Conolysin-Mt: A Conus peptide that disrupts cellular membranes

Biochemistry

Volumn 46, Issue 44, 2007, Pages 12586-12593

  Biggs, Jason S ^a   Rosenfeld, Yosef ^b   Shai, Yechiel ^b   Olivera, B M ^a  

^a UNIVERSITY OF UTAH   (United States)

^b WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CONSTANTS; CONOPEPTIDE; HEMOLYTIC ACTIVITY; ION CHANNELS; MODEL MEMBRANES;

CELL MEMBRANES; CHOLESTEROL; ESCHERICHIA COLI;

PEPTIDES;

CONOLYSIN MT; ION CHANNEL; PEPTIDE; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLGLYCEROL; UNCLASSIFIED DRUG; VENOM;

ADOLESCENT; ANTIMICROBIAL ACTIVITY; ARTICLE; BINDING AFFINITY; CELL MEMBRANE; CONCENTRATION (PARAMETERS); CONUS MUSTELINUS; CONUS SNAIL; CYTOLYSIS; ERYTHROCYTE; ESCHERICHIA COLI; HEMOLYSIS; HUMAN; HUMAN CELL; MEMBRANE PERMEABILITY; MINIMUM INHIBITORY CONCENTRATION; MOUSE; NONHUMAN; PRIORITY JOURNAL; STAPHYLOCOCCUS AUREUS;

AMINO ACID SEQUENCE; ANIMALS; CELL MEMBRANE; CONOTOXINS; CONUS SNAIL; CYTOTOXINS; DRUG EVALUATION; EUKARYOTIC CELLS; HUMANS; MELITTEN; MICE; MOLECULAR SEQUENCE DATA; PEPTIDES; PROKARYOTIC CELLS; SEQUENCE HOMOLOGY, AMINO ACID;

CONUS MUSTELINUS; ESCHERICHIA COLI; EUKARYOTA; POSIBACTERIA; PROKARYOTA; STAPHYLOCOCCUS AUREUS;

EID: 35848966578     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700775p     Document Type: Article

References (33)

1. Alouf, J. E. (2001) Pore-forming bacterial protein toxins: An overview, Curr. Top. Microbiol. Immunol. 257, 1-14.
2. Habermann, E. (1972) Bee and wasp venoms, Science 177, 314-322.
3. 1H-NMR studies of monomelic melittin in aqueous solution, Biochim. Biophys. Acta 622, 219-230.
4. Talbot, J. C., Dufourcq, J., de Bony, J., Faucon, J. F., and Lussan, C. (1979) Conformational change and self association of monomeric melittin, FEBS Lett. 102, 191-193.
5. Tatham, A. S., Hider, R. C., and Drake, A. F. (1983) The effect of counterions on melittin aggregation, Biochem. J. 211, 683-686.
6. 1H-NMR studies of self-aggregation of melittin in aqueous solution, Biochim. Biophys. Acta 622, 231-244.
7. DeGrado, W. F., Musso, G. F., Lieber, M., Kaiser, E. T., and Kezdy, F. J. (1982) Kinetics and mechanism of hemolysis induced by melittin and by a synthetic melittin analogue, Biophys. J. 37, 329-338.
8. Juvvadi, P., Vunnam, S., and Merrifield, R. B. (1996) Synthetic melittin, its enantio, retro, and retroenantio isomers, and selected chimeric analogs: Their antibacterial, hemolytic, and lipid bilayer action, J. Am. Chem. Soc. 118, 8989-8997.
9. Perez-Paya, E., Houghten, R. A., and Blondelle, S. E. (1995) The role of amphipathicity in the folding, self-association and biological activity of multiple subunit small proteins, J. Biol. Chem. 270, 1048-1056.
10. Beschiaschvili, G., and Seelig, J. (1990) Melittin binding to mixed phosphatidylglycerol/phosphatidylcholine membranes, Biochemistry 29, 52-58.
11. Jacobsen, R. B., Koch, E. D., Lange-Malecki, B., Stocker, M., Verhey, J., Van Wagoner, R. M., Vyazovkina, A., Olivera, B. M., and Terlau, H. (2000) Single amino acid substitutions in kappa-conotoxin pviia disrupt interaction with the shaker k+ channel, J. Biol. Chem. 275, 24639-24644.
12. Horton, R. M., Manfredi, A. A., and Conti-Tronconi, B. M. (1993) The 'embryonic' gamma subunit of the nicotinic acetylcholine receptor is expressed in adult extraocular muscle, Neurology 43, 983-986.
13. Gazit, E., Lee, W. J., Brey, P. T., and Shai, Y. (1994) Mode of action of the antibacterial cecropin b2: A spectrofluorometric study, Biochemistry 33, 10681-10692.
14. Kliger, Y., Aharoni, A., Rapaport, D., Jones, P., Blumenthal, R., and Shai, Y. (1997) Fusion peptides derived from the hiv type 1 glycoprotein 41 associate within phospholipid membranes and inhibit cell-cell fusion. Structure-function study, J. Biol. Chem. 272, 13496-13505.
15. Allen, T. M., and Cleland, L. G. (1980) Serum-induced leakage of liposome contents, Biochim. Biophys. Acta 597, 418-426.
16. Oren, Z., and Shai, Y. (1996) A class of highly potent antibacterial peptides derived from pardaxin, a pore-forming peptide isolated from moses sole fish pardachirus marmoratus, Eur. J. Biochem. 237, 303-310.
17. Surewicz, W. K., Mantsch, H. H., and Chapman, D. (1993) Determination of protein secondary structure by fourier transform infrared spectroscopy: A critical assessment, Biochemistry 32, 389-394.
18. Clark, C., Olivera, B. M., and Cruz, L. J. (1981) A toxin from the venom of the marine snail conus geographus which acts on the vertebrate central nervous system, Toxicon 19, 691-699.
19. Olivera, B. M., McIntosh, J. M., Clark, C., Middlemas, D., Gray, W. R., and Cruz, L. J. (1985) A sleep-inducing peptide from conus geographus venom, Toxicon 23, 277-282.
20. Bessalle, R., Kapitkovsky, A., Gorea, A., Shalit, I., and Fridkin, M. (1990) All-d-magainin: Chirality, antimicrobial activity and proteolytic resistance, FEBS Lett. 274, 151-155.
21. Wade, D., Boman, A., Wahlin, B., Drain, C. M., Andreu, D., Boman, H. G., and Merrifield, R. B. (1990) All-d amino acid-containing channel-forming antibiotic peptides, Proc. Natl. Acad. Sci. U.S.A 87, 4761-4765.
22. Oren, Z., and Shai, Y. (1997) Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: Structure-function study, Biochemistry 36, 1826-1835.
23. Terlau, H., and Olivera, B. M. (2004) Conus venoms: A rich source of novel ion channel-targeted peptides, Physiol. Rev. 84, 41-68.
24. Olivera, B. M. (2002) Conus venom peptides: Reflections from the biology of clades and species, Annu. Rev. Ecol. Syst. 33, 25-47.
25. Olivera, B. M. (2006) Conus peptides: Biodiversity-based discovery and exogenomics, J. Biol. Chem. 281, 31173-31177.
26. Papo, N., and Shai, Y. (2003) New lytic peptides based on the d,l-amphipathic helix motif preferentially kill tumor cells compared to normal cells, Biochemistry 42, 9346-9354.
27. Merrifield, R. B., Juvvadi, P., Andreu, D., Ubach, J., Boman, A., and Boman, H. G. (1995) Retro and retrosenantio analogs of cecropin-melittin hybrids, Proc. Natl. Acad. Sci. U.S.A. 92, 3449-3453.
28. Park, S. C. Kim, J. Y., Shin, S. O., Jeong, C. Y., Kim, M. H., Shin, S. Y., Cheong, G. W., Park, Y., and Hahm, K. S. (2006) Investigation of toroidal pore and oligomerization by melittin using transmission electron microscopy, Biochem. Biophys. Res. Commun. 343, 222-228.
29. Smith, R., Separovic, F., Milne, T. J., Whittaker, A., Bennett, F. M., Cornell, B. A., and Makriyannis, A. (1994) Structure and orientation of the pore-forming peptide, melittin, in lipid bilayers, J. Mol. Biol. 241, 456-466.
30. Ladokhin, A. S., Selsted, M. E., and White, S. H. (1997) Sizing membrane pores in lipid vesicles by leakage of co-encapsulated markers: Pore formation by melittin, Biophys. J. 72, 1762-1766.
31. Papo, N., and Shai, Y. (2003) Exploring peptide membrane interaction using surface plasmon resonance: Differentiation between pore formation versus membrane disruption by lytic peptides, Biochemistry 42, 458-466.
32. Rex, S., and Schwarz, G. (1998) Quantitative studies on the melittin-induced leakage mechanism of lipid vesicles, Biochemistry 37, 2336-2345.
33. Ladokhin, A. S., and White, S. H. (2001) 'Detergent-like' permeabilization of anionic lipid vesicles by melittin, Biochim. Biophys. Acta 1514, 253-260.