Cite this paper:
LIANG Pengjuan, LI Shangyong, WANG Kun, WANG Fang, XING Mengxin, HAO Jianhua, SUN Mi. A thermostable serralysin inhibitor from marine bacterium Flavobacterium sp. YS-80-122[J]. HaiyangYuHuZhao, 2018, 36(2): 483-489

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

LIANG Pengjuan1,2, LI Shangyong1,2, WANG Kun1,3, WANG Fang1, XING Mengxin1,2, HAO Jianhua1,2, SUN Mi1,2
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
Abstract:
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 coli. 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 0.64 μmol/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.
Key words:    serralysin inhibitor|sequence analysis|kinetic parameter|thermostable   
Received: 2016-10-13   Revised:
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