家蚕生物反应器表达人GM-CSF的研究
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摘要
人粒细胞巨噬细胞集落刺激因子是一种在体外调控粒细胞、单核／巨噬细胞分化、增殖和存活的造血性糖蛋白细胞因子。本研究成功地利用家蚕核型多角体杆状病毒表达系统在家蚕蛹中表达并纯化出重组人粒细胞巨噬细胞集落刺激因子。
通过RT-PCR技术，我们利用一对特异引物从人胚纤维原细胞中扩增到人GM-CSF基因。将扩增的GM-CSF PCR产物用EcoRI和BamHI酶切后插入到同样酶切的家蚕杆状病毒转移载体pUBM-4中，从而构成了重组载体pBM-CSF。将该质粒与线性化的Bm-BacPAK6 DNA共转染家蚕细胞BmN，在培养的贴壁细胞中挑出空斑，经过3轮纯化，获得重组病毒vBm-CSF。
我们利用重组病毒vBm-CSF感染家蚕蛹来表达重组人粒细胞巨噬细胞集落刺激因子。经SDS-PAGE和Western blotting鉴定表明在重组病毒感染的家蚕蛹体内存在重组人粒细胞巨噬细胞集落刺激因子。表达产物分子量约为29kDa，在蚕蛹中的表达量约为97μg／蛹；在蚕蛹粗提物中的rhGM-CSF生物活性约为6.8×10~6cfu／mg。
与以前在家蚕细胞和幼虫中分泌表达的hGM-CSF相比，我们在家蚕蛹表达的hGM-CSF表现出较大的差异：分子量较大、表达量和生物活性偏低，这可能与蛋白的翻译后修饰有关。因而，有必要对蚕蛹表达的hGM-CSF进行大量表达和纯化以鉴定该表达产物的相关理化性质。为此，我们将重组病毒接种了大量的蚕蛹来表达hGM-CSF。通过硫酸铵分级沉淀、凝胶排阻过滤和离子交换层析多步纯化，最终我们以10.5％的得率从700头接种重组病毒的家蚕蛹中获得3.5mg纯度达97％的蚕蛹表达产物Bm-hGM-CSF。经检测，高纯度的表达产物Bm-hGM-CSF生物活性达约8.4×10~6cfs／mg。
对纯化的表达产物进行理化性质分析。等电聚焦电泳表明，家蚕蛹表达产物Bm-hGM-CSF等电点约为5.1，与家蚕细胞和幼虫中表达hGM-CSF很接近；肽谱分析发现，Bm-hGM-CSF与原核hGM-CSF在肽谱的表现上非常相似；去糖基化分析表明，Bm-hGM-CSF带有高甘露糖型糖链。这些情况表明，高度的高甘露糖化导致了Bm-hGM-CSF表现出较大差异。
To date, many recombinant proteins have been expressed in Bombyx mori cells or silkworm larvae, apart from in pupae. Silkworm pupae may be more suitable for the expression of heterologous proteins as a bioreactor. If maintained at an appropriate temperature, silkworm pupae could be inoculated with recombinant baculovirus for the expression of a protein of interest. In this study, human granulocyte-macrophage colony-stimulating factor was successfully expressed in silkworm pupae using B. mori nucleopolyhedrovirus, purified and characterized with respect to its physico-chemical properties. The target protein expressed had an apparent molecular mass of 29 kDa and an isoelectric point of 5.1. The protein was purified using three chromatographic steps with a final recovery of 10.3%. Finally, approximately 3.5 mg of the protein was obtained with a biological activity of up to 8.4 × 10~6 cfu mg~(-1). The results of this study suggest that silkworm pupae represent a convenient and low-cost bioreactor for the expression of heterologous proteins.
通过RT-PCR技术，我们利用一对特异引物从人胚纤维原细胞中扩增到人GM-CSF基因。将扩增的GM-CSF PCR产物用EcoRI和BamHI酶切后插入到同样酶切的家蚕杆状病毒转移载体pUBM-4中，从而构成了重组载体pBM-CSF。将该质粒与线性化的Bm-BacPAK6 DNA共转染家蚕细胞BmN，在培养的贴壁细胞中挑出空斑，经过3轮纯化，获得重组病毒vBm-CSF。
我们利用重组病毒vBm-CSF感染家蚕蛹来表达重组人粒细胞巨噬细胞集落刺激因子。经SDS-PAGE和Western blotting鉴定表明在重组病毒感染的家蚕蛹体内存在重组人粒细胞巨噬细胞集落刺激因子。表达产物分子量约为29kDa，在蚕蛹中的表达量约为97μg／蛹；在蚕蛹粗提物中的rhGM-CSF生物活性约为6.8×10~6cfu／mg。
与以前在家蚕细胞和幼虫中分泌表达的hGM-CSF相比，我们在家蚕蛹表达的hGM-CSF表现出较大的差异：分子量较大、表达量和生物活性偏低，这可能与蛋白的翻译后修饰有关。因而，有必要对蚕蛹表达的hGM-CSF进行大量表达和纯化以鉴定该表达产物的相关理化性质。为此，我们将重组病毒接种了大量的蚕蛹来表达hGM-CSF。通过硫酸铵分级沉淀、凝胶排阻过滤和离子交换层析多步纯化，最终我们以10.5％的得率从700头接种重组病毒的家蚕蛹中获得3.5mg纯度达97％的蚕蛹表达产物Bm-hGM-CSF。经检测，高纯度的表达产物Bm-hGM-CSF生物活性达约8.4×10~6cfs／mg。
对纯化的表达产物进行理化性质分析。等电聚焦电泳表明，家蚕蛹表达产物Bm-hGM-CSF等电点约为5.1，与家蚕细胞和幼虫中表达hGM-CSF很接近；肽谱分析发现，Bm-hGM-CSF与原核hGM-CSF在肽谱的表现上非常相似；去糖基化分析表明，Bm-hGM-CSF带有高甘露糖型糖链。这些情况表明，高度的高甘露糖化导致了Bm-hGM-CSF表现出较大差异。
To date, many recombinant proteins have been expressed in Bombyx mori cells or silkworm larvae, apart from in pupae. Silkworm pupae may be more suitable for the expression of heterologous proteins as a bioreactor. If maintained at an appropriate temperature, silkworm pupae could be inoculated with recombinant baculovirus for the expression of a protein of interest. In this study, human granulocyte-macrophage colony-stimulating factor was successfully expressed in silkworm pupae using B. mori nucleopolyhedrovirus, purified and characterized with respect to its physico-chemical properties. The target protein expressed had an apparent molecular mass of 29 kDa and an isoelectric point of 5.1. The protein was purified using three chromatographic steps with a final recovery of 10.3%. Finally, approximately 3.5 mg of the protein was obtained with a biological activity of up to 8.4 × 10~6 cfu mg~(-1). The results of this study suggest that silkworm pupae represent a convenient and low-cost bioreactor for the expression of heterologous proteins.
引文
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