δ-hemolysin, an update on a membrane-interacting peptide

Peptides

Volumn 30, Issue 4, 2009, Pages 817-823

  Verdon, Julien ^a   Girardin, Nicolas ^a   Lacombe, Christian ^a   Berjeaud, Jean Marc ^a   Héchard, Yann ^a  

^a UNIVERSITÉ DE POITIERS   (France)

Author keywords

Antimicrobial; Bacteria; Curvature strain; Detergent; Erythrocyte; Hemolysis; Pore; Staphylococcus

Indexed keywords

CHEMOKINE RECEPTOR CXCR6; DELTA HEMOLYSIN; HEMOLYSIN; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

CYTOLYSIS; ESCHERICHIA COLI; GENE EXPRESSION; HEMOLYSIS; NONHUMAN; PRIORITY JOURNAL; REVIEW; STAPHYLOCOCCUS AUREUS;

AMINO ACID SEQUENCE; ANIMALS; BACTERIAL PROTEINS; CELL MEMBRANE; HEMOLYSIN PROTEINS; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP;

ESCHERICHIA COLI; LEGIONELLA; STAPHYLOCOCCUS; STAPHYLOCOCCUS AUREUS;

EID: 62749134453     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2008.12.017     Document Type: Review

References (55)

1. Almeida P.F., Vaz W.L., and Thompson T.E. Lateral diffusion in the liquid phases of dimyristoylphosphatidylcholine/cholesterol lipid bilayers: a free volume analysis. Biochemistry 31 (1992) 6739-6747
2. Alouf J.E., Dufourcq J., Siffert O., Thiaudiere E., and Geoffroy C. Interaction of staphylococcal delta-toxin and synthetic analogues with erythrocytes and phospholipid vesicles. Biological and physical properties of the amphipathic peptides. Eur J Biochem 183 (1989) 381-390
3. Balaban N., and Novick R.P. Translation of RNAIII, the Staphylococcus aureus agr regulatory RNA molecule, can be activated by a 3′-end deletion. FEMS Microbiol Lett 133 (1995) 155-161
4. Bechinger B. The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. Biochim Biophys Acta 1462 (1999) 157-183
5. Bechinger B., and Lohner K. Detergent-like actions of linear amphipathic cationic antimicrobial peptides. Biochim Biophys Acta 1758 (2006) 1529-1539
6. Bernheimer A.W. Interactions between membranes and cytolytic bacterial toxins. Biochim Biophys Acta 465 (1974) 378-390
7. Bladon C.M., Bladon P., and Parkinson J.A. Delta-toxin analogues as peptide models for protein ion channels. Biochem Soc Trans 20 (1992) 862-864
8. Brauner J.W., Mendelsohn R., and Prendergast F.G. Attenuated total reflectance Fourier transform infrared studies of the interaction of melittin, two fragments of melittin, and delta-hemolysin with phosphatidylcholines. Biochemistry 26 (1987) 8151-8158
9. Colacicco G., Basu M.K., Buckelew Jr. A.R., and Bernheimer A.W. Surface properties of membrane systems. Transport of staphylococcal delta-toxin from aqueous to membrane phase. Biochim Biophys Acta 465 (1977) 378-390
10. Dhople V.M., and Nagaraj R. Conformation and activity of delta-lysin and its analogs. Peptides 26 (2005) 217-225
11. Dhople V.M., and Nagaraj R. Delta-toxin, unlike melittin, has only hemolytic activity and no antimicrobial activity: rationalization of this specific biological activity. Biosci Rep 13 (1993) 245-250
12. Dhople V.M., and Nagaraj R. Generation of analogs having potent antimicrobial and hemolytic activities with minimal changes from an inactive 16-residue peptide corresponding to the helical region of Staphylococcus aureus delta-toxin. Protein Eng 8 (1995) 315-318
13. Dinges M.M., Orwin P.M., and Schlievert P.M. Exotoxins of Staphylococcus aureus. Clin Microbiol Rev 13 (2000) 16-34
14. 31P-NMR study. Eur J Biochem 187 (1990) 581-587
15. Dufourcq J., Faucon J.F., Fourche G., Dasseux J.L., Le Maire M., and Gulik-Krzywicki T. Morphological changes of phosphatidylcholine bilayers induced by melittin: vesicularization, fusion, discoidal particles. Biochim Biophys Acta 859 (1986) 33-48
16. Fitton J.E., Dell A., and Shaw W.V. The amino acid sequence of the delta haemolysin of Staphylococcus aureus. FEBS Lett 115 (1980) 209-212
17. Fitton J.E., Hunt D.F., Marasco J., Shabanowitz J., Winston S., and Dell A. The amino acid sequence of delta haemolysin purified from a canine isolate of S. aureus. FEBS Lett 169 (1984) 25-29
18. Frazier M.L., Wright J.R., Pokorny A., and Almeida P.F. Investigation of domain formation in sphingomyelin/cholesterol/POPC mixtures by fluorescence resonance energy transfer and Monte Carlo simulations. Biophys J 92 (2007) 2422-2433
19. Geisinger E., Adhikari R.P., Jin R., Ross H.F., and Novick R.P. Inhibition of rot translation by RNAIII, a key feature of agr function. Mol Microbiol 61 (2006) 1038-1048
20. Ji G., Pei W., Zhang L., Qiu R., Lin J., Benito Y., et al. Staphylococcus intermedius produces a functional agr autoinducing peptide containing a cyclic lactone. J Bacteriol 187 (2005) 3139-3150
21. Kantor H.S., Temples B., and Shaw W.V. Staphylococcal delta hemolysin: purification and characterization. Arch Biochem Biophys 151 (1972) 142-156
22. Kerr I.D., Doak D.G., Sankararamakrishnan R., Breed J., and Sansom M.S. Molecular modelling of Staphylococcal delta-toxin ion channels by restrained molecular dynamics. Protein Eng 9 (1996) 161-171
23. Kerr I.D., Dufourcq J., Rice J.A., Fredkin D.R., and Sansom M.S. Ion channel formation by synthetic analogues of staphylococcal delta-toxin. Biochim Biophys Acta 1236 (1995) 219-227
24. Kreger A.S., Kim K.S., Zaboretzky F., and Bernheimer A.W. Purification and properties of staphylococcal delta hemolysin. Infect Immun 3 (1971) 449-465
25. Lee K.H., Fitton J.E., and Wuthrich K. Nuclear magnetic resonance investigation of the conformation of delta-haemolysin bound to dodecylphosphocholine micelles. Biochim Biophys Acta 911 (1987) 144-153
26. 31P nuclear magnetic resonance and Fourier transform infrared spectroscopic, and X-ray diffraction studies. Biochemistry 38 (1999) 16514-16528
27. Marks J., and Vaughan A.C. Staphylococcal delta-haemolysin. J Pathol Bacteriol 62 (1950) 597-615
28. Matsuzaki K., Murase O., Fujii N., and Miyajima K. Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore. Biochemistry 34 (1995) 6521-6526
29. McKevitt A.I., Bjornson G.L., Mauracher C.A., and Scheifele D.W. Amino acid sequence of a deltalike toxin from Staphylococcus epidermidis. Infect Immun 58 (1990) 1473-1475
30. Mehlin C., Headley C.M., and Klebanoff S.J. An inflammatory polypeptide complex from Staphylococcus epidermidis: isolation and characterization. J Exp Med 189 (1999) 907-918
31. Mellor I.R., Thomas D.H., and Sansom M.S. Properties of ion channels formed by Staphylococcus aureus delta-toxin. Biochim Biophys Acta 942 (1988) 280-294
32. Pokorny A., and Almeida P.F. Kinetics of dye efflux and lipid flip-flop induced by delta-lysin in phosphatidylcholine vesicles and the mechanism of graded release by amphipathic, alpha-helical peptides. Biochemistry 43 (2004) 8846-8857
33. Pokorny A., and Almeida P.F. Permeabilization of raft-containing lipid vesicles by delta-lysin: a mechanism for cell sensitivity to cytotoxic peptides. Biochemistry 44 (2005) 9538-9544
34. Pokorny A., Birkbeck T.H., and Almeida P.F. Mechanism and kinetics of delta-lysin interaction with phospholipid vesicles. Biochemistry 41 (2002) 11044-11056
35. Pokorny A., Kilelee E.M., Wu D., and Almeida P.F. The activity of the amphipathic peptide delta-lysin correlates with phospholipid acyl chain structure and bilayer elastic properties. Biophys J (2008)
36. Pokorny A., Yandek L.E., Elegbede A.I., Hinderliter A., and Almeida P.F. Temperature and composition dependence of the interaction of delta-lysin with ternary mixtures of sphingomyelin/cholesterol/POPC. Biophys J 91 (2006) 2184-2197
37. 31P-NMR study. Biophys J 68 (1995) 965-977
38. Pott T., Dufourcq J., and Dufourc E.J. Fluid or gel phase lipid bilayers to study peptide-membrane interactions?. Eur Biophys J 25 (1996) 55-59
39. Raghunathan G., Seetharamulu P., Brooks B.R., and Guy H.R. Models of delta-hemolysin membrane channels and crystal structures. Proteins 8 (1990) 213-225
40. Rietveld A., and Simons K. The differential miscibility of lipids as the basis for the formation of functional membrane rafts. Biochim Biophys Acta 1376 (1998) 467-479
41. Ryu K.S., Han H.S., and Kim H. Interaction of glucagon with dimyristoylphosphatidylcholine in vesicular and discoidal complexes. J Biochem 123 (1998) 55-61
42. Sankaram M.B., and Thompson T.E. Cholesterol-induced fluid-phase immiscibility in membranes. Proc Natl Acad Sci USA 88 (1991) 8686-8690
43. Sankaram M.B., and Thompson T.E. Interaction of cholesterol with various glycerophospholipids and sphingomyelin. Biochemistry 29 (1990) 10670-10675
44. Sengupta D., Leontiadou H., Mark A.E., and Marrink S.J. Toroidal pores formed by antimicrobial peptides show significant disorder. Biochim Biophys Acta (2008)
45. Silvestro L., and Axelsen P.H. Membrane-induced folding of cecropin A. Biophys J 79 (2000) 1465-1477
46. Simons K., and Ikonen E. Functional rafts in cell membranes. Nature 387 (1997) 569-572
47. Talbot J.C., Thiaudiere E., Vincent M., Gallay J., Siffert O., and Dufourcq J. Dynamics and orientation of amphipathic peptides in solution and bound to membranes: a steady-state and time-resolved fluorescence study of staphylococcal delta-toxin and its synthetic analogues. Eur Biophys J 30 (2001) 147-161
48. 1H NMR study of the solution structure of delta-hemolysin. Biochemistry 27 (1988) 1643-1647
49. Tegmark K., Morfeldt E., and Arvidson S. Regulation of agr-dependent virulence genes in Staphylococcus aureus by RNAIII from coagulase-negative staphylococci. J Bacteriol 180 (1998) 3181-3186
50. Thelestam M. Membrane damage by staphylococcal alpha-toxin to different types of cultured mammalian cell. Biochim Biophys Acta 762 (1983) 481-488
51. Thelestam M., and Mollby R. Determination of toxin-induced leakage of different-size nucleotides through the plasma membrane of human diploid fibroblasts. Infect Immun 11 (1975) 640-648
52. Thiaudiere E., Siffert O., Talbot J.C., Bolard J., Alouf J.E., and Dufourcq J. The amphiphilic alpha-helix concept. Consequences on the structure of staphylococcal delta-toxin in solution and bound to lipids. Eur J Biochem 195 (1991) 203-213
53. Verdon J., Berjeaud J.M., Lacombe C., and Hechard Y. Characterization of anti-Legionella activity of warnericin RK and delta-lysin I from Staphylococcus warneri. Peptides 29 (2008) 978-984
54. Williams R.E.O., and Harper G.J. Staphylococcal haemolysins on sheep-blood agar with evidence for a fourth haemolysin. J Pathol Bacteriol 59 (1947) 69-78
55. Wiseman G.M. The hemolysins of Staphylococcus aureus. Bacteriol Rev 39 (1975) 317-344