Toxins 2016, 8(5), 119; doi:10.3390/toxins8050119
The Spider Venom Peptide Lycosin-II Has Potent Antimicrobial Activity against Clinically Isolated Bacteria
1
Department of Medical Genetics, 2nd XiangYa Hospital of Central South University, Changsha 410011, China
2
Department of Gastroenterology, 2nd XiangYa Hospital of Central South University, Changsha 410011, China
3
Clinical Laboratory, 2nd XiangYa Hospital of Central South University, Changsha 410011, China
4
Medical Experimental Animal Center, 2nd XiangYa Hospital of Central South University, Changsha 410011, China
5
College of Life Sciences, Hunan Normal University, Changsha 410081, Hunan, China
*
Authors to whom correspondence should be addressed.
Academic Editor: Glenn F. King
Received: 2 February 2016 / Revised: 5 April 2016 / Accepted: 6 April 2016 / Published: 26 April 2016
(This article belongs to the Special Issue Arthropod Venoms)
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 Mg2+ 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. View Full-TextKeywords:
antimicrobial peptides; spider venom; drug-resistant bacteria; cationic α-helical conformation
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
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MDPI and ACS Style
Wang, Y.; Wang, L.; Yang, H.; Xiao, H.; Farooq, A.; Liu, Z.; Hu, M.; Shi, X. The Spider Venom Peptide Lycosin-II Has Potent Antimicrobial Activity against Clinically Isolated Bacteria. Toxins 2016, 8, 119.
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