title: Antimicrobial potential of lycosin-I, a cationic and amphiphilic peptide from the venom of the spider Lycosa singorensis.
abstract: Antimicrobial peptides (AMPs) are significant components of the innate immune system and play indispensable roles in the resistance to bacterial infection. Here, we investigated the antimicrobial activity of lycosin-I, a 24-residue cationic anticancer peptide derived from Lycosa singorensis with high structural similarity to several cationic and amphiphilic antimicrobial peptides. The antimicrobial activity of lycosin-I against 27 strains of microbes including bacteria and fungi was examined and compared with that of the Xenopus-derived AMP magainin 2 using a microdilution assay. Lycosin-I inhibited the growth of most microorganisms at low micromolar concentrations, and was a more potent inhibitor than magainin 2. Lycosin-I showed rapid, selective and broad-spectrum bactericidal activity and a synergistic effect with traditional antibiotics. In vivo, it showed potent bactericidal activity in a mouse thigh infection model. High Mg2+ concentrations reduced the antibacterial effect of lycosin-I, implying that the peptide might directly interact with the bacterial cell membrane. Uptake of the fluorogenic dye SYTOX and changes in the surface of lycosin-Itreated bacterial cells observed by scanning electron microscopy confirmed that lycosin-I permeabilized the cell membrane, resulting in the rapid bactericidal effect. Taken together, our findings indicate that lycosin-I is a promising peptide with the potential for the development of novel antibacterial agents.
authors: College of Life Sciences, Hunan Normal University, Changsha, Hunan, China. liuzh@hunnu.edu.cn
authors: H
authors: H
authors: Tan
authors: X
authors: X
authors: Ding
authors: S
authors: S
authors: Meng
authors: C
authors: C
authors: Liu
authors: H
authors: H
authors: Wang
authors: L
authors: L
authors: Xia
authors: Z
authors: Z
authors: Liu
authors: S
authors: S
authors: Liang
mesh_terms: D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D000890:Anti-Infective Agents / Q000494:pharmacology* / Q000627:therapeutic use; D023181:Antimicrobial Cationic Peptides / Q000494:pharmacology* / Q000627:therapeutic use; D001419:Bacteria / Q000187:drug effects / Q000254:growth & development / Q000648:ultrastructure; D004912:Erythrocytes / Q000187:drug effects; D006461:Hemolysis / Q000187:drug effects; D006801:Humans; D054806:Magainins / Q000494:pharmacology; D008274:Magnesium / Q000494:pharmacology; D051379:Mice; D008826:Microbial Sensitivity Tests; D050296:Microbial Viability / Q000187:drug effects; D013111:Spider Venoms / Q000494:pharmacology* / Q000627:therapeutic use; D013112:Spiders / Q000737:chemistry*; D013203:Staphylococcal Infections / Q000188:drug therapy / Q000382:microbiology / Q000473:pathology; D029867:Xenopus Proteins / Q000494:pharmacology
chemical_list: D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D054806:Magainins; D013111:Spider Venoms; D029867:Xenopus Proteins; C586566:lycosin-I, Lycosa singorensis; C053301:magainin 2 peptide, Xenopus; D008274:Magnesium