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^*; Sun Mi^*

来源：Journal of Oceanology and Limnology, 2018, 36(2): 483-489.

DOI：10.1007/s00343-018-6266-y

• serralysin inhibitor
• sequence analysis
• kinetic parameter
• thermostable

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 mu mol/L. LupI was thermostable at high temperature, in which 35.6%-90.7% of its inhibitory activity was recovered after treatment at 100 degrees C for 1-60 min followed by incubation at 0 degrees C. This novel inhibitor may represent a candidate drug for the treatment of serralysin-related infections.

• 出版日期2018-3
• 单位中国水产科学研究院; 上海海洋大学