Physico-chemical and biophysical study of the interaction of hexa- and heptaacyl lipid A from Erwinia carotovora with magainin 2-derived antimicrobial peptides

Biochimica et Biophysica Acta - Biomembranes

Volumn 1778, Issue 10, 2008, Pages 2051-2057

  Fukuoka, Satoshi ^a   Howe, Jörg ^b   Andrä, Jörg ^b   Gutsmann, Thomas ^b   Rössle, Manfred ^c   Brandenburg, Klaus ^b  

^a AIST Shikoku   (Japan)

^b RESEARCH CENTER BORSTEL   (Germany)

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Antimicrobial peptide; Cytokine; Endotoxin neutralization; Lipid A; Lipopolysaccharide

Indexed keywords

BACTERIUM LIPOPOLYSACCHARIDE; LIPID A DERIVATIVE; MAGAININ 2; POLYPEPTIDE ANTIBIOTIC AGENT; TUMOR NECROSIS FACTOR ALPHA;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CHEMICAL STRESS; CYTOKINE PRODUCTION; DIFFERENTIAL SCANNING CALORIMETRY; ELECTROPHORETIC MOBILITY; GEL; HUMAN; HUMAN CELL; HYDROPHOBICITY; INFRARED SPECTROSCOPY; LIQUID; MONONUCLEAR CELL; NONHUMAN; PARAMETER; PECTOBACTERIUM CAROTOVORUM; PHASE TRANSITION; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN LIPID INTERACTION; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY; ZETA POTENTIAL;

ANIMALS; ANTI-INFECTIVE AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; HUMANS; LEUKOCYTES, MONONUCLEAR; LIPID A; PECTOBACTERIUM CAROTOVORUM; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TUMOR NECROSIS FACTOR-ALPHA; XENOPUS PROTEINS;

ANURA; NEGIBACTERIA; PECTOBACTERIUM CAROTOVORUM;

EID: 52049088942     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2008.03.022     Document Type: Article

References (42)

1. Rietschel E.Th., Seydel U., Zähringer U., Schade U.F., Brade L., Loppnow H., Feist W., Wang M.-H., Ulmer A.J., Flad H.-D., Brandenburg K., Kirikae T., Grimmecke D., Holst O., and Brade H. Bacterial endotoxin: molecular relationships between structure and activity. Infect. Dis. Clin. North Am. 5 (1991) 753-779
2. Dentener M.A., Von Asmuth E.J.U., Francot G.J.M., and Buurman W.A. Interaction between CD14 lipopolysaccharide binding protein and bactericidal/permeability-increasing protein during lipopolysaccharide-induced cell activation. Prog. Clin. Biol. Res. 388 (1994) 59-70
3. Hailman E., Lichenstein H.S., Wurfel M.M., Miller D.S., Johnson D.A., Kelley M., Busse L.A., Zukowski M.M., and Wright S.D. Lipopolysaccharide (LPS)-binding protein accelerates the binding of LPS to CD14. J. Exp. Med. 179 (1994) 269-277
4. Zähringer U., Salvetzki R., Ulmer A.J., and Rietschel E.Th. Isolation, chemical analysis and biological investigations of natural lipid A and lipid A-antagonists. J. Endotoxin Res. 3 Suppl. 1 (1996) 33
5. Fukuoka S., Brandenburg K., Müller M., Lindner B., Koch M.H.J., and Seydel U. Physico-chemical analysis of lipid A fractions of lipopolysaccharide from Erwinia carotovora in relation to bioactivity. Biochim. Biophys. Acta 1510 (2001) 185-197
6. Duclohier H., Molle G., and Spach G. Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers. Biophys. J. 56 (1989) 1017-1021
7. Haukland H.H., Ulvatne H., Sandvik K., and Vorland L.H. The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm. FEBS Lett. 508 (2001) 389-393
8. Cruciani R.A., Barker J.L., Durell S.R., Raghunathan G., Guy H.R., Zasloff M., and Stanley E.F. Magainin 2, a natural antibiotic from frog skin, forms ion channels in lipid bilayer membranes. Eur. J. Pharmacol. 226 (1992) 287-296
9. Matsuzaki K., Sugishita K., and Miyajima K. Interactions of an antimicrobial peptide, magainin 2, with lipopolysaccharide-containing liposomes as a model for outer membranes of Gram-negative bacteria. FEBS Lett. 449 (1999) 221-224
10. Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1462 (1999) 55-70
11. Matsuzaki K., Harada M., Funakoshi S., Fujii N., and Miyajima K. Physicochemical determinants for the interactions of magainins 1 and 2 with acidic lipid bilayers. Biochim. Biophys. Acta 1063 (1991) 162-170
12. Grant Jr. E., Beeler T.J., Taylor K.M.P., Gable K., and Roseman M.A. Mechanism of magainin 2a induced permeabilization of phospholipid vesicles. Biochemistry 31 (1992) 9912-9918
13. Rana F.R., and Blazyk J. Interactions between the antimicrobial peptide, magainin 2, and Salmonella typhimurium lipopolysaccharides. FEBS Lett. 293 (1991) 11-15
14. Rana F.R., Sultany C.M., and Blazyk J. Interactions between Salmonella thyphimurium lipopolysaccharide and the antimicrobial peptide, magainin 2 amide. FEBS Lett. 261 (1990) 464-467
15. Rana F.R., Macias E.A., Sultany C.M., Modzrakowski M.C., and Blazyk J. Interactions between magainin 2 and Salmonella typhimurium outer membranes: effect of lipopolysaccharide structure. Biochemistry 30 (1991) 5858-5866
16. Andrä J., Monreal D., Martinez d.T., Olak C., Brezesinski G., Gomez S.S., Goldmann T., Bartels R., Brandenburg K., and Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens. J. Biol. Chem. 282 (2007) 14719-14728
17. Blondelle S.E., and Houghten R.A. Design of model amphipathic peptides having potent antimicrobial activities. Biochemistry 31 (1992) 12688-12694
18. Fukuoka S., Kamishima H., Sode K., and Karube I. Extracellular lipopolysaccharide production by Erwinia carotovora. J. Ferment. Bioeng. 68 (1989) 320-324
19. Fukuoka S., Kamishima H., Nagawa Y., Nakashini H., Ishikawa K., Niwa Y., Tamiya E., and Karube I. Structural characterization of lipid A component of Erwinia carotovora lipopolysaccharide. Arch. Microbiol. 157 (1992) 311-318
20. Brandenburg K., Kusumoto S., and Seydel U. Conformational studies of synthetic lipid A analogues and partial structures by infrared spectroscopy. Biochim. Biophys. Acta 1329 (1997) 193-201
21. Brandenburg K., Jürgens G., Müller M., Fukuoka S., and Koch M.H.J. Biophysical characterization of lipopolysaccharide and lipid A inactivation by lactoferrin. Biol. Chem. 382 (2001) 1215-1225
22. Koch M.H.J. Instruments and methods for small-angle scattering with synchrotron radiation. Makromol. Chem., Macromol. Symp. 15 (1988) 79-90
23. Rössle M., Kläring R., Ristau U., Bobrahn B., Jahn D., Gehrmann T., Konarev P., Round A., Fiedler S., Hermes C., and Svergun D. Upgrade of the small-angle X-ray scattering beamline at the European Molecular Biology Laboratory, Hamburg. J. Appl. Crystallogr. 40 (2007) s190-s194
24. Andrä J., Lamata M., Martinez de Tejada G., Bartels R., Koch M.H.J., and Brandenburg K. Cyclic antimicrobial peptides based on Limulus anti-lipopolysaccharide factor for neutralization of lipopolysaccharide. Biochem. Pharmacol. 68 (2004) 1297-1307
25. Feist W., Ulmer A.J., Musehold J., Brade H., Kusumoto S., and Flad H.-D. Induction of tumor necrosis factor-alpha release by lipopolysaccharide and defined lipopolysaccharide partial structures. Immunobiology 179 (1989) 293-307
26. Schromm A.B., Brandenburg K., Loppnow H., Zähringer U., Rietschel E.T.h., Carroll S.F., Koch M.H.J., Kusumoto S., and Seydel U. The charge of endotoxin molecules influences their conformation and interleukin-6 inducing capacity. J. Immunol. 161 (1998) 5464-5471
27. Brandenburg K., and Wiese A. Endotoxins: relationships between structure, function, and activity. Curr. Top. Med. Chem. 4 (2004) 1127-1146
28. Fukuoka S., Knirel Y.A., Lindner B., Moll H., Seydel U., and Zähringer U. Elucidation of the structure of the core region and the complete structure of the R-type lipopolysaccharide of Erwinia carotovora FERM P-7576. Eur. J. Biochem. 250 (1997) 55-62
29. Giacometti A., Cirioni O., Barchiesi F., Del Prete M.S., and Scalise G. Antimicrobial activity of polycationic peptides. Peptides 20 (1999) 1265-1273
30. Ganz T., and Lehrer R.I. Antibiotic peptides from higher eukaryotes: biology and applications. Mol. Med. Today 5 (1999) 292-297
31. Travis S.M., Anderson N.N., Forsyth W.R., Espiritu C., Conway B.D., Greenberg E.P., McCray Jr. P.B., Lehrer R.I., Welsh M.J., and Tack B.F. Bactericidal activity of mammalian cathelicidin-derived peptides. Infect. Immun. 68 (2000) 2748-2755
32. Apponyi M.A., Pukala T.L., Brinkworth C.S., Maselli V.M., Bowie J.H., Tyler M.J., Booker G.W., Wallace J.C., Carver J.A., Separovic F., Doyle J., and Llewellyn L.E. Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance. Peptides 25 (2004) 1035-1054
33. Andrä J., Gutsmann T., Garidel P., and Brandenburg K. Mechanisms of endotoxin neutralization by synthetic cationic compounds. J. Endotoxin Res. 12 (2006) 261-277
34. Rosenfeld Y., Papo N., and Shai Y. Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides. Peptide properties and plausible modes of action. J. Biol. Chem. 281 (2006) 1636-1643
35. Morrison D.C. Antibiotic-mediated endotoxin release - contribution to pathogenesis in Gram-negative sepsis. J. Endotoxin Res. 3 (1996) 173-279
36. Brandenburg K., Moriyon I., Arraiza M.D., Lehwark-Yvetot G., Koch M.H.J., and Seydel U. Biophysical investigations into the interaction of lipopolysaccharide with polymyxins. Thermochim. Acta 382 (2002) 189-198
37. Howe J., Andrä J., Conde R., Iriarte M., Garidel P., Koch M.H., Gutsmann T., Moriyon I., and Brandenburg K. Thermodynamic analysis of the lipopolysaccharide-dependent resistance of gram-negative bacteria against polymyxin B. Biophys. J. 92 (2007) 2796-2805
38. II structures of lipid A from Salmonella enterica serovar Minnesota by X-ray diffraction and freeze-fracture electron microscopy. Chem. Phys. Lipids 91 (1998) 53-69
39. Ding L., Yang L., Weiss T.M., Waring A.J., Lehrer R.I., and Huang H.W. Interaction of antimicrobial peptides with lipopolysaccharides. Biochemistry 42 (2003) 12251-12259
40. Ambroggio E.E., Separovic F., Bowie J., and Fidelio G.D. Surface behaviour and peptide-lipid interactions of the antibiotic peptides, Maculatin and Citropin. Biochim. Biophys. Acta 1664 (2004) 31-37
41. Rana F., and Blazyk J. Outer membrane structure in smooth and rough strains of Salmonella typhimurium and their susceptibility to the antimicrobial peptides, magainins and defensins. Prog. Clin. Biol. Res. 292 (1989) 77-85
42. Giacometti A., Cirioni O., Ghiselli R., Orlando F., Kamysz W., Rocchi M., D'Amato G., Mocchegiani F., Silvestri C., Lukasiak J., Saba V., and Scalise G. Effects of pexiganan alone and combined with betalactams in experimental endotoxic shock. Peptides 26 (2005) 207-216