Enhanced efficiency of a targeted fusogenic peptide

Biochimica et Biophysica Acta - Biomembranes

Volumn 1372, Issue 1, 1998, Pages 102-116

  Decout, A ^a   Labeur, C ^a   Goethals, M ^b   Brasseur, R ^c   Vandekerckhove, J ^b   Rosseneu, M ^a  

^a GHENT UNIVERSITY   (Belgium)

^b DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^c UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

Amyloid; Fusogenic peptide; Liposome; Phosphatidylinositol 4,5 bisphosphate; Targeting

Indexed keywords

AMYLOID BETA PROTEIN; CHIMERIC PROTEIN; HYBRID PROTEIN; LIPOSOME; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE;

ARTICLE; CIRCULAR DICHROISM; CYTOTOXICITY; MEMBRANE FUSION; MEMBRANE STABILIZATION; MEMBRANE VESICLE; PRIORITY JOURNAL;

DOSE-RESPONSE RELATIONSHIP, DRUG; LIPOSOMES; MEMBRANE FUSION; PEPTIDE FRAGMENTS; PHOSPHATIDYLCHOLINES; PHOSPHATIDYLETHANOLAMINES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT FUSION PROTEINS;

EID: 0032562960     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(98)00050-9     Document Type: Article

References (46)

1. Horth M., Lambrecht B., Khim M.C.L., Bex F., Thiriard C., Ruysschaert J.M., Burny A., Brasseur R. Theoretical and functional analysis of the SIV fusion peptide. EMBO J. 10:1991;2747-2755.
2. Blobel C.P., Wolfsberg T.G., Turck C.W., Myles D.G., Primakoff P., White J.M. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature. 356:1992;248-252.
3. Vonèche V., Portetelle D., Kettman R., Willems L., Limbach K., Paoletti E., Ruysschaert J.M., Burny A., Brasseur R. Fusogenic segments of bovine leukemia virus and simian immunodeficiency virus are interchangeable and mediate fusion by means of oblique insertion in the lipid bilayer of their target cells. Proc. Natl. Acad. Sci. U.S.A. 89:1992;3810-3814.
4. White J.M. Membrane fusion. Science. 258:1992;917-924.
5. Zimmerberg J., Vogel S.S., Chernomordik L.V. Mechanism of membrane fusion. Annu. Rev. Biophys. Biomol. Struct. 22:1993;433-466.
6. S. Ohnishi, in: N. Düzgünes, F. Bronner (Eds.), Membrane Fusion in Fertilization, Cellular Transport and Viral Infection, Academic Press, New York, 1988, pp. 257-296.
7. Brasseur R., Vandenbranden M., Cornet B., Ruysschaert J.M. Orientation into the lipid bilayer of an asymmetric amphipathic helical peptide at the N-terminus of viral fusion protein. Biochim. Biophys. Acta. 1029:1990;267-273.
8. Brasseur R., Pillot T., Lins L., Vandekerckhove J., Rosseneu M. Peptide in membranes: tipping the balance of membrane stability. Trends Biochem. Sci. 22:1997;167-171.
9. 2-terminal extremity of simian immunodeficiency virus gp32 and their mode of insertion into the lipid bilayer: an infrared spectroscopy study. Virology. 68:1994;1139-1148.
10. Pillot T., Goethals M., Vanloo B., Talussot C., Brasseur R., Vandekerckhove J., Rosseneu M., Lins L. Fusogenic properties of the C-terminal domain of the Alzeimer β-amyloid peptide. J. Biol. Chem. 271:1996;28757-28765.
11. Pillot T., Lins L., Goethals M., Vanloo B., Vandekerckhove J., Baert J., Rosseneu M., Brasseur R. The 118-135 peptide of the human prion protein promotes the fusion of unilamellar liposomes together with amyloid fibril formation. J. Mol. Biol. 274:1997;381-393.
12. Epand R.M., Martin I., Ruysschaert J.M., Epand R.M. Membrane orientation of the SIV fusion peptide determines its effect on bilayer stability and ability to promote membrane fusion. Biochem. Biophys. Res. Commun. 205:1994;1938-1943.
13. Tatulian S.A., Hinterdorfer P., Baber G., Tamm L.K. Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy. EMBO J. 14:1995;5514-5523.
14. Martin I., Schaal H., Scheid A., Ruysschaert J.M. Lipid membrane fusion induced by the human immunodeficiency virus type 1gp41 N-terminal extremity is determined by its orientation in the lipid bilayer. J. Virol. 70:1996;298-304.
15. Selkoe D.J. Amyloid β-protein: new clues to the genesis of Alzheimer's disease. Curr. Opin. Neurobiol. 4:1994;708-716.
16. Arispe N., Pollarde H.B., Rojas E. Alzheimer disease amyloid β-protein forms calcium channels in bilayer membranes: blockage by tromethanine and aluminium. Proc. Natl. Acad. Sci. U.S.A. 90:1993;567-571.
17. Arispe N., Pollarde H.B., Rojas E. Giant multilevel cation channels formed by Alzheimer disease amyloid β-protein. Proc. Natl. Acad. Sci. U.S.A. 90:1993;10573-10577.
18. Terzi E., Hölzemann G., Seelig J. Self-association of β-amyloid peptide (1-40) in solution and binding to lipid membranes. J. Mol. Biol. 252:1995;633-642.
19. Lassing I., Lindberg U. Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin. Nature. 314:1985;472-474.
20. 2 and inhibits its hydrolysis by phospholipase C. Science. 247:1990;1575-1578.
21. MacLaurin J., Chakrabartty A. Membrane disruption by Alzheimer β-amyloid peptides mediated through specific binding to either phospholipids or gangliosides. J. Biol. Chem. 271(43):1996;26482-26489.
22. MacLaurin J., Chakrabartty A. Characterization of the interactions of Alzheimer β-amyloid peptides with phospholipid membranes. Eur. J. Biochem. 245:1997;355-363.
23. Gettemans J., De Ville Y., Waelkens E., Vandekerckhove J. The actin-binding properties of the Physarum actin-fragmin complex. J. Biol. Chem. 270:1995;2644-2651.
24. T'Jampens D., Meerschaert K., Constantin B., Bailey J., Cook L.J., Corte V., De Mol H., Goethals M., Van Damme J., Vandekerckhove J., Gettemans J. Molecular cloning, overexpression, developmental regulation and immunolocalization of fragmin P, a gelsonin-related actin-binding protein from Physarum polycephalum plasmodia. J. Cell Sci. 110:1997;1215-1226.
25. Yu F.X., Sun H.Q., Janmey P.A., Yin H.L. gCap 39, a calcium ion- and polyphosphoinositide regulated actin capping protein. J. Biol. Chem. 267:1990;14616-14621.
26. Janmey P.A., Lamb J., Allen P.G., Matsudaira P.T. Phosphoinositide-binding peptides derived from the sequences of gelsonin and villin. J. Biol. Chem. 267:1992;11818-11823.
27. Janmey P.A., Stossel T.P. Modulation of gelsonin function by phosphatidylinositol 4,5-bisphosphate. Nature. 325:1987;362-364.
28. Derossi D., Calvet S., Trembleau A., Brunissen A., Chassaing G., Prochiantz A. Cell internalisation of the third helix of the Antennapedia homeodomain is receptor-independent. J. Biol. Chem. 271:1996;18188-18193.
29. Brasseur R., De Meutter J., Vanloo B., Goormaghtigh E., Ruysschaert J.M., Rosseneu M. Mode of assembly of amphiphatic helical segments in model high-density lipoproteins. Biochim. Biophys. Acta. 1043:1990;245-252.
30. Johnson W.C. Jr. Protein secondary structure and circular dichroism: a practical guide. Proteins Struct. Funct. Genet. 7:1990;205-214.
31. Janmey P.A., Stossel T.P. Gelsonin-polyphosphoinositide interaction. Full expression of gelsolin-inhibiting function by polyphosphoinositides in vesicular form and inactivation by dilution, aggregation or masking of the inositol head group. J. Biol. Chem. 264:1989;4825-4831.
32. Kendall D.A., MacDonald R.C. Characterization of a fluorescence assay to monitor changes in the aqueous volume of lipid vesicles. Anal. Biochem. 134:1983;26-33.
33. Defrise-Quertain F., Cabiaux V., Vandenbranden M., Wattiez R., Falmagne P., Ruysschaert J.M. pH-Dependent bilayer destabilisation and fusion of phospholipidic large unilamellar vesicles induced by diphtheria toxin and its fragments A and B. Biochemistry. 28:1989;3406-3413.
34. Eisenberg S., Weiss R.M., Terwilliger T.C. The helical hydrophobic moment: a measure of the amphiphilicity of a helix. Nature. 299:1982;371-374.
35. S.J. Morris, D. Bradley, C.C. Gibson, P.D. Smith, R. Blumenthal, Use of membrane associated fluorescence probes to monitor fusion of bilayer vesicles: application to rapid kinetics using pyrene excimer/monomer fluorescence, in: L.M. Loem (Ed.), Spectroscopic Membrane Probes, Vol. 1, CRC press, Boca Raton, FL, 1988, pp. 161-191.
36. Rapaport D., Shai Y. Interaction of fluorescently labeled analogues of the amino-terminal fusion peptide of Sendai Virus with phospholipid membranes. J. Biol. Chem. 269:1994;15124-15131.
37. P.R. Cullis, M.J. Hope, Physical properties and functional roles of lipids in membranes, in: D.E. Vance, J. Vance (Eds.), Biochemistry of Lipids, Lipoproteins and Membranes, Vol. 20, Elsevier, The Netherlands, 1991, pp. 1-41.
38. 31P -NMR study Biochim. Biophys. Acta. 877:1986;216-219.
39. 2 terminus of influenza HA-2. J. Biol. Chem. 262:1987;2500-2505.
40. Harter C., James P., Bachi T., Semenza G., Brunner J. Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the 'fusion peptide'. J. Biol. Chem. 264:1989;6454-6459.
41. Takahashi S. Conformation of membrane fusion-active 20-residue peptides with and without lipid bilayers. Implication of alpha-helix formation for membrane fusion. Biochemistry. 29:1990;6257-6264.
42. Rafalski M., Ortiz A., Rockwell A., van Ginkel L.C., Lear J.D., DeGrado W.F., Wilschut J. Membrane fusion activity of the influenza virus hemagglutinin: interaction of HA-2 N-terminal peptides with phospholipid vesicles. J. Biochemistry. 30:1991;10211-10220.
43. Epand R.F., Cheetham J., Epand R.F., Yeagle P.L., Richardson C.D., DeGrado W.F. Peptide models for the membrane destabilizing actions of viral fusion protein. Biopolymers. 32:1992;309-314.
44. Muga A., Neugebauer W., Hirama T., Surewicz W.K. Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion. Biochemistry. 33:1994;4444-4448.
45. Colotto A., Martin I., Ruysschaert J.M., Sen A., Hui S.W., Epand R.M. Structural study of the interaction between the SIV fusion peptide and model membranes. Biochemistry. 35:1996;980-989.
46. Niggli V., Andreoli C., Roy C., Mangeat P. Identification of a phosphatidylinositol-4,5-bisphosphate-binding domain in the N-terminal region of ezrin. Biochem. Biophys. 76:1995;172-176.