The Spider Venom Peptide Lycosin-II Has Potent Antimicrobial Activity against Clinically Isolated Bacteria.
The Spider Venom Peptide Lycosin-II Has Potent Antimicrobial Activity against Clinically Isolated Bacteria.
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DOI：
10.3390/toxins8050119
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发表时间：
2016-04-26
期刊：
影响因子：
4.2
通讯作者：
Shi X
中科院分区：
文献类型：
--
作者：
Wang Y;Wang L;Yang H;Xiao H;Farooq A;Liu Z;Hu M;Shi X
抗菌肽已被公认为开发抗耐药细菌的新型抗生素的优秀候选者。最近的研究表明，蜘蛛毒液是鉴定新型抗菌肽的来源。在本研究中，我们从蜘蛛Lycosa singoriensis毒液中分离并鉴定了一种名为lycosin-II的抗菌肽。它含有21个缺乏半胱氨酸残基的氨基酸残基，形成典型的线性两亲阳离子α-螺旋构象。lycos - ii对从医院患者中分离的耐药菌株，包括多重耐药鲍曼不动杆菌，显示出强大的抑菌作用，这对感染治疗提出了巨大的挑战。lycos - ii的抑制能力可能来自于它与细胞膜的结合，因为Mg2+可以与结合位点竞争以降低lycos - ii的抑菌效力。我们的数据表明，lycoin - ii可能是开发治疗耐药细菌感染的新型抗生素的先导。
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.