SMAP-29: a potent antibacterial and antifungal peptide from sheep leukocytes

被引:176
作者
Skerlavaj, B
Benincasa, M
Risso, A
Zanetti, M
Gennaro, R
机构
[1] Univ Trieste, Dipartimento Biochim Biofis & Chim Macromol, I-34127 Trieste, Italy
[2] Univ Udine, Dipartimento Sci & Tecnol Biomed, I-33100 Udine, Italy
[3] Lab Nazl CIB, Area Sci Pk, I-34012 Trieste, Italy
来源
FEBS LETTERS | 1999年 / 463卷 / 1-2期
关键词
antimicrobial peptide; cathelicidin; amphipathic helix; lytic peptide;
D O I
10.1016/S0014-5793(99)01600-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
SMAP-29 is a cathelicidin-derived peptide deduced from sheep myeloid mRNA, The C-terminally amidated form of this peptide was chemically synthesized and shown to exert a potent antimicrobial activity. Antibiotic-resistant clinical isolates highly susceptible to this peptide include MRSA and VREF isolates, that are a major worldwide problem, and mucoid Pseudomonas aeruginosa associated with chronic respiratory inflammation in CF patients. In addition, SMAP-29 is also active against fungi, including Cryptococcus neoformans isolated from immunocompromised patients. SMAP-29 causes significant morphological alterations of the bacterial surfaces, as shown by scanning electron microscopy, and is also hemolytic against human, but not sheep erythrocytes. Its potent antimicrobial activity suggests that this peptide is an excellent candidate as a lead compound for the development of novel antiinfective agents. (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码:58 / 62
页数:5
相关论文
共 32 条
  • [1] CDNA SEQUENCES OF 3 SHEEP MYELOID CATHELICIDINS
    BAGELLA, L
    SCOCCHI, M
    ZANETTI, M
    [J]. FEBS LETTERS, 1995, 376 (03) : 225 - 228
  • [2] Boman HG, 1998, SCAND J IMMUNOL, V48, P15
  • [3] HEMOLYSIS OF ERYTHROCYTES AND FLUORESCENCE POLARIZATION CHANGES ELICITED BY PEPTIDE TOXINS, ALIPHATIC-ALCOHOLS, RELATED GLYCOLS AND BENZYLIDENE DERIVATIVES
    CASTRO, VROE
    ASHWOOD, ER
    WOOD, SG
    VERNON, LP
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1990, 1029 (02) : 252 - 258
  • [4] PSEUDOMONAS-AERUGINOSA CYTO-TOXIN - THE INFLUENCE OF SPHINGOMYELIN ON BINDING AND CATION PERMEABILITY INCREASE IN MAMMALIAN ERYTHROCYTES
    CROWELL, KM
    LUTZ, F
    [J]. TOXICON, 1989, 27 (05) : 531 - 540
  • [5] Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides
    Dathe, M
    Wieprecht, T
    Nikolenko, H
    Handel, L
    Maloy, WL
    MacDonald, DL
    Beyermann, M
    Bienert, M
    [J]. FEBS LETTERS, 1997, 403 (02): : 208 - 212
  • [6] 3-DIMENSIONAL STRUCTURE OF MEMBRANE AND SURFACE-PROTEINS
    EISENBERG, D
    [J]. ANNUAL REVIEW OF BIOCHEMISTRY, 1984, 53 : 595 - 623
  • [7] Ganz T, 1997, SEMIN HEMATOL, V34, P343
  • [8] Biological characterization of a novel mammalian antimicrobial peptide
    Gennaro, R
    Scocchi, M
    Merluzzi, L
    Zanetti, M
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 1998, 1425 (02): : 361 - 368
  • [9] Juban M M, 1997, Methods Mol Biol, V78, P73
  • [10] Using host defenses to fight infectious diseases
    Kelley, KJ
    [J]. NATURE BIOTECHNOLOGY, 1996, 14 (05) : 587 - &