论文部分内容阅读
参考GenBank中鸭源鸡杆菌(Gallibacterium anatis,G.anatis)UMN179的外膜蛋白W(outer membrane protein W,OmpW)基因序列设计1对引物,对鸭源鸡杆菌PDS-RZ-1-SLG株的OmpW基因进行克隆、测序,并通过生物信息学软件对该蛋白结构与功能进行分析及预测。结果显示:OmpW基因大小为705bp,编码234个氨基酸;与鸭源鸡杆菌UMN179株、F149株及12656/12株的OmpW氨基酸同源性分别为88.9%、78.7%和79.6%;OmpW相对分子质量为25 300,等电点为7.88,是能够稳定存在的蛋白,N端有1个疏水性的α螺旋信号肽,C端有1个疏水性的β折叠区域,并且在外膜表面存在1个保守性的B细胞线性表位。本试验成功克隆了鸭源鸡杆菌PDS-RZ-1-SLG株的OmpW基因,并对其结构与功能进行初步分析和预测,为进一步研究其生物学功能及其应用奠定基础。
A pair of primers was designed based on the OmpW gene sequence of Gallibacterium anatis (G.anatis) UMN179 in GenBank. OmpW gene was cloned, sequenced, and the structure and function of the protein were analyzed and predicted by bioinformatics software. The results showed that the OmpW gene was 705bp in size and encoded 234 amino acids. The OmpW amino acid identities of OmpW gene were 88.9%, 78.7% and 79.6%, respectively. The OmpW amino acid identities with O. nipponense UMN179, F149 and 12656/12 were 0.98, Is 25 300 and the isoelectric point is 7.88, which is a stable protein. There is a hydrophobic α-helix signal peptide at the N-terminus and a hydrophobic β-sheet at the C-terminus, and has a conserved surface on the outer membrane Sexual B cell linear epitopes. In this study, OmpW gene was successfully cloned from Pichia pastoris strain PDS-RZ-1-SLG and its structure and function were preliminarily analyzed and predicted, which laid the foundation for further study of its biological function and its application.