Detergent-like activity and a-helical structure of warnericin RK, an anti-Legionella peptide

Biophysical Journal

Volumn 97, Issue 7, 2009, Pages 1933-1940

  Verdon, Julien ^a   Falge, Mirjam ^b   Maier, Elke ^c   Bruhn, Heike ^b   Steinert, Michael ^d   Faber, Cornelius ^e   Benz, Roland ^f   Héchard, Yann ^a  

^a UNIVERSITÉ DE POITIERS   (France)

^b UNIVERSITY OF WÜRZBURG   (Germany)

^c UNIVERSITY OF WÜRZBURG   (Germany)

^d TECHNICAL UNIVERSITY OF BRAUNSCHWEIG   (Germany)

^e UNIVERSITY HOSPITAL MÜNSTER   (Germany)

^f JACOBS UNIVERSITY BREMEN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMPHOPHILE; DELTA LYSIN; DETERGENT; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; WARNERICIN RK; ANTIMICROBIAL CATIONIC PEPTIDE; ION CHANNEL;

ALPHA HELIX; ARTICLE; BACTERIAL CELL; CIRCULAR DICHROISM; ERYTHROCYTE; HEMOLYSIS; HUMAN; HUMAN CELL; LEGIONELLA PNEUMOPHILA; MEMBRANE PERMEABILITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN STRUCTURE; STAPHYLOCOCCUS; ARTIFICIAL MEMBRANE; CELL MEMBRANE; CHEMISTRY; CYTOLOGY; DRUG EFFECT; ELECTRIC CONDUCTIVITY; ENZYME SPECIFICITY; LEGIONELLA; LIPID BILAYER; METABOLISM; OSMOSIS; PERMEABILITY; PROTEIN SECONDARY STRUCTURE;

BACTERIA (MICROORGANISMS); LEGIONELLA; LEGIONELLA PNEUMOPHILA; STAPHYLOCOCCUS;

ANTIMICROBIAL CATIONIC PEPTIDES; CELL MEMBRANE; CIRCULAR DICHROISM; DETERGENTS; ELECTRIC CONDUCTIVITY; HUMANS; ION CHANNELS; LEGIONELLA; LIPID BILAYERS; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANES, ARTIFICIAL; OSMOSIS; PERMEABILITY; PROTEIN STRUCTURE, SECONDARY; SUBSTRATE SPECIFICITY;

EID: 70350006751     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.06.053     Document Type: Article

References (33)

1. Aerts, A. M., I. E. Francois, B. P. Cammue, and K. Thevissen. 2008. The mode of antifungal action of plant, insect and human defensins. Cell. Mol. Life Sci. 65:2069-2079.
2. Bowdish, D. M., D. J. Davidson, and R. E. Hancock. 2006. Immuno-modulatory properties of defensins and cathelicidins. Curr. Top. Microbiol. Immunol. 306:27-66.
3. Hancock, R. E., and R. Lehrer. 1998. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 16:82-88.
4. Kagan, B. L., T. Ganz, and R. I. Lehrer. 1994. Defensins: a family of antimicrobial and cytotoxic peptides. Toxicology. 87:131-149.
5. Lehrer, R. I. 2004. Primate defensins. Nat. Rev. Microbiol. 2:727-738.
6. Brogden, K. A. 2005. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3:238-250.
7. Bechinger, B., and K. Lohner. 2006. Detergent-like actions of linear amphipathic cationic antimicrobial peptides. Biochim. Biophys. Acta. 1758:1529-1539.
8. Shai, Y. 1999. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by a-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta. 1462:55-70.
9. Verdon, J., J. M. Berjeaud, C. Lacombe, and Y. Hechard. 2008. Characterization of anti-Legionella activity of warnericin RK and δ-lysin I from Staphylococcus warneri. Peptides. 29:978-984.
10. Fields, B. S., R. F. Benson, and R. E. Besser. 2002. Legionella and Legionnaires' disease: 25 years of investigation. Clin. Microbiol. Rev. 15:506-526.
11. Steinert, M., U. Hentschel, and J. Hacker. 2002. Legionella pneumophila: an aquatic microbe goes astray. FEMS Microbiol. Rev. 26:149-162.
12. Wiseman, G. M. 1975. The hemolysins of Staphylococcus aureus. Bacteriol. Rev. 39:317-344.
13. Dhople, V. M., and R. Nagaraj. 1993. δ-Toxin, unlike melittin, has only hemolytic activity and no antimicrobial activity: rationalization of this specific biological activity. Biosci. Rep. 13:245-250.
14. Kreger, A. S., K. S. Kim, F. Zaboretzky, and A. W. Bernheimer. 1971. Purification and properties of staphylococcal δ hemolysin. Infect. Immun. 3:449-465.
15. Verdon, J., N. Girardin, C. Lacombe, J. M. Berjeaud, and Y. Hechard. 2009. δ-Hemolysin, an update on a membrane-interacting peptide. Peptides. 30:817-823.
16. Thelestam, M. 1983. Membrane damage by staphylococcal α-toxin to different types of cultured mammalian cell. Biochim. Biophys. Acta. 762:481-488.
17. Pokorny, A., and P. F. Almeida. 2005. Permeabilization of raft-containing lipid vesicles by δ-lysin: a mechanism for cell sensitivity to cytotoxic peptides. Biochemistry. 44:9538-9544. (Pubitemid 40962052)
18. Pokorny, A., T. H. Birkbeck, and P. F. Almeida. 2002. Mechanism and kinetics of δ-lysin interaction with phospholipid vesicles. Biochemistry. 41:11044-11056. (Pubitemid 35001219)
19. Pokorny, A., E. M. Kilelee, D. Wu, and P. F. Almeida. 2008. The activity of the amphipathic peptide δ-lysin correlates with phospholipid acyl chain structure and bilayer elastic properties. Biophys. J. 95:4748-4755.
20. Benz, R., K. Janko, W. Boos, and P. Lauger. 1978. Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli. Biochim. Biophys. Acta. 511:305-319.
21. Benz, R., K. Janko, and P. Lauger. 1979. Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli. Biochim. Biophys. Acta. 551:238-247.
22. Ludwig, A., A. Schmid, R. Benz, and W. Goebel. 1991. Mutations affecting pore formation by haemolysin from Escherichia coli. Mol. Gen. Genet. 226:198-208.
23. Wütrhrich, K. 1986. NMR of Proteins and Nucleic Acids. Wiley, New York.
24. Linge, J. P., M. Habeck, W. Rieping, and M. Nilges. 2003. ARIA: automated NOE assignment and NMR structure calculation. Bioinformatics. 19:315-316.
25. Duclohier, H., and H. Wroblewski. 2001. Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues. J. Membr. Biol. 184:1-12.
26. Sahl, H. G., M. Kordel, and R. Benz. 1987. Voltage-dependent depolarization of bacterial membranes and artificial lipid bilayers by the peptide antibiotic nisin. Arch. Microbiol. 149:120-124.
27. Benz, R., A. Schmid, and R. E. Hancock. 1985. Ion selectivity of Gramnegative bacterial porins. J. Bacteriol. 162:722-727. (Pubitemid 15059747)
28. Melo, M. N., R. Ferre, and M. A. Castanho. 2009. Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations. Nat. Rev. Microbiol. 7:245-250.
29. Lee, K. H., J. E. Fitton, and K. Wuthrich. 1987. Nuclear magnetic resonance investigation of the conformation of δ-haemolysin bound to dodecylphosphocholine micelles. Biochim. Biophys. Acta. 911:144-153.
30. Tappin, M. J., A. Pastore, R. S. Norton, J. H. Freer, and I. D. Campbell. 1988. High-resolution 1H NMR study of the solution structure of δ-hemolysin. Biochemistry. 27:1643-1647.
31. Mellor, I. R., D. H. Thomas, and M. S. Sansom. 1988. Properties of ion channels formed by Staphylococcus aureus δ-toxin. Biochim. Biophys. Acta. 942:280-294.
32. Kerr, I. D., J. Dufourcq, J. A. Rice, D. R. Fredkin, and M. S. Sansom. 1995. Ion channel formation by synthetic analogues of staphylococcal δ-toxin. Biochim. Biophys. Acta. 1236:219-227.
33. Finnerty, W. R., R. A. Makula, and J. C. Feeley. 1979. Cellular lipids of the Legionnaires' disease bacterium. Ann. Intern. Med. 90:631-634.