Structure-microbicidal activity relationship of synthetic fragments derived from the antibacterial α-helix of human lactoferrin

Antimicrobial Agents and Chemotherapy

Volumn 54, Issue 1, 2010, Pages 418-425

  Haversen L ^a   Kondori, N ^a   Baltzer, L ^b,c   Hanson, L A ^a   Dolphin, G T ^b   Duner K ^a   Mattsby Baltzer, I ^a  

^a UNIVERSITY OF GOTHENBURG   (Sweden)

^b LINKÖPING UNIVERSITY   (Sweden)

^c UPPSALA UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ANTIINFECTIVE AGENT; ARGININE; ASPARAGINE; CYSTEINE; GLUTAMINE; LACTOFERRIN; LEUCINE; LIPID A; LIPOPOLYSACCHARIDE; LYSINE; LYSYLCYSTEINYLPHENYLALANYLGLUTAMINYLTRYPTOPHANYLGLUTAMINYLARGINYLASPARAGINYLMETHIONYLARGINYLLYSYLVALYLARGININE; SODIUM CHLORIDE; TRYPTOPHAN; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANTIMICROBIAL ACTIVITY; ARTICLE; CANDIDA ALBICANS; CONTROLLED STUDY; ESCHERICHIA COLI; NONHUMAN; PH MEASUREMENT; PRIORITY JOURNAL; STAPHYLOCOCCUS AUREUS; SUBSTITUTION REACTION;

AMINO ACID SEQUENCE; AMINO ACIDS; ANTI-BACTERIAL AGENTS; CANDIDA ALBICANS; ESCHERICHIA COLI; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; LACTOFERRIN; LIMULUS TEST; LIPOPOLYSACCHARIDES; METALS; MICROBIAL SENSITIVITY TESTS; MILK, HUMAN; MOLECULAR MIMICRY; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; SODIUM CHLORIDE; STAPHYLOCOCCUS AUREUS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 73849146045     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00908-09     Document Type: Article

References (38)

1. Aguilera, O., H. Ostolaza, L. M. Quiros, and J. F. Fierro. 1999. Permeabilizing action of an antimicrobial lactoferricin-derived peptide on bacterial and artificial membranes. FEBS Lett. 462:273-277.
2. Anderson, B. F., H. M. Baker, G. E. Norris, D. W. Rice, and E. N. Baker. 1989. Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8 Å resolution. J. Mol. Biol. 209:711-734.
3. Appelmelk, B. J., Y. Q. An, M. Geerts, B. G. Thijs, H. A. de Boer, D. M. MacLaren, J. de Graaff, and J. H. Nuijens. 1994. Lactoferrin is a lipid A-binding protein. Infect. Immun. 62:2628-2632.
4. Bellamy, W., M. Takase, K. Yamauchi, H. Wakabayashi, K. Kawase, and M. Tomita. 1992. Identification of the bactericidal domain of lactoferrin. Biochim. Biophys. Acta 1121:130-136.
5. Chapple, D. S., R. Hussain, C. L. Joannou, R. E. Hancock, E. Odell, R. W. Evans, and G. Siligardi. 2004. Structure and association of human lactoferrin peptides with Escherichia coli lipopolysaccharide. Antimicrob. Agents Chemother. 48:2190-2198.
6. Chapple, D. S., C. L. Joannou, D. J. Mason, J. K. Shergill, E. W. Odell, V. Gant, and R. W. Evans. 1998. A helical region on human lactoferrin - its role in antibacterial pathogenesis. Adv. Exp. Med. Biol. 443:215-220.
7. Chen, P. W., C. L. Shyu, and F. C. Mao. 2003. Antibacterial activity of short hydrophobic and basic-rich peptides. Am. J. Vet. Res. 64:1088-1092.
8. Crowhurst, K. A., and J. D. Forman-Kay. 2003. Aromatic and methyl NOEs highlight hydrophobic clustering in the unfolded state of an SH3 domain. Biochemistry 42:8687-8695.
9. Elass-Rochard, E., A. Roseanu, D. Legrand, M. Trif, V. Salmon, C. Motas, J. Montreuil, and G. Spik. 1995. Lactoferrin-lipopolysaccharide interaction: involvement of the 28-34 loop region of human lactoferrin in the high-affinity binding to Escherichia coli 055B5 lipopolysaccharide. Biochem. J. 312:839-845.
10. Ellison, R. T., III, T. J. Giehl, and F. M. LaForce. 1988. Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin. Infect. Immun. 56:2774-2781.
11. Faber, C., H. P. Stallmann, D. M. Lyaruu, U. Joosten, C. von Eiff, A. van Nieuw Amerongen, and P. I. Wuisman. 2005. Comparable efficacies of the antimicrobial peptide human lactoferrin 1-11 and gentamicin in a chronic methicillin-resistant Staphylococcus aureus osteomyelitis model. Antimicrob. Agents Chemother. 49:2438-2444.
12. Farnaud, S., A. Patel, E. W. Odell, and R. W. Evans. 2004. Variation in antimicrobial activity of lactoferricin-derived peptides explained by structure modelling. FEMS Microbiol. Lett. 238:221-226.
13. Farnaud, S., C. Spiller, L. C. Moriarty, A. Patel, V. Gant, E. W. Odell, and R. W. Evans. 2004. Interactions of lactoferricin-derived peptides with LPS and antimicrobial activity. FEMS Microbiol. Lett. 233:193-199.
14. Goldman, M. J., G. M. Anderson, E. D. Stolzenberg, U. P. Kari, M. Zasloff, and J. M. Wilson. 1997. Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 88:553-560.
15. Hancock, R. E., and D. S. Chapple. 1999. Peptide antibiotics. Antimicrob. Agents Chemother. 43:1317-1323.
16. Håversen, L., B. G. Ohlsson, M. Hahn-Zoric, L. A. Hanson, and I. Mattsby-Baltzer. 2002. Lactoferrin down-regulates the LPS-induced cytokine production in monocytic cells via NF-kappa B. Cell Immunol. 220:83-95.
17. Håversen, L. A., L. Baltzer, G. Dolphin, L. A. Hanson, and I. Mattsby-Baltzer. 2003. Anti-inflammatory activities of human lactoferrin in acute dextran sulphate-induced colitis in mice. Scand. J. Immunol. 57:2-10.
18. Håversen, L. A., I. Engberg, L. Baltzer, G. Dolphin, L. A. Hanson, and I. Mattsby-Baltzer. 2000. Human lactoferrin and peptides derived from a surface-exposed helical region reduce experimental Escherichia coli urinary tract infection in mice. Infect. Immun. 68:5816-5823.
19. Hunter, H. N., A. R. Demcoe, H. Jenssen, T. J. Gutteberg, and H. J. Vogel. 2005. Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent. Antimicrob. Agents Chemother. 49:3387-3395.
20. Japelj, B., P. Pristovsek, A. Majerle, and R. Jerala. 2005. Structural origin of endotoxin neutralization and antimicrobial activity of a lactoferrin-based peptide. J. Biol. Chem. 280:16955-16961.
21. Klein-Seetharaman, J., M. Oikawa, S. B. Grimshaw, J. Wirmer, E. Duchardt, T. Ueda, T. Imoto, L. J. Smith, C. M. Dobson, and H. Schwalbe. 2002. Long-range interactions within a nonnative protein. Science 295:1719-1722.
22. Lupetti, A., A. Paulusma-Annema, M. M. Welling, S. Senesi, J. T. van Dissel, and P. H. Nibbering. 2000. Candidacidal activities of human lactoferrin peptides derived from the N terminus. Antimicrob. Agents Chemother. 44:3257-3263.
23. Mann, D. M., E. Romm, and M. Migliorini. 1994. Delineation of the glycosaminoglycan-binding site in the human inflammatory response protein lactoferrin. J. Biol. Chem. 269:23661-23667.
24. Morrison, D. C., and D. M. Jacobs. 1976. Binding of polymyxin B to the lipid A portion of bacterial lipopolysaccharides. Immunochemistry 13:813-818.
25. Naidu, S. S., U. Svensson, A. R. Kishore, and A. S. Naidu. 1993. Relationship between antibacterial activity and porin binding of lactoferrin in Escherichia coli and Salmonella typhimurium. Antimicrob. Agents Chemother. 37:240-245.
26. Nibbering, P. H., E. Ravensbergen, M. M. Welling, L. A. van Berkel, P. H. van Berkel, E. K. Pauwels, and J. H. Nuijens. 2001. Human lactoferrin and peptides derived from its N terminus are highly effective against infections with antibiotic-resistant bacteria. Infect. Immun. 69:1469-1476.
27. Odell, E. W., R. Sarra, M. Foxworthy, D. S. Chapple, and R. W. Evans. 1996. Antibacterial activity of peptides homologous to a loop region in human lactoferrin. FEBS Lett. 382:175-178.
28. Porter, E. M., E. van Dam, E. V. Valore, and T. Ganz. 1997. Broad-spectrum antimicrobial activity of human intestinal defensin 5. Infect. Immun. 65:2396-2401.
29. Schibli, D. J., R. F. Epand, H. J. Vogel, and R. M. Epand. 2002. Tryptophanrich antimicrobial peptides: comparative properties and membrane interactions. Biochem. Cell Biol. 80:667-677.
30. Stallmann, H. P., C. Faber, A. L. Bronckers, J. M. de Blieck-Hogervorst, C. P. Brouwer, A. V. Amerongen, and P. I. Wuisman. 2005. Histatin and lactoferrin derived peptides: Antimicrobial properties and effects on mammalian cells. Peptides 26:2355-2359.
31. Tanida, T., T. Okamoto, E. Ueta, T. Yamamoto, and T. Osaki. 2006. Antimicrobial peptides enhance the candidacidal activity of antifungal drugs by promoting the efflux of ATP from Candida cells. J. Antimicrob. Chemother. 57:94-103.
32. Viejo-Diaz, M., M. T. Andres, J. Perez-Gil, M. Sanchez, and J. F. Fierro. 2003. Potassium efflux induced by a new lactoferrin-derived peptide mimicking the effect of native human lactoferrin on the bacterial cytoplasmic membrane. Biochemistry (Moscow) 68:217-227.
33. Vogel, H. J., D. J. Schibli, W. Jing, E. M. Lohmeier-Vogel, R. F. Epand, and R. M. Epand. 2002. Towards a structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides. Biochem. Cell Biol. 80:49-63.
34. Vorland, L. H. 1999. Lactoferrin: a multifunctional glycoprotein. APMIS 107:971-981.
35. Vorland, L. H., H. Ulvatne, J. Andersen, H. H. Haukland, O. Rekdal, J. S. Svendsen, and T. J. Gutteberg. 1999. Antibacterial effects of lactoferricin B. Scand. J. Infect. Dis. 31:179-184.
36. Wessolowski, A., M. Bienert, and M. Dathe. 2004. Antimicrobial activity of arginine- and tryptophan-rich hexapeptides: the effects of aromatic clusters, D-amino acid substitution and cyclization. J. Pept. Res. 64:159-169.
37. Yamauchi, K., M. Tomita, T. J. Giehl, and R. T. Ellison, 3rd. 1993. Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect. Immun. 61:719-728.
38. Zhang, G. H., D. M. Mann, and C. M. Tsai. 1999. Neutralization of endotoxin in vitro and in vivo by a human lactoferrin-derived peptide. Infect. Immun. 67:1353-1358.