抗鹅细小病毒VP3蛋白单克隆抗体的制备及对应抗原表位的定位
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摘要
小鹅瘟(Gosling plague,GP)又名鹅细小病毒病,是由鹅细小病毒(Goose Parvovirus,GPV)引起雏鹅、雏番鸭以急性肠炎及肝、肾、心实质器官炎症为特征的烈性传染病。GPV的致病性强,致死率高,对养鹅业的影响严重,造成巨大的经济损失。由于本病长期困扰着养鹅业,因此制备单克隆抗体,并对相应抗原表位进行定位对本病的诊断和防治有重要意义。GPV VP3蛋白是鹅细小病毒的主要结构蛋白,也是病毒的主要衣壳蛋白,暴露于病毒粒子表面,含有GPV主要抗原决定簇,是GPV主要免疫保护性抗原,约占总蛋白的80%。因其能刺激机体产生具有中和作用的抗体,是研制基因工程重组疫苗的首选蛋白。通过免疫VP3蛋白制备抗GPV VP3的单克隆抗体,并利用单克隆抗体对GPV VP3的B细胞抗原表位进行定位,有助于了解其抗原结构与功能的关系,在小鹅瘟病的胶体金、ELISA等临床和实验室检测方法的建立,疫苗研制,疾病治疗等方面起到重要作用。
本实验利用Ni-NTA亲和层析纯化后的GPV VP3重组蛋白作为免疫原,经腹腔接种免疫4~6周龄BALB/c小鼠3次,末次免疫3d后取小鼠脾细胞与SP2/0骨髓瘤细胞融合,利用已建立的间接ELISA方法进行筛选,经有限稀释法进行4次亚克隆,最终获得4株能稳定分泌抗GPV VP3单克隆抗体的杂交瘤细胞株,分别命名为1F1、2A9、3B11、4A2。亚类鉴定1F1为IgG2b亚类,其余3株为IgG1亚类,轻链均为κ链。ELISA检测,其腹水效价分别达到1:819 200、1:1 638 400、1:409 600、1:819 200。Western blot鉴定表明获得的4株单抗均能特异性识别GPV VP3重组蛋白和GPV VP3天然蛋白;免疫电镜和间接免疫荧光证明4株单抗能够与GPV全病毒结合。
根据实验室已鉴定的GPV VP3蛋白线性抗原表位区结果,设计并合成互相重叠5个氨基酸的10aa短肽寡聚核酸片段,退火后,连入pET-32a载体,诱导表达获得相应的小片段融合蛋白,利用制备的单抗通过Western blot进行抗原性鉴定。同样方法进行短肽片段两端氨基酸的逐个缺失,进一步定位出两个抗原表位为430~435aa和643~647aa。
本研究制备了抗GPV VP3单克隆抗体,并对相应B细胞抗原表位进行了定位。为建立以表位为基础的抗原抗体诊断方法提供了物质基础,对设计新型GPV亚单位疫苗等方面具有重要意义,单抗和抗原表位均为GPV后续实验奠定物质基础,为其联合应用提供广泛的应用前景。
Gosling plague also known as Goose Parvovirus (GPV) infection, causes domestic goslings and Muscovy ducklings with chordapsus and liver, kidney, the heart substance organ inflamm violent contagious disease. GPV has high pathogenicity and lethality, makes severity effect to goose-producing countries, and causes huge economic loss. Owing to the hindrance to the development of goose cultural industry because of the disease, there needs Monoclonal Antibodies (McAb) and epitope for diagnosis and prevention. VP3 is the main structural protein of GPV, and also the main capsid protein, exposing the superficies of the nucleocapsid, contains GPV main antigen determinant, and it is the immune protective antigen of GPV, 80% of total protein. Because it can excite neutralization antibody, it is the preferred protein to develop genetic engineering recombinate vaccine. Preparation of McAb against VP3 protein and the location of linear B-cell epitope with McAbs will conduce to understand the relation of antigenic structure and function. It plays an important role in locating linear B-cell epitope of VP3, setting up gold colloid and ELISA clinical detect methods of gosling plague. It is also important for vaccine development, disease management and so on.
The recombinant protein GPV VP3 was used as immunogen after purification by Ni-NTA. The 4 to 6 weeks-old BALB/c mice were intraperitoneally immunized with the VP3 protein for three times, then myeloma cells SP2/0 were fused with the spleen cells of the immunized BALB/c mice on day 3 post-last-immunization. Four hybridoma cell lines against the VP3 protein were obtained by screening with the indirect ELISA, named 1F1, 2A9, 3B11, 4A2, respectively. The first McAbs were identified to be IgG2b, and the others to be IgG1 withκlight chain. The ELISA titer of the 4 McAbs ascites were 1:819 200, 1:1 638 400, 1:409 600, 1:819 200, respectively. Western-blot analysis showed that the four McAbs could react with GPV VP3 recombinant protein and GPV native protein VP3 specifically, and the four McAbs could combine with GPV certified by IFA and immunoelectron microscopy.
On the basis of the epitopes results of GPV VP3 protein which have already been identified in previous study, oligomeric nucleic acid fragments of ten amino acid fragments mutually coinciding five amino acids were contrived, after annealing, connected with pET-32a, derivation expressed, small fragment fusion proteins were gained. The antigenicity were identified by Western blot. With the same method, amino acids were deleted one by one, and two epitopes were located at 430-435aa and 643-647aa.
This study has prepared McAbs against protein GPV VP3 and located the epitope of them. It has a significant meaning for early diagnosis and designing the safe and effective genetic engineering epitide vaccine against GPV on the basis of the molecule level of epitopes. McAbs and epitope will be used as material foundation for the further experiment of GPV, and will also offer far-reaching prospect for their association.
本实验利用Ni-NTA亲和层析纯化后的GPV VP3重组蛋白作为免疫原,经腹腔接种免疫4~6周龄BALB/c小鼠3次,末次免疫3d后取小鼠脾细胞与SP2/0骨髓瘤细胞融合,利用已建立的间接ELISA方法进行筛选,经有限稀释法进行4次亚克隆,最终获得4株能稳定分泌抗GPV VP3单克隆抗体的杂交瘤细胞株,分别命名为1F1、2A9、3B11、4A2。亚类鉴定1F1为IgG2b亚类,其余3株为IgG1亚类,轻链均为κ链。ELISA检测,其腹水效价分别达到1:819 200、1:1 638 400、1:409 600、1:819 200。Western blot鉴定表明获得的4株单抗均能特异性识别GPV VP3重组蛋白和GPV VP3天然蛋白;免疫电镜和间接免疫荧光证明4株单抗能够与GPV全病毒结合。
根据实验室已鉴定的GPV VP3蛋白线性抗原表位区结果,设计并合成互相重叠5个氨基酸的10aa短肽寡聚核酸片段,退火后,连入pET-32a载体,诱导表达获得相应的小片段融合蛋白,利用制备的单抗通过Western blot进行抗原性鉴定。同样方法进行短肽片段两端氨基酸的逐个缺失,进一步定位出两个抗原表位为430~435aa和643~647aa。
本研究制备了抗GPV VP3单克隆抗体,并对相应B细胞抗原表位进行了定位。为建立以表位为基础的抗原抗体诊断方法提供了物质基础,对设计新型GPV亚单位疫苗等方面具有重要意义,单抗和抗原表位均为GPV后续实验奠定物质基础,为其联合应用提供广泛的应用前景。
Gosling plague also known as Goose Parvovirus (GPV) infection, causes domestic goslings and Muscovy ducklings with chordapsus and liver, kidney, the heart substance organ inflamm violent contagious disease. GPV has high pathogenicity and lethality, makes severity effect to goose-producing countries, and causes huge economic loss. Owing to the hindrance to the development of goose cultural industry because of the disease, there needs Monoclonal Antibodies (McAb) and epitope for diagnosis and prevention. VP3 is the main structural protein of GPV, and also the main capsid protein, exposing the superficies of the nucleocapsid, contains GPV main antigen determinant, and it is the immune protective antigen of GPV, 80% of total protein. Because it can excite neutralization antibody, it is the preferred protein to develop genetic engineering recombinate vaccine. Preparation of McAb against VP3 protein and the location of linear B-cell epitope with McAbs will conduce to understand the relation of antigenic structure and function. It plays an important role in locating linear B-cell epitope of VP3, setting up gold colloid and ELISA clinical detect methods of gosling plague. It is also important for vaccine development, disease management and so on.
The recombinant protein GPV VP3 was used as immunogen after purification by Ni-NTA. The 4 to 6 weeks-old BALB/c mice were intraperitoneally immunized with the VP3 protein for three times, then myeloma cells SP2/0 were fused with the spleen cells of the immunized BALB/c mice on day 3 post-last-immunization. Four hybridoma cell lines against the VP3 protein were obtained by screening with the indirect ELISA, named 1F1, 2A9, 3B11, 4A2, respectively. The first McAbs were identified to be IgG2b, and the others to be IgG1 withκlight chain. The ELISA titer of the 4 McAbs ascites were 1:819 200, 1:1 638 400, 1:409 600, 1:819 200, respectively. Western-blot analysis showed that the four McAbs could react with GPV VP3 recombinant protein and GPV native protein VP3 specifically, and the four McAbs could combine with GPV certified by IFA and immunoelectron microscopy.
On the basis of the epitopes results of GPV VP3 protein which have already been identified in previous study, oligomeric nucleic acid fragments of ten amino acid fragments mutually coinciding five amino acids were contrived, after annealing, connected with pET-32a, derivation expressed, small fragment fusion proteins were gained. The antigenicity were identified by Western blot. With the same method, amino acids were deleted one by one, and two epitopes were located at 430-435aa and 643-647aa.
This study has prepared McAbs against protein GPV VP3 and located the epitope of them. It has a significant meaning for early diagnosis and designing the safe and effective genetic engineering epitide vaccine against GPV on the basis of the molecule level of epitopes. McAbs and epitope will be used as material foundation for the further experiment of GPV, and will also offer far-reaching prospect for their association.
引文
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