College of Life Sciences, Wuhan University
2003年,非典型性肺炎在全世界30多个国家广泛流行,给人类健康带来了极大的威胁和伤害。2003年4月16日,WHO正式确定非典型性肺炎的病原体是冠状病毒家族中的一个变种,将此病毒正式命名为“SARS病毒”。虽然目前没有新的SARS疫情发生,但是SARS仍然对全人类的健康存在着威胁。因此,对SARS病毒的实验研究将有助于了解SARS疾病的传播以及感染机制和控制SARS疾病。
武汉大学生命科学学院从湖北SARS病人血清中分离到了SARS冠状病毒湖北株SARS-CoV(Hubei)。我们对该毒株的核衣壳蛋白(Nucleocapsid protein,N protein)的基因序列进行了测序(序列已提交至基因库Genbank,序号为AY365036),并使用DNAStar软件对SARS-CoV(Hubei)的N蛋白的基因序列同在中国北京、广东、浙江、香港和台湾分离出的其他11株SARS病毒的N蛋白的基因序列,以及加拿大、新加坡、意大利、德国和美国的SARS病毒的N蛋白的基因序列进行了对比。序列对比的结果表明,N蛋白基因序列上出现了两处碱基替代,分别是第284个核苷酸由T变为C和第689个核苷酸由A变为G。这两处的碱基替代都是错义突变,均导致了蛋白质氨基酸序列的改变,即在N蛋白的氨基酸序列上的第95个氨基酸由缬氨酸突变为丙氨酸,第230个氨基酸由精氨酸突变为谷氨酸。
由于非典型性肺炎有极高的传染性,因此发展在SARS冠状病毒感染早期的诊断技术是当务之急。我们应用PCR技术从已有的pGEMT-N质粒中扩增获得长度约为1.2kb的N基因序列,并将此DNA序列克隆到原核表达载体pET-His中,将重组质粒pET-His-N转化大肠杆菌BL21(DE3)后,IPTG诱导使其在大肠杆菌中表达,收集菌体,超声波振荡裂解菌体,用Ni-NTA-Superflow亲和层析柱从裂解液中纯化N蛋白,SDS-PAGE检测N蛋白纯化情况。我们用纯化的重组N蛋白作为抗原,用ELISA检测16份已确诊的非典型性肺炎病人阳性血清和131份正常人阴性血清的SARS冠状病毒特异性IgG抗体。发病10天的SARS病人血清的阳性检出率是81.3%(13/16),发病20天的SARS病人血清的阳性检出率是100%(16/16),发病30天的SARS病人血清的阳性检出率是100%(16/16),阴性血
The sudden outbreak of the human severe acute respiratory syndrome (SARS) in 2002 prompted the establishment of a global scientific network subsuming most of the traditional rivalries in the competitive field of virology. Within months of the SARS outbreak, collaborative work revealed the identity of the disastrous pathogen as SARS-associated coronavirus (SARS-CoV). Even in a situation of no new infections, SARS remains a major health hazard, as new epidemics may arise. Therefore, further experimental and clinical research is required to understand its infectious mechanism and control the disease.Given the highly contagious and acute nature of the disease, there is an urgent need for development of diagnostic assays that can detect SARS-CoV infection, more importantly, at its early stages. One important viral protein that can serve this goal is nucleocapsid (N) due to its high antigenic nature. The N protein gene sequence of SARS-CoV Hubei isolate strain was performed and the sequence was deposited to the Genbank accession number (AY365036). The N protein gene sequence alignment with N protein of eleven isolates from different regions in China (Beijing, Guangzhu and Zhejiang, Hong Kong and Taiwan) and other countries (Canada, Singapore, Italy, Germany and USA) revealed two basses substitution in N protein gene. These nucleotide changes were located at positions 284 and 689 from (T to C) and (A to G), respectively. The changes were non-synonymous and resulted in amino aids changes, valine to alanine and arginine to glutamine, at amino acid positions 95 and 230 of the N protein, respectively.The full length of N protein is 422 amino acids (aa) with an amino-terminal hexahistidine-tag was expressed in E.coli system, BL21(DE3), and purified by Ni-NTA affinity column chromatography to homogeneity. Recombinant purified SARS-CoV N protein was employed to establish an antigen-capturing enzyme linked immunosorbent assay (ELISA) and used to measure the SARS-CoV specific IgG antibodies from 16 SARS-CoV infected patients' sera and from 131 control subjects. Specific antibody responses to the purified recombinant N protein after 10, 20, and 30 days of disease onset were observed in 13 of 16 (81.3%), 16 of 16 (100%) and L6 of 16 (100%) Comparison of detection results with a commercially available diagnostic kit coated with a mixture of
SARS-CoV viral proteins showed 9 of 16 (56.3%), 13 of 16 (81.3%), and 15 of 16 (93.7%) positive responses, respectively. None of 131 control sera subjects gave positive reaction in either assay. This data suggests that the N protein of SARS-CoV is immunodominant and this ELISA based test assay for detecting the SARS-CoV N antigen may hold a significant value for SARS diagnosis.Understanding the intracellular localization properties on N protein might shed light on its molecular mechanism during SARS infection and its possible role in SARS pathogenesis. Although coronaviruses and arteriviruses encode N protein whose principle function is to bind viral RNA, the proteins themselves are of a different size and have no discernable homology. However, an identical nucleolar-cytoplasmic localization pattern is observed. In this study, we further investigated whether this nucleolar localization pattern extends to SARS-CoV N protein. Rabbit polyclonal antibody specific for the purified N protein was generated and used to examine its intracellular localization using confocal microscopy. PSORT II program sequence analysis of the N protein identified three classical putative nuclear localization signal (NLS) motifs, labeled NLS1, NLS2 and NLS3 located at positions aa34-44, aa257-265 and aa369-390, respectively. The indirect immunofluorescence staining showed that wild type N protein localized mainly to the cytoplasm in Vero E6 infected with SARS-CoV and Vero E6, Vero and HeLa cells transfected with plasmid expressing full length N protein, and was not clear in the nucleolus.Intriguingly, the expression of C-terminal N protein was found in the cytoplasm and nucleus, concentrated in the nucleolus. This feature was confirmed to the nucleolus by using specific monoclonal antibody to nucleolar shuttling phosphorprotein B23. The results of various deletion mutants either alone or fused to enhanced green fluorescent protein (EGFP) showed that the region covering aa232-289 and overlapping NLS2 is responsible for this nucleolar localization and might considered as nucleolar localization signal (NoLS). Furthermore, deletion of leucine rich region (LRR; 220-LALLLLDRLNRL) resulted in the accumulation of N protein to the cytoplasm and nucleolus, and when fusing this peptide to EGFP localization was cytoplasmic, suggesting that the N protein may act as a shuttle protein. Leptomycin B treatment, a know inhibitor to the nuclear export signal (NES)-CRMl pathway has no effect on the localization pattern of full length N protein demonstrating that N protein maybe export via NES-CRM1 independent pathway or LRR may act as a masking signal. In addition, flow cytometric analysis and colony formation efficiency assays demonstrated that constitutive N-expressing Vero E6 cells exhibited cell growth retardation concomitantly
with prolonged Go/Gi phase and shortened S phase of the cell cycle compared with control cells. Taken together, these results demonstrated that N protein may act as a nucleolar-cytoplasmic shuttling protein and the localization to the nucleus/nucleolus implies that N protein maybe involved in the regulating of cell cycle, possibly by delaying the cell growth, to promote intracellular conditions for virus assembly and sequestering ribosomes for translation of viral proteins.Patients with SARS usually have rapid progression of pneumonitis. Approximately one-third of SARS patients developed (Acute Respiratory Distress Syndrome, ARDS), one-tenth of the patients succumbed to death and one-tenth of patients revealed pulmonary fibrosis. The mechanisms of SARS-CoV infection caused atypical pneumonia remain unclear. Nuclear factor-kB (NF-kB) is a critical regulator of the immediate early pathogen response, playing an important role in promoting inflammation and in the regulation of cell proliferation and survival; moreover, many studies have shown that NF-kB played an important role in the pathogenesis of lung disease. In this research study we further investigated the possible regulatory mechanism of SARS-CoV N protein and NF-kB by using luciferase reporter assay. Our result showed that SARS-CoV N protein can significantly activate NF-kB only in Vero E6 cells, but there is no such significant activation in Vero or HeLa cell lines compared with backbone vector, suggested that this NF-kB activation is cell type specific. Furthermore, this NF-kB activation in Vero E6 cells expressing-N protein was shown to be concentration dependent. Different deletion mutation of N protein revealed that conformation of full length N protein was crucial for the NF-kB activation. This unique function of SARS-CoV N protein from other members of coronavirus family postulated that N protein can be a good target for the development of vaccine and antiviral drugs.
2003年,非典型性肺炎在全世界30多个国家广泛流行,给人类健康带来了极大的威胁和伤害。2003年4月16日,WHO正式确定非典型性肺炎的病原体是冠状病毒家族中的一个变种,将此病毒正式命名为“SARS病毒”。虽然目前没有新的SARS疫情发生,但是SARS仍然对全人类的健康存在着威胁。因此,对SARS病毒的实验研究将有助于了解SARS疾病的传播以及感染机制和控制SARS疾病。
武汉大学生命科学学院从湖北SARS病人血清中分离到了SARS冠状病毒湖北株SARS-CoV(Hubei)。我们对该毒株的核衣壳蛋白(Nucleocapsid protein,N protein)的基因序列进行了测序(序列已提交至基因库Genbank,序号为AY365036),并使用DNAStar软件对SARS-CoV(Hubei)的N蛋白的基因序列同在中国北京、广东、浙江、香港和台湾分离出的其他11株SARS病毒的N蛋白的基因序列,以及加拿大、新加坡、意大利、德国和美国的SARS病毒的N蛋白的基因序列进行了对比。序列对比的结果表明,N蛋白基因序列上出现了两处碱基替代,分别是第284个核苷酸由T变为C和第689个核苷酸由A变为G。这两处的碱基替代都是错义突变,均导致了蛋白质氨基酸序列的改变,即在N蛋白的氨基酸序列上的第95个氨基酸由缬氨酸突变为丙氨酸,第230个氨基酸由精氨酸突变为谷氨酸。
由于非典型性肺炎有极高的传染性,因此发展在SARS冠状病毒感染早期的诊断技术是当务之急。我们应用PCR技术从已有的pGEMT-N质粒中扩增获得长度约为1.2kb的N基因序列,并将此DNA序列克隆到原核表达载体pET-His中,将重组质粒pET-His-N转化大肠杆菌BL21(DE3)后,IPTG诱导使其在大肠杆菌中表达,收集菌体,超声波振荡裂解菌体,用Ni-NTA-Superflow亲和层析柱从裂解液中纯化N蛋白,SDS-PAGE检测N蛋白纯化情况。我们用纯化的重组N蛋白作为抗原,用ELISA检测16份已确诊的非典型性肺炎病人阳性血清和131份正常人阴性血清的SARS冠状病毒特异性IgG抗体。发病10天的SARS病人血清的阳性检出率是81.3%(13/16),发病20天的SARS病人血清的阳性检出率是100%(16/16),发病30天的SARS病人血清的阳性检出率是100%(16/16),阴性血
The sudden outbreak of the human severe acute respiratory syndrome (SARS) in 2002 prompted the establishment of a global scientific network subsuming most of the traditional rivalries in the competitive field of virology. Within months of the SARS outbreak, collaborative work revealed the identity of the disastrous pathogen as SARS-associated coronavirus (SARS-CoV). Even in a situation of no new infections, SARS remains a major health hazard, as new epidemics may arise. Therefore, further experimental and clinical research is required to understand its infectious mechanism and control the disease.Given the highly contagious and acute nature of the disease, there is an urgent need for development of diagnostic assays that can detect SARS-CoV infection, more importantly, at its early stages. One important viral protein that can serve this goal is nucleocapsid (N) due to its high antigenic nature. The N protein gene sequence of SARS-CoV Hubei isolate strain was performed and the sequence was deposited to the Genbank accession number (AY365036). The N protein gene sequence alignment with N protein of eleven isolates from different regions in China (Beijing, Guangzhu and Zhejiang, Hong Kong and Taiwan) and other countries (Canada, Singapore, Italy, Germany and USA) revealed two basses substitution in N protein gene. These nucleotide changes were located at positions 284 and 689 from (T to C) and (A to G), respectively. The changes were non-synonymous and resulted in amino aids changes, valine to alanine and arginine to glutamine, at amino acid positions 95 and 230 of the N protein, respectively.The full length of N protein is 422 amino acids (aa) with an amino-terminal hexahistidine-tag was expressed in E.coli system, BL21(DE3), and purified by Ni-NTA affinity column chromatography to homogeneity. Recombinant purified SARS-CoV N protein was employed to establish an antigen-capturing enzyme linked immunosorbent assay (ELISA) and used to measure the SARS-CoV specific IgG antibodies from 16 SARS-CoV infected patients' sera and from 131 control subjects. Specific antibody responses to the purified recombinant N protein after 10, 20, and 30 days of disease onset were observed in 13 of 16 (81.3%), 16 of 16 (100%) and L6 of 16 (100%) Comparison of detection results with a commercially available diagnostic kit coated with a mixture of
SARS-CoV viral proteins showed 9 of 16 (56.3%), 13 of 16 (81.3%), and 15 of 16 (93.7%) positive responses, respectively. None of 131 control sera subjects gave positive reaction in either assay. This data suggests that the N protein of SARS-CoV is immunodominant and this ELISA based test assay for detecting the SARS-CoV N antigen may hold a significant value for SARS diagnosis.Understanding the intracellular localization properties on N protein might shed light on its molecular mechanism during SARS infection and its possible role in SARS pathogenesis. Although coronaviruses and arteriviruses encode N protein whose principle function is to bind viral RNA, the proteins themselves are of a different size and have no discernable homology. However, an identical nucleolar-cytoplasmic localization pattern is observed. In this study, we further investigated whether this nucleolar localization pattern extends to SARS-CoV N protein. Rabbit polyclonal antibody specific for the purified N protein was generated and used to examine its intracellular localization using confocal microscopy. PSORT II program sequence analysis of the N protein identified three classical putative nuclear localization signal (NLS) motifs, labeled NLS1, NLS2 and NLS3 located at positions aa34-44, aa257-265 and aa369-390, respectively. The indirect immunofluorescence staining showed that wild type N protein localized mainly to the cytoplasm in Vero E6 infected with SARS-CoV and Vero E6, Vero and HeLa cells transfected with plasmid expressing full length N protein, and was not clear in the nucleolus.Intriguingly, the expression of C-terminal N protein was found in the cytoplasm and nucleus, concentrated in the nucleolus. This feature was confirmed to the nucleolus by using specific monoclonal antibody to nucleolar shuttling phosphorprotein B23. The results of various deletion mutants either alone or fused to enhanced green fluorescent protein (EGFP) showed that the region covering aa232-289 and overlapping NLS2 is responsible for this nucleolar localization and might considered as nucleolar localization signal (NoLS). Furthermore, deletion of leucine rich region (LRR; 220-LALLLLDRLNRL) resulted in the accumulation of N protein to the cytoplasm and nucleolus, and when fusing this peptide to EGFP localization was cytoplasmic, suggesting that the N protein may act as a shuttle protein. Leptomycin B treatment, a know inhibitor to the nuclear export signal (NES)-CRMl pathway has no effect on the localization pattern of full length N protein demonstrating that N protein maybe export via NES-CRM1 independent pathway or LRR may act as a masking signal. In addition, flow cytometric analysis and colony formation efficiency assays demonstrated that constitutive N-expressing Vero E6 cells exhibited cell growth retardation concomitantly
with prolonged Go/Gi phase and shortened S phase of the cell cycle compared with control cells. Taken together, these results demonstrated that N protein may act as a nucleolar-cytoplasmic shuttling protein and the localization to the nucleus/nucleolus implies that N protein maybe involved in the regulating of cell cycle, possibly by delaying the cell growth, to promote intracellular conditions for virus assembly and sequestering ribosomes for translation of viral proteins.Patients with SARS usually have rapid progression of pneumonitis. Approximately one-third of SARS patients developed (Acute Respiratory Distress Syndrome, ARDS), one-tenth of the patients succumbed to death and one-tenth of patients revealed pulmonary fibrosis. The mechanisms of SARS-CoV infection caused atypical pneumonia remain unclear. Nuclear factor-kB (NF-kB) is a critical regulator of the immediate early pathogen response, playing an important role in promoting inflammation and in the regulation of cell proliferation and survival; moreover, many studies have shown that NF-kB played an important role in the pathogenesis of lung disease. In this research study we further investigated the possible regulatory mechanism of SARS-CoV N protein and NF-kB by using luciferase reporter assay. Our result showed that SARS-CoV N protein can significantly activate NF-kB only in Vero E6 cells, but there is no such significant activation in Vero or HeLa cell lines compared with backbone vector, suggested that this NF-kB activation is cell type specific. Furthermore, this NF-kB activation in Vero E6 cells expressing-N protein was shown to be concentration dependent. Different deletion mutation of N protein revealed that conformation of full length N protein was crucial for the NF-kB activation. This unique function of SARS-CoV N protein from other members of coronavirus family postulated that N protein can be a good target for the development of vaccine and antiviral drugs.
引文
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