A thermostable serralysin inhibitor from marine bacterium Flavobacterium sp. YS-80-122  

作　　者：LIANG Pengjuan LI Shangyong WANG Kun WANG Fang XING Mengxin HAO Jianhua SUNMi 梁朋娟;李尚勇;王昆;王芳;邢孟欣;郝建华;孙谧(Key Laboratory of Polar Fisheries Development, Ministry of Agriculture, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China;Laboratory for Marine Drugs and Bioproducts, Qingdao National Laboratory for Marine Science and Technology, Qingdao 266071, China;Shanghai Ocean University, Shanghai 201306, China)

机构地区：[1]Key Laboratory of Polar Fisheries Development, Ministry of Agriculture, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China [2]Laboratory for Marine Drugs and Bioproducts, Qingdao National Laboratory for Marine Science and Technology, Qingdao 266071, China [3]Shanghai Ocean University, Shanghai 201306, China

出　　处：《Journal of Oceanology and Limnology》2018年第2期483-489,共7页海洋湖沼学报（英文）

基　　金：Supported by the National Natural Science Foundation of China(No.41376175);the Joint Funds of the National Natural Science Foundation of China(No.U1406402-5);the International S&T Cooperation Program of China(No.2014DFG30890);the Qingdao Science and Technology Plan Project(No.14-2-4-11-jch);the National Science Foundation for PostDoctoral Scientists of China(No.2016M590673);the Application Foundation of Qingdao for Post-Doctoral Scientists of China(No.Q51201601)

摘　　要：Serralysin inhibitors have been proposed as potent drugs against many diseases and may help to prevent further development of antibiotic-resistant pathogenic bacteria. In this study, a novel serralysin inhibitor gene, lupI, was cloned from the marine bacterium Flavobacterium sp. YS-80-122 and expressed in Escherichia coll. The deduced serralysin inhibitor, LupI, shows 〈40% amino acid identity to other reported serralysin inhibitors. Multiple sequence alignment and phylogenetic analysis of LupI with other serralysin inhibitors indicated that LupI was a novel type of serralysin inhibitor. The inhibitory constant for LupI towards its target metalloprotease was 0.64mol/L. LupI was thermostable at high temperature, in which 35.6%-90.7% of its inhibitory activity was recovered after treatment at 100℃ for 1-60 min followed by incubation at 0℃. This novel inhibitor may represent a candidate drug for the treatment of serralysin-related infections.Serralysin inhibitors have been proposed as potent drugs against many diseases and may help to prevent further development of antibiotic-resistant pathogenic bacteria. In this study, a novel serralysin inhibitor gene, l up I, was cloned from the marine bacterium F lavobacterium sp. YS-80-122 and expressed in Escherichia coli. The deduced serralysin inhibitor, Lup I, shows <40% amino acid identity to other reported serralysin inhibitors. Multiple sequence alignment and phylogenetic analysis of Lup I with other serralysin inhibitors indicated that Lup I was a novel type of serralysin inhibitor. The inhibitory constant for Lup I towards its target metalloprotease was 0.64 μmol/L. Lup I was thermostable at high temperature, in which 35.6%–90.7% of its inhibitory activity was recovered after treatment at 100°C for 1–60 min followed by incubation at 0°C. This novel inhibitor may represent a candidate drug for the treatment of serralysin-related infections.

关 键 词：serralysin inhibitor sequence analysis kinetic parameter THERMOSTABLE 

分 类 号：P[天文地球]