A thermostable serralysin inhibitor from marine bacterium <italic style="font-style: italic">Flavobacterium</italic> sp. YS-80-122

Pengjuan LIANG; Shangyong LI; Kun WANG; Fang WANG; Mengxin XING; Jianhua HAO; Mi SUN

doi:10.1007/s00343-018-6266-y

Your Location：

Home >

Browse articles >

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

Biology | Updated：2023-05-19

- A thermostable serralysin inhibitor from marine bacterium Flavobacterium sp. YS-80-122
- Chinese Journal of Oceanology and Limnology Vol. 36, Issue 2, Pages: 483-489(2018)
- Affiliations：
  
  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
- Author bio：
  
  HAO Jianhua, haojh@ysfri.ac.cn
  SUN Mi, sunmi@ysfri.ac.cn
- Funds：
- DOI：10.1007/s00343-018-6266-y
  CLC：
- Received：13 October 2016，
  
  Accepted：26 December 2016，
  
  Online First：22 February 2018，
  
  Published：2018-03
- Accepted：
Scan QR Code
Pengjuan LIANG, Shangyong LI, Kun WANG, et al. A thermostable serralysin inhibitor from marine bacterium Flavobacterium sp. YS-80-122[J]. Chinese Journal of Oceanology and Limnology, 2018, 36(2): 483-489.
DOI：

Pengjuan LIANG, Shangyong LI, Kun WANG, et al. A thermostable serralysin inhibitor from marine bacterium Flavobacterium sp. YS-80-122[J]. Chinese Journal of Oceanology and Limnology, 2018, 36(2): 483-489. DOI： 10.1007/s00343-018-6266-y.

摘要

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.

关键词

Keywords

references

Arumugam S, Gray R D, Lane A N. 2008. NMR structure note:alkaline proteinase inhibitor APRin from Pseudomonas aeruginosa . J. Biomol. NMR, 40(3):213-217.

Bae K H, Kim I C, Kim K S, Shin Y C, Byun S M. 1998. The Leu-3 residue of Serratia marcescens metalloprotease inhibitor is important in inhibitory activity and binding with Serratia marcescens metalloprotease. Arch. Biochem.Biophys., 352(1):37-43.

Bardoel B W, van Kessel K P M, van Strijp J A G, Milder F J. 2012. Inhibition of Pseudomonas aeruginosa virulence:characterization of the AprA-AprI interface and species selectivity. J. Mol. Biol., 415(3):573-583.

Baumann U, Bauer M, Létoffé S, Delepelaire P, Wandersman C. 1995. Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi. J. Mol. Biol., 248(3):653-661.

Dhanaraj V, Ye Q Z, Johnson L L, Hupe D J, Ortwine D F, Dunbar J B Jr, Rubin J R, Pavlovsky A, Humblet C, Blundell T L. 1996. Designing inhibitors of the metalloproteinase superfamily:comparative analysis of representative structures. Drug Des. Discov., 13(3-4):3-14.

Feltzer R E, Gray R D, Dean W L, Pierce W M Jr. 2000.Alkaline proteinase inhibitor of Pseudomonas aeruginosa :interaction of native and N-terminally truncated inhibitor proteins with Pseudomonas metalloproteinases. J. Biol. Chem., 275(28):21 002-21 009.

Feltzer R E, Trent J O, Gray R D. 2003. Alkaline proteinase inhibitor of Pseudomonas aeruginosa :a mutational and molecular dynamics study of the role of n-terminal residues in the inhibition of pseudomonas alkaline proteinase. J. Biol. Chem., 278(28):25 952-25 957.

Hao J H, Sun M. 2015. Purification and characterization of a cold alkaline protease from a psychrophilic Pseudomonas aeruginosa HY1215. Appl. Biochem. Biotechnol., 175(2):715-722.

Hege T, Baumann U. 2001. Protease C of Erwinia chrysanthemi :the crystal structure and role of amino acids Y228 and E189. J. Mol. Biol., 314(2):187-193.

Hege T, Feltzer R E, Gray R D, Baumann U. 2001. Crystal structure of a complex between Pseudomonas aeruginosa alkaline protease and its cognate inhibitor:inhibition by a Zinc-NH 2 coordinative bond. J. Biol. Chem., 276(37):35 087-35 092.

Ji X F, Zheng Y, Wang W, Sheng J, Hao J H, Sun M. 2013.Virtual screening of novel reversible inhibitors for marine alkaline protease MP. J. Mol. Graph. Model., 46:125-131.

Kida Y, Higashimoto Y, Inoue H, Shimizu T, Kuwano K. 2008.A novel secreted protease from Pseudomonas aeruginosa activates NF-κB through protease-activated receptors.Cell. Microbiol., 10(7):1 491-1 504.

Kida Y, Inoue H, Shimizu T, Kuwano K. 2007. Serratia marcescens serralysin induces inflammatory responses through protease-activated receptor 2. Infect. Immun., 75(1):164-174.

Kim K S, Kim T U, Kim I J, Byun S M, Shin Y C. 1995.Characterization of a metalloprotease inhibitor protein(SmaPI) of Serratia marcescens . Appl. Environ.Microbiol., 61(8):3 035-3 041.

Létoffé S, Delepelaire P, Wandersman C. 1989. Characterization of a protein inhibitor of extracellular proteases produced by Erwinia chrysanthemi . Mol. Microbiol., 3(1):79-86.

Li S Y, Wang L N, Yang J, Bao J, Liu J Z, Lin S X, Hao J H, Sun M. 2016. Affinity purification of metalloprotease from marine bacterium using immobilized metal affinity chromatography. J. Sep. Sci., 39(11):2 050-2 056.

Liao C H, McCallus D E. 1998. Biochemical and genetic characterization of an extracellular protease from Pseudomonas fluorescens CY091. Appl. Environ.Microbiol., 64(3):914-921.

Louis D, Sorlier P, Wallach J. 1998. Quantitation and enzymatic activity of the alkaline protease from Pseudomonas aeruginosa in culture supernatants from clinical strains.Clin. Chem. Lab. Med., 36(5):295-298.

Wang F, Hao J H, Yang C Y, Sun M. 2010. Cloning, expression, and identification of a novel extracellular cold-adapted alkaline protease gene of the marine bacterium strain YS-80-122. Appl. Biochem. Biotechnol., 162(5):1 497-1 505.

Views

Downloads

CSCD

Alert me when the article has been cited

Submit

Tools

Publicity Resources

Identification and characterization of microbial agents in a bloom of floating microorganisms in the Hailang River, China in 2006

Sequence analysis of the ITS region and 5.8S rDNA of Porphyra haitanensis

Multivariable Constrained Model Predictive Control ofAero-Engine Based on Augmented Predictive Model

Parametric Model of Lubricant Particle Trajectory inAnnulus Inter-Spools

PI Gain Scheduling Control for Flight EnvironmentSimulation System of Altitude Ground TestFacilities Based on LMI Pole Assignment

Related Author

Weili Wu

Jinglin Wang

Licheng Liu

Jun Jiang

Yan Chen

Tao Hu

Weijun Chen

Yanyan Li

Related Institution

Beijing Institute of Genomics Chinese Academy of Sciences

State Key Laboratory of Pathogen and Biosecurity Institute of Microbiology and Epidemiology Academy of Military Medical Sciences

Department of Cell Biology Medical College of Soochow University

Department of Biology and Food Engineering Changshu Institute of Technology

Institute of Oceanology Chinese Academy of Sciences

Address：Editorial Office of JOL, 88 Haijun Rd. Qingdao, 266000, China
Tel：+86-532-82898754 Email：jol@qdio.ac.cn
Technical support is provided by Beijing Founder electronics co., LTD 京ICP备09064830号-19 京公网安备11010802024621
It is recommended to read the content of this site in Chrome&IE9+. Please switch to extreme mode in browser 360.
Cookies We use cookies to help provide and enhance our service and tailor content. By continuing, you agree to the use of cookies.

⁰

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

DOI：10.1007/s00343-018-6266-y

摘要

Abstract

关键词

Keywords

references