Congeners of SMAP29 kill ovine pathogens and induce ultrastructural damage in bacterial cells

被引:75
作者
Kalfa, VC
Jia, HP
Kunkle, RA
McCray, PB
Tack, BF
Brogden, KA
机构
[1] USDA ARS, Natl Anim Dis Ctr, Resp Dis Livestock Res Unit, Ames, IA 50010 USA
[2] Univ Iowa, Coll Med, Dept Pediat, Iowa City, IA 52242 USA
[3] Univ Iowa, Coll Med, Dept Microbiol, Iowa City, IA 52242 USA
关键词
D O I
10.1128/AAC.45.11.3256-3261.2001
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
SMAP29, an ovine cathelicidin, was systematically altered to create a family of 23 related peptides for MIC and minimum bactericidal concentration determinations. SMAP28, SMAP29, and a derivative of SMAP29 called ovispirin were all antimicrobial. However, many congeners of SMAP29 and ovispirin were not as active as the parent molecules. With immunoelectron microscopy, SMAP29 was seen on membranes and within the cytoplasm of Pseudomonas aeruginosa PAO1.
引用
收藏
页码:3256 / 3261
页数:6
相关论文
共 16 条
[1]   CDNA SEQUENCES OF 3 SHEEP MYELOID CATHELICIDINS [J].
BAGELLA, L ;
SCOCCHI, M ;
ZANETTI, M .
FEBS LETTERS, 1995, 376 (03) :225-228
[2]   PASTEURELLA-HAEMOLYTICA LIPOPOLYSACCHARIDE-ASSOCIATED PROTEIN INDUCES PULMONARY INFLAMMATION AFTER BRONCHOSCOPIC DEPOSITION IN CALVES AND SHEEP [J].
BROGDEN, KA ;
ACKERMANN, MR ;
DEBEY, BM .
INFECTION AND IMMUNITY, 1995, 63 (09) :3595-3599
[4]   The ovine cathelicidin SMAP29 kills ovine respiratory pathogens in vitro and in an ovine model of pulmonary infection [J].
Brogden, KA ;
Kalfa, VC ;
Ackermann, MR ;
Palmquist, DE ;
McCray, PB ;
Tack, BF .
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 2001, 45 (01) :331-334
[5]   The outer membrane of Brucella ovis shows increased permeability to hydrophobic probes and is more susceptible to cationic peptides than are the outer membranes of mutant rough Brucella abortus strains [J].
Freer, E ;
Pizarro-Cerdá, J ;
Weintraub, A ;
Bengoechea, JA ;
Moriyón, I ;
Hultenby, K ;
Gorvel, JP ;
Moreno, E .
INFECTION AND IMMUNITY, 1999, 67 (11) :6181-6186
[6]  
Groisman Eduardo A., 1994, Trends in Microbiology, V2, P444, DOI 10.1016/0966-842X(94)90802-8
[7]  
HENK WG, 1995, SCANNING MICROSCOPY, V9, P501
[8]   Molecular analysis of the sheep cathelin family reveals a novel antimicrobial peptide [J].
Mahoney, MM ;
Lee, AY ;
BrezinskiCaliguri, DJ ;
Huttner, KM .
FEBS LETTERS, 1995, 377 (03) :519-522
[9]   Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity [J].
Oren, Z ;
Lerman, JC ;
Gudmundsson, GH ;
Agerberth, B ;
Shai, Y .
BIOCHEMICAL JOURNAL, 1999, 341 :501-513
[10]   A comparative study on the structure and function of a cytolytic α-helical peptide and its antimicrobial β-sheet diastereomer [J].
Oren, Z ;
Hong, J ;
Shai, Y .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1999, 259 (1-2) :360-369