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Antimicrobial Potential of Lycosin-I, a Cationic and Amphiphilic Peptide from the Venom of the Spider Lycosa singorensis

[ Vol. 13 , Issue. 6 ]

Author(s):

H. Tan, X. Ding, S. Meng, C. Liu, H. Wang, L. Xia, Z. Liu and S. Liang   Pages 900 - 910 ( 11 )

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.

Keywords:

Antimicrobial activity, antimicrobial peptide, cell membrane permeabilization, lycosin-I, spider venom.

Affiliation:

College of Life Sciences, Hunan Normal University, Changsha, 410081, Hunan, China.



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