摘要
目的研究肺炎链球菌主要毒力蛋白神经氨酸酶Nan A的基本特性,为新型疫苗研究打下基础。方法分离、纯化和鉴定重组Nan A;利用生物信息学和蛋白分析软件探索Nan A的蛋白特性。结果 Nan A全长1 039个氨基酸,其功能单位为第316-791位氨基酸片段,活性与全长Nan A无差异;Nan A片段水溶性和稳定性佳;Nan A蛋白表面负性电荷为主,活性中心以正性电荷为主,Tyr752或Asp372突变即可令其失活。结论Nan A可作为新型肺炎链球菌疫苗研发的新靶点。
[Objectives] To investigate the biological properties of sialidase Nan A from Streptococcus pneumoniae, providing basic research data for Nan A as a potential vaccine target. [Methods] Nan A was cloned, over-expressed and purified for biological experiments. The three-dimensional structure was analyzed with the structure date deposited to the protein data bank. [Results] The recombinant Nan A is stable and highly soluble. Nan A consists of 1 039 amino acids, however, the functional domain retaining sialidase activity was found to be 316-791 aa. The surface of Nan A is mainly positively charged, while the active site was negatively charged. Site mutation of Tyr752 or Asp372 could deactivate Nan A. [Conclusion] Nan A could be a potential vaccine target.
出处
《中国现代医学杂志》
CAS
CSCD
北大核心
2014年第8期22-25,共4页
China Journal of Modern Medicine
基金
霍英东青年教师基础研究项目资金(No:131039)
江西省自然科学基金(No:20114BAB215002)
