摘要
肺炎嗜衣原体主要外膜蛋白是其特征抗原之一。实验中通过PCR方法从肺炎嗜衣原体基因组中扩增主要外膜蛋白基因,插入pET32a(+)表达载体,转化BL21(DE3)感受态细胞,得到表达56kD融合蛋白的工程菌株。该菌株的表达量可达53%,提纯后的主要外膜蛋白纯度可达90%以上,在Western Blotting试验和胶体金免疫层析试验中显示了良好的抗原性。
Major outer membrane protein （MOMP） is one of chlamydophila pneumoniae （Cpn） characteristic antigens . MOMP gene was amplified from complete genome by PCR and was inserted to expressed plasmid pET32a（ ＋ ）. And then, the recombinant plasmid was transferred into BL21 （ DE3 ） to construct a engineered bacteria of expressing a 56 kD fusion protein. The expression level of MOMP is as high as 53% of total protein in the engineered bacteria. After purification, the MOMP is purified over 90% and showed a better antigenicity in Western Blotting and colloidal gold immunochromatography.
出处
《微生物学免疫学进展》
2008年第1期32-35,共4页
Progress In Microbiology and Immunology
关键词
肺炎嗜衣原体
主要外膜蛋白
抗原性
Chlamydophila pneumoniae
Major outer membrane protein
Protein
Antigenicity
