title: The Spider Venom Peptide Lycosin-II Has Potent Antimicrobial Activity against Clinically Isolated Bacteria.
abstract: Antimicrobial peptides have been accepted as excellent candidates for developing novel antibiotics against drug-resistant bacteria. Recent studies indicate that spider venoms are the source for the identification of novel antimicrobial peptides. In the present study, we isolated and characterized an antibacterial peptide named lycosin-II from the venom of the spider Lycosa singoriensis. It contains 21 amino acid residue lacking cysteine residues and forms a typical linear amphipathic and cationic α-helical conformation. Lycosin-II displays potent bacteriostatic effect on the tested drug-resistant bacterial strains isolated from hospital patients, including multidrug-resistant A. baumannii, which has presented a huge challenge for the infection therapy. The inhibitory ability of lycosin-II might derive from its binding to cell membrane, because Mg(2+) could compete with the binding sites to reduce the bacteriostatic potency of lycosin-II. Our data suggest that lycosin-II might be a lead in the development of novel antibiotics for curing drug-resistant bacterial infections.
authors.affiliation: Department of Medical Genetics, 2nd XiangYa Hospital of Central South University, Changsha 410011, China. tsm2076@yeah.net.|Department of Gastroenterology, 2nd XiangYa Hospital of Central South University, Changsha 410011, China. tsm2076@yeah.net.
authors.forename: Yongjun
authors.initials: Y
authors.lastname: Wang
authors.affiliation: Clinical Laboratory, 2nd XiangYa Hospital of Central South University, Changsha 410011, China. wl13787024873@163.com.
authors.forename: Ling
authors.initials: L
authors.lastname: Wang
authors.affiliation: Department of Medical Genetics, 2nd XiangYa Hospital of Central South University, Changsha 410011, China. tracytsm2009@163.com.
authors.forename: Huali
authors.initials: H
authors.lastname: Yang
authors.affiliation: Medical Experimental Animal Center, 2nd XiangYa Hospital of Central South University, Changsha 410011, China. leon228890575@163.com.
authors.forename: Haoliang
authors.initials: H
authors.lastname: Xiao
authors.affiliation: College of Life Sciences, Hunan Normal University, Changsha 410081, Hunan, China. drathar.cn@hotmail.com.
authors.forename: Athar
authors.initials: A
authors.lastname: Farooq
authors.affiliation: College of Life Sciences, Hunan Normal University, Changsha 410081, Hunan, China. liuzh@hunnu.edu.cn.
authors.forename: Zhonghua
authors.initials: Z
authors.lastname: Liu
authors.affiliation: Clinical Laboratory, 2nd XiangYa Hospital of Central South University, Changsha 410011, China. minhu013@sina.com.
authors.forename: Min
authors.initials: M
authors.lastname: Hu
authors.affiliation: Department of Medical Genetics, 2nd XiangYa Hospital of Central South University, Changsha 410011, China. drxiaoliushi@sina.cn.|Department of Gastroenterology, 2nd XiangYa Hospital of Central South University, Changsha 410011, China. drxiaoliushi@sina.cn.
authors.forename: Xiaoliu
authors.initials: X
authors.lastname: Shi
mesh_terms: D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D001419:Bacteria / Q000187:drug effects / Q000254:growth & development; D002478:Cells, Cultured; D002851:Chromatography, High Pressure Liquid; D024901:Drug Resistance, Multiple, Bacterial; D004912:Erythrocytes / Q000187:drug effects; D006461:Hemolysis / Q000187:drug effects; D006801:Humans; D008274:Magnesium / Q000494:pharmacology; D008826:Microbial Sensitivity Tests; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013111:Spider Venoms / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D013111:Spider Venoms; C000624377:lycosin-II, Lycosa singoriensis; D008274:Magnesium
keywords: antimicrobial peptides; cationic α-helical conformation; drug-resistant bacteria; spider venom