Antibacterial and antifungal properties of alpha-helical, cationic peptides in the venom of scorpions from southern Africa.

Two novel pore-forming peptides have been isolated from the venom of the South-African scorpion Opistophtalmus carinatus. These peptides, designated opistoporin 1 and 2, differ by only one amino acid and belong to a group of alpha-helical, cationic peptides. For the first time, a comparison of the primary structures of alpha-helical pore-forming peptides from scorpion venom was undertaken. This analysis revealed that peptides in the range of 40-50 amino acids contain a typical scorpion conserved sequence S(x)3KxWxS(x)5L. An extensive study of biological activity of synthesized opistoporin 1 and parabutoporin, a pore-forming peptide previously isolated from the venom of the South-African scorpion Parabuthus schlechteri, was undertaken to investigate an eventual cell-selective effect of the peptides. Opistoporin 1 and parabutoporin were most active in inhibiting growth of Gram-negative bacteria (1.3-25 micro m), while melittin and mastoparan, two well-known cytolytic peptides, were more effective against Gram-positive bacteria in the same concentration range. In addition, the peptides showed synergistic activity with some antibiotics commonly used in therapy. Opistoporin 1 and parabutoporin had hemolytic activity intermediate between the least potent mastoparan and the highly lytic melittin. Furthermore, all peptides inhibited growth of fungi. Experiments with SYTOX green suggested that this effect is related to membrane permeabilization.

[1]  F. Gervais,et al.  Bee venom melittin blocks neutrophil O2− production , 1986, Inflammation.

[2]  E. Villegas,et al.  Oxyopinins, Large Amphipathic Peptides Isolated from the Venom of the Wolf Spider Oxyopes kitabensis with Cytolytic Properties and Positive Insecticidal Cooperativity with Spider Neurotoxins* , 2002, The Journal of Biological Chemistry.

[3]  H. Naoki,et al.  Purification, structure-function analysis, and molecular characterization of novel linear peptides from scorpion Opisthacanthus madagascariensis. , 2002, Biochemical and biophysical research communications.

[4]  Jürg Müller,et al.  Cupiennin 1, a New Family of Highly Basic Antimicrobial Peptides in the Venom of the Spider Cupiennius salei(Ctenidae)* , 2002, The Journal of Biological Chemistry.

[5]  M. Zasloff.  Antimicrobial peptides of multicellular organisms , 2002, Nature.

[6]  N. Kawai,et al.  Anoplin, a novel antimicrobial peptide from the venom of the solitary wasp Anoplius samariensis. , 2001, Biochimica et biophysica acta.

[7]  A. Tossi,et al.  Amphipathic alpha helical antimicrobial peptides: A systematic study of the effects of structural and physical properties on biological activity. , 2001 .

[8]  Alessandro Tossi,et al.  Amphipathic α helical antimicrobial peptides. , 2001 .

[9]  R. Hancock,et al.  Cationic peptides: effectors in innate immunity and novel antimicrobials. , 2001, The Lancet. Infectious diseases.

[10]  R. Norton,et al.  Characterization of unique amphipathic antimicrobial peptides from venom of the scorpion Pandinus imperator. , 2001, The Biochemical journal.

[11]  H. Naoki,et al.  IsCT, a novel cytotoxic linear peptide from scorpion Opisthacanthus madagascariensis. , 2001, Biochemical and biophysical research communications.

[12]  J. Rossier,et al.  Ponericins, New Antibacterial and Insecticidal Peptides from the Venom of the Ant Pachycondyla goeldii * , 2001, The Journal of Biological Chemistry.

[13]  M. Fridkin,et al.  Structure-function relationship in the interaction of mastoparan analogs with neutrophil NADPH oxidase. , 2001, Biochemical Pharmacology.

[14]  J. Winderickx,et al.  A gene encoding a sphingolipid biosynthesis enzyme determines the sensitivity of Saccharomyces cerevisiae to an antifungal plant defensin from dahlia (Dahlia merckii). , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[15]  A. Torres-Larios,et al.  Hadrurin, a new antimicrobial peptide from the venom of the scorpion Hadrurus aztecus. , 2000, European journal of biochemistry.

[16]  J. Bland,et al.  D-cecropin B: proteolytic resistance, lethality for pathogenic fungi and binding properties. , 2000, Medical mycology.

[17]  L. Possani,et al.  Scorpine, an anti‐malaria and anti‐bacterial agent purified from scorpion venom , 2000, FEBS letters.

[18]  Wenxin Li,et al.  Cloning and Characterization of a Novel cDNA Sequence Encoding the Precursor of a Novel Venom Peptide (BmKbpp) Related to a Bradykinin‐Potentiating Peptide from Chinese Scorpion Buthus martensii Karsch , 2000, IUBMB life.

[19]  J. Desmet,et al.  A novel class of pore-forming peptides in the venom of parabuthus schlechteri Purcell (scorpions: buthidae) , 2000 .

[20]  Alessandro Tossi,et al.  Amphipathic, α‐helical antimicrobial peptides , 2000 .

[21]  M. Dathe,et al.  Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. , 1999, Biochimica et biophysica acta.

[22]  H. Vogel,et al.  Diversity of antimicrobial peptides and their mechanisms of action. , 1999, Biochimica et biophysica acta.

[23]  M. Benincasa,et al.  SMAP‐29: a potent antibacterial and antifungal peptide from sheep leukocytes , 1999, FEBS letters.

[24]  Franky R. G. Terras,et al.  Permeabilization of Fungal Membranes by Plant Defensins Inhibits Fungal Growth , 1999, Applied and Environmental Microbiology.

[25]  G A Gutman,et al.  A unified nomenclature for short-chain peptides isolated from scorpion venoms: alpha-KTx molecular subfamilies. , 1999, Trends in pharmacological sciences.

[26]  R. Benz,et al.  Influence of proline residues on the antibacterial and synergistic activities of alpha-helical peptides. , 1999, Biochemistry.

[27]  B. Baldo,et al.  Cytotoxicity of pilosulin 1, a peptide from the venom of the jumper ant Myrmecia pilosula. , 1998, Biochimica et biophysica acta.

[28]  K. Krause,et al.  Aerolysin Induces G-protein Activation and Ca2+Release from Intracellular Stores in Human Granulocytes* , 1998, The Journal of Biological Chemistry.

[29]  M. Adams,et al.  Lycotoxins, Antimicrobial Peptides from Venom of the Wolf SpiderLycosa carolinensis * , 1998, The Journal of Biological Chemistry.

[30]  D. Andreu,et al.  Animal antimicrobial peptides: an overview. , 1998, Biopolymers.

[31]  M. Poot,et al.  Bacterial viability and antibiotic susceptibility testing with SYTOX green nucleic acid stain , 1997, Applied and environmental microbiology.

[32]  M. Dathe,et al.  Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides , 1997, FEBS letters.

[33]  C. Legros,et al.  Les toxines de scorpion , 1997 .

[34]  A. Ménez,et al.  [Structures and functions of animal toxins]. , 1997, Comptes rendus des seances de la Societe de biologie et de ses filiales.

[35]  P. Fehlbaum,et al.  Characterization of Novel Cysteine-rich Antimicrobial Peptides from Scorpion Blood* , 1996, The Journal of Biological Chemistry.

[36]  M. Vaara,et al.  Group of peptides that act synergistically with hydrophobic antibiotics against gram-negative enteric bacteria , 1996, Antimicrobial agents and chemotherapy.

[37]  M. Bibby,et al.  Antimicrobial activity of cecropins. , 1996, The Journal of antimicrobial chemotherapy.

[38]  M. Danilenko,et al.  The assembly of neutrophil NADPH oxidase: effects of mastoparan and its synthetic analogues. , 1995, The Biochemical journal.

[39]  N. Fujii,et al.  Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2. , 1995, Biochemistry.

[40]  W. Maloy,et al.  Structure–activity studies on magainins and other host defense peptides , 1995, Biopolymers.

[41]  R. Hancock,et al.  The interaction of a recombinant cecropin/melittin hybrid peptide with the outer membrane of Pseudomonas aeruginosa , 1994, Molecular microbiology.

[42]  Y. Shai.  Pardaxin: channel formation by a shark repellant peptide from fish. , 1994, Toxicology.

[43]  A. Mor,et al.  The NH2-terminal alpha-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity. , 1994, The Journal of biological chemistry.

[44]  A. Ménez,et al.  Purification and characterization of a scorpion defensin, a 4kDa antibacterial peptide presenting structural similarities with insect defensins and scorpion toxins. , 1993, Biochemical and biophysical research communications.

[45]  Franky R. G. Terras,et al.  Analysis of two novel classes of plant antifungal proteins from radish (Raphanus sativus L.) seeds. , 1992, The Journal of biological chemistry.

[46]  C. Bronner,et al.  G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides. , 1990, Trends in pharmacological sciences.

[47]  J. Vanderleyden,et al.  An automated quantitative assay for fungal growth inhibition , 1990 .

[48]  F. Lutz,et al.  Pseudomonas aeruginosa cytotoxin: the influence of sphingomyelin on binding and cation permeability increase in mammalian erythrocytes. , 1989, Toxicon : official journal of the International Society on Toxinology.

[49]  M. Zasloff,et al.  Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor , 1987 .

[50]  D. Eisenberg.  Three-dimensional structure of membrane and surface proteins. , 1984, Annual review of biochemistry.

[51]  C. Kitada,et al.  A new mast cell degranulating peptide "mastoparan" in the venom of Vespula lewisii. , 1979, Chemical & pharmaceutical bulletin.

[52]  L. J. Cole,et al.  Antibacterial Action of Melittin, a Polypeptide from Bee Venom , 1968, Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine.