Initial Binding Sites of Antimicrobial Peptides in Staphylococcus aureus and Escherichia coli

References

• Steiner H, Hultmark D, Engstrøm Å, Bennich H, Boman HG. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 1981; 292: 246–8.
   Google Scholar
• Selsted ME, Brown DM, DeLange RJ, Lehrer RI. Primary structures of MCP-1 and MCP-2, natural peptide antibiotics of rabbit lung macrophages. J Biol Chem 1983; 258: 14485–9.
   PubMed Web of Science ®Google Scholar
• Zasloff M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc Natl Acad Sci USA 1987; 84: 5449–53.
   PubMed Web of Science ®Google Scholar
• Lee J-Y, Boman A, Sun C, Andersson M, Jørnvall H, Mutt V, et al. Antibacterial peptides from pig intestine: isolation of a mammalian cecropin. Proc Natl Acad Sci USA 1989; 86: 9159–62.
   PubMed Web of Science ®Google Scholar
• Lambert J, Keppi E, Dimarcq JL, Wicker C, Reichhart JM, Dunbar B, et al. Insect immunity: isolation from immune blood of the dipteran Phormia terranovae of two insect antibacterial peptides with sequence homology to rabbit lung macrophage bactericidal peptides. Proc Natl Acad Sci USA 1989; 86: 262–6.
   PubMed Web of Science ®Google Scholar
• Matsuyama K, Natori S. Purification of three antibacterial proteins from the culture medium of NIH-Sape-4, an embryonic cell line in Sarcophaga peregrina. J Biol Chem 1988; 263: 17112–6.
   PubMed Web of Science ®Google Scholar
• Diamond G, Zasloff M, Eck H, Bressaur M, Maloy WL, Bevins CL. Tracheal antimicrobial peptide, a novel cysteinerich peptide from mammalian tracheal mucosa: peptide isolation and cloning of cDNA. Proc Natl Acad Sci USA 1991; 88: 3952–6.
   PubMed Web of Science ®Google Scholar
• Juretic D. Antimicrobial peptides of the magainin family: membrane depolarization studies on E. coli and cytochrome oxidase liposomes. Studia Biophysica 1990; 138: 79–86.
   Google Scholar
• Westerhoff HV, Juretic D, Hendler RW, Zasloff M. Magainin and the disruption of membrane-linked free-energy transduction. Proc Natl Acad Sci USA 1989; 86: 6597–601.
   PubMed Web of Science ®Google Scholar
• Piers KL, Brown MH, Hancock REW. Improvement of the outer membrane-permeabilizing and lipopolysaccharide-binding activities of an antimicrobial cationic peptide by C-terminal modification. Antimicrob Agents Chemother 1994; 38: 2311–6.
   Google Scholar
• Bellamy W, Takase M, Wakabayashi H, Kawase K, Tomita M. Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J Appl Bacteriol 1992; 73: 72–9.
   Google Scholar
• Vorland LH, Ulvatne H, Andersen J, Haukland HH, Rekdal Ø, Svendsen JS, et al. Antibacterial effects of lactoferricin B. Scand J Infect Dis 1999; 31: 179–84.
   PubMed Web of Science ®Google Scholar
• Christensen B, Fink J, Merrifield RB, Mauzerall D. Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc Natl Acad Sci USA 1988; 85: 5072–6.
   PubMed Web of Science ®Google Scholar
• Steiner H, Andreu D, Merrifield RB. Binding and action of cecropin and cecropin analogues: antibacterial peptides from insects. Biochim Biophys Acta 1988; 939: 260–6.
   Google Scholar
• Tomita M, Bellamy W, Takase M, Yamauchi K, Wakabayashi H, Kawase K. Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin. J Dairy Sci 1991; 74: 4137–42.
   PubMed Web of Science ®Google Scholar
• Bellamy W, Takase M, Yamauchi K, Wakabayashi H, Kawase K, Tomita M. Identification of the bactericidal domain of lactoferrin. Biochim Biophys Acta 1992; 1121: 130–6.
   PubMed Web of Science ®Google Scholar
• Bellamy W, Wakabayashi H, Takase M, Kawase K, Shimamura S, Tomita M. Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin. Med Microbiol Immunol 1993; 182: 97–105.
   PubMed Web of Science ®Google Scholar
• Isamida T, Tanaka T, Omata Y, Yamauchi K, Shimazaki K, Saiko A. Protective effect of lactoferricin against Toxoplasma gondii infection in mice. J Vet Med Sci 1998; 60: 241–4.
   PubMed Web of Science ®Google Scholar
• Turchany JM, Aley SB, Gillin FC. Giardicidal activity of lactoferrin and N-terminal peptides. Infect Immun 1995; 63: 4550–2.
   PubMed Web of Science ®Google Scholar
• Yoo Y-C, Watanabe S, Watanabe R, Hatu K, Shimazaki K, Azuma I. Bovine lactoferrin and lactoferricin, a peptide derived from bovine lactoferrin, inhibit tumor metastasis in mice. Jpn J Cancer Res 1997; 88: 184–90.
   Google Scholar
• Yamauchi K, Tomita M, Giehl TJ, Ellison III RT. Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect Immun 1993; 61: 719–28.
   Google Scholar
• Bessale R, Kapitovsky A, Gorea A, Shalit I, Fridkin M. All D-magainin-chirality, antimicrobial activity and proteolytic resistance. FEBS Lett 1990; 274: 151–4.
   Google Scholar
• Wade D, Boman A, Wahlin B, Drain CM, Andreu D, Boman HG, et al. All D-amino acid containing channel forming antibiotic peptides. Proc Natl Acad Sci USA 1990; 87: 4761–6.
   PubMed Web of Science ®Google Scholar
• Casteels P, Teemst P. Apidaecin-type peptide antibiotics function through a non-pore forming mechanism involving stereospecificity. Biochem Biophys Res Comm 1994; 199: 339–45.
   PubMed Web of Science ®Google Scholar
• Nikaido H, Vaara M. The molecular basis of bacterial outer membrane permeability. Microbiol Rev 1985; 49: 1–32.
   PubMedGoogle Scholar
• David SA, Mathan VI, Balaram P. Interaction of mellitin with endotoxic lipid A. Biochim Biophys Acta 1992; 1123: 269–74.
   PubMed Web of Science ®Google Scholar
• Rana FR, Macias EA, Sultany CM, Modzradowski MC, Blazyk J. Interactions between magainin 2 and Salmonella typhimurium outer membranes: effect of lipopolysaccharide structure. Biochemistry 1991; 30: 5858–66.
   Google Scholar
• Sawyer JG, Martin NL, Hancock REW. Interaction of macrophage cationic proteins with the outer membrane of Pseudomonas aeruginosa. Infect Immun 1988; 56: 693–8.
   Google Scholar
• Pooley HM, Karamata D. Teichoic acid synthesis in Bacillus subtilis: genetic organization and biological roles. In: Ghuyssen J-M, Hakenbeck R, eds. Bacterial cell wall. Amsterdam: Elsevier, 1994: 187–98.
   Google Scholar
• Fischer W, Koch UH. Alanyl lipoteichoic acid of Staphylococcus aureus: functional and dynamic aspects. Biochem Soc Trans 1985; 13: 984–6.
   PubMed Web of Science ®Google Scholar
• Koch UH, Haas R, Fischer W. The role of lipoteichoic acid biosynthesis in membrane lipid metabolism of growing Staphylococcus aureus. Eur J Biochem 1984; 138: 357–63.
   Google Scholar
• Labischinski H, Naumann D, Fischer W. Small and medium-angle X-ray analysis of bacterial lipoteichoic acid phase structure. Eur J Biochem 1991; 202: 1269–74.
   Google Scholar
• Amsterdam D. Susceptibility testing of antimicrobials in liquid media. In: Lorian V, ed. Antibiotics in laboratory medicine. 4th ed. Philadelphia: Williams and Wilkins, 1996: 75–8.
   Google Scholar
• Fischer W. Physiology of lipoteichoic acids in bacteria. Adv Microb Physiol 1988; 29: 233–302.
   PubMed Web of Science ®Google Scholar
• Knox KW, Wicken AJ. Immunological properties of teichoic acid. Bacteriol Rev 1973; 37: 215–57.
   PubMedGoogle Scholar
• Chapple DS, Masson DJ, Joannou CL, Odell EW, Gant V, Evans RW. Structure-function relationship of antibacterial synthetic peptides homologues to a helical surface region on human lactoferrin against Escherichia coli serotype O111. Infect Immun 1998; 66: 2434–40.
   PubMed Web of Science ®Google Scholar
• Elass-Rochard E, Roseanu A, Legrand D, Trif M, Salmon V, Motas C, et al. Lactoferrin–lipopolysaccharide interaction: involvement of the 28–34 loop region of human lactoferrin in the high-affinity binding to Escherichia coli O55B5 lipopolysaccharide. Biochem J 1995; 312: 839–45.
   Google Scholar