Antibacterial Activity and Mechanism of a Scorpion Venom Peptide Derivative In Vitro and In Vivo

被引：96

作者：

Cao, Luyang ^{[1
]}

Dai, Chao ^{[1
]}

Li, Zhongjie ^{[1
]}

Fan, Zheng ^{[1
]}

Song, Yu ^{[1
]}

Wu, Yingliang ^{[1
]}

Cao, Zhijian ^{[1
]}

Li, Wenxin ^{[1
]}

机构：

[1] Wuhan Univ, Coll Life Sci, State Key Lab Virol, Wuhan 430072, Peoples R China

来源：

PLOS ONE | 2012年 / 7卷 / 07期

关键词：

ANTIMICROBIAL PEPTIDES; FUNCTIONAL-CHARACTERIZATION; ANTIBIOTIC-RESISTANCE;

D O I：

10.1371/journal.pone.0040135

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

BmKn2 is an antimicrobial peptide (AMP) characterized from the venom of scorpion Mesobuthus martensii Karsch by our group. In this study, Kn2-7 was derived from BmKn2 to improve the antibacterial activity and decrease hemolytic activity. Kn2-7 showed increased inhibitory activity against both Gram-positive bacteria and Gram-negative bacteria. Moreover, Kn2-7 exhibited higher antibacterial activity against clinical antibiotic-resistant strains such as methicillin-resistant Staphylococcus aureus (MRSA). In addition, the topical use of Kn2-7 effectively protected the skin of mice from infection in an S. aureus mouse skin infection model. Kn2-7 exerted its antibacterial activity via a bactericidal mechanism. Kn2-7 killed S. aureus and E. coli rapidly by binding to the lipoteichoic acid (LTA) in the S. aureus cell wall and the lipopolysaccharides (LPS) in the E. coli cell wall, respectively. Finally, the hemolytic activity of Kn2-7 was significantly decreased, compared to the wild-type peptide BmKn2. Taken together, the Kn2-7 peptide can be developed as a topical therapeutic agent for treating bacterial infections.

引用

页数：11

共 29 条

[21] The Antimicrobial Peptide Histatin-5 Causes a Spatially Restricted Disruption on the Candida albicans Surface, Allowing Rapid Entry of the Peptide into the Cytoplasm [J].

Mochon, A. Brian ;

Liu, Haoping .

PLOS PATHOGENS, 2008, 4 (10)

[22] Antibacterial and antifungal properties of α-helical, cationic peptides in the venom of scorpions from southern Africa [J].

Moerman, L ;

Bosteels, S ;

Noppe, W ;

Willems, J ;

Clynen, E ;

Schoofs, L ;

Thevissen, K ;

Tytgat, J ;

Van Eldere, J ;

van der Walt, J ;

Verdonck, F .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 2002, 269 (19) :4799-4810

[23] Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus [J].

Mygind, PH ;

Fischer, RL ;

Schnorr, KM ;

Hansen, MT ;

Sönksen, CP ;

Ludvigsen, S ;

Raventós, D ;

Buskov, S ;

Christensen, B ;

De Maria, L ;

Taboureau, O ;

Yaver, D ;

Elvig-Jorgensen, SG ;

Sorensen, MV ;

Christensen, BE ;

Kjærulff, S ;

Frimodt-Moller, N ;

Lehrer, RI ;

Zasloff, M ;

Kristensen, HH .

NATURE, 2005, 437 (7061) :975-980

[24]

Paulmann M, 2012, J BIOL CHEM 1224

[25] Hadrurin, a new antimicrobial peptide from the venom of the scorpion Hadrurus aztecus [J].

Torres-Larios, A ;

Gurrola, GB ;

Zamudio, FZ ;

Possani, LD .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 2000, 267 (16) :5023-5031

[26] Cloning and functional characterization of a new antimicrobial peptide gene StCT1 from the venom of the scorpion Scorpiops tibetanus [J].

Yuan, Wenying ;

Cao, Luyang ;

Ma, Yibao ;

Mao, Panyong ;

Wang, Weipeng ;

Zhao, Ruiming ;

Wu, Yingliang ;

Cao, Zhijian ;

Li, Wenxin .

PEPTIDES, 2010, 31 (01) :22-26

[27] Antimicrobial peptides of multicellular organisms [J].

Zasloff, M .

NATURE, 2002, 415 (6870) :389-395

[28] Identification and functional characterization of novel scorpion venom peptides with no disulfide bridge from Buthus martensii Karsch [J].

Zeng, XC ;

Wang, SX ;

Zhu, Y ;

Zhu, SY ;

Li, WX .

PEPTIDES, 2004, 25 (02) :143-150

[29] Imcroporin, a New Cationic Antimicrobial Peptide from the Venom of the Scorpion Isometrus maculates [J].

Zhao, Zhenhuan ;

Ma, Yibao ;

Dai, Chao ;

Zhao, Ruiming ;

Li, SongRyong ;

Wu, Yingliang ;

Cao, Zhijian ;

Li, Wenxin .

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 2009, 53 (08) :3472-3477

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