Contribution of the hydrophobicity gradient to the secondary structure and activity of fusogenic peptides

References

• Begona Ruiz-Arguello, M., Goni, F. M., Pereira, F. B. and Nieva, J. L., 1998, Phosphatidylinositol-dependent membrane fusion induced by a putative fusogenic sequence of Ebola virus. Journal of Virology, 72, 1775- 1781.
   Google Scholar
• Bosch, M. L., Earl, P. L., Fargnoli, K., Picciafuoco, S., Giombini, F., Wong-Staal, F. and Franchini, G., 1989, Identification of the fusion peptide of primate immunodeficiency viruses. Science, 244, 694 - 697.
   PubMed Web of Science ®Google Scholar
• Brasseur, R., 1991, Differentiation of lipid-associating helices by use of three-dimensional molecular hydrophobicity potential calculations. Journal of Biological Chemistry, 266, 16120- 16127.
   PubMed Web of Science ®Google Scholar
• Brasseur, R., Vandenbranden, M., Cornet, B. and Ruysschaert, J. M., 1990a, Orientation into the lipid bilayer of an asymmetric amphipathic helical peptide at the N-terminus of viral fusion protein. Biochimica et Biophysica Acta, 1029, 267 - 273.
   PubMed Web of Science ®Google Scholar
• Brasseur, R., De Meutter, J., Vanloo, B., Goormaghtigh, E., Ruysschaert, J.-M., Baert, J. and Rosseneu, M., 1990b, Mode of assembly of amphipathic helical segments in model high- density lipoproteins. Biochimica et Biophysica Acta, 1043, 245 - 252.
   PubMed Web of Science ®Google Scholar
• Brasseur, R., Vanloo, B., Deleys, R., Lins, L., Labeur, C., Taveirne, J., Ruysschaert, J.-M. and Rosseneu, M., 1993, Synthetic model peptides for apolipoproteins. I. Design and properties of synthetic model peptides for the amphipathic helices of the plasma apolipoproteins. Biochimica et Biophysica Acta, 1170, 1 - 7.
   Google Scholar
• Brasseur, R., Pillot, T., Lins, L., Vandekerckhove, J. and Rosseneu, M., 1997, Peptides in membranes: tipping the balance of membrane stability. Trends in Biochemical Sciences, 22, 167 - 171.
   PubMed Web of Science ®Google Scholar
• Brunner, J. and Tsurudome, M., 1993, Fusion-protein membranes interactions as studied by hydrophobic photolabeling. In Viral Fusion Mechanisms, J. Bentz, ed. (Boca Raton, Ann Arbor, London & Tokyo: CRC Press), pp. 67 - 88.
   Google Scholar
• Chakrabartty, A. and Baldwin, R. L., 1995, Stability of a-helices. Advances in Protein Chemistry, 46, 141 - 176.
   PubMedGoogle Scholar
• Colotto, A., Martin, I., Ruysschaert, J. M., Sen, A., Hui, S. W. and Epand, R. M., 1996, Structural study of the interaction between the SIV fusion peptide and model membranes. Biochemistry, 35, 980 - 989.
   PubMed Web of Science ®Google Scholar
• Eisenberg, D., Weiss, R. M. and Terwilliger, T. C., 1984, The hydrophobic moment detects periodicity in protein hydrophobicity. Proceedings of the National Academy of Sciences, USA, 81, 140 - 144.
   PubMed Web of Science ®Google Scholar
• Epand, R. M. and Epand, R. F., 1994, Relationship between the infectivity of influenza virus and the ability of its fusion peptide to perturb bilayers. Biochemical and Biophysical Research Communications, 202, 1420- 1425.
   PubMed Web of Science ®Google Scholar
• Epand, R. F., Martin, I., Ruysschaert, J. M. and Epand, R. M., 1994, Membrane orientation of the SIV fusion peptide determines its effect on bilayer stability and ability to promote membrane fusion. Biochemical and Biophysical Research Communications, 205, 1938 - 1943.
   PubMed Web of Science ®Google Scholar
• Gallaher, W. R., 1987, Detection of a fusion peptide sequence in the transmembrane protein of the human immunodeficiency virus. Cell, 50, 327 - 328.
   PubMed Web of Science ®Google Scholar
• Gallaher, W. R., Segrest, J. P. and Hunter E., 1992, Are fusion peptides really `sided’ insertional helices? Cell, 70, 531 - 532.
   PubMed Web of Science ®Google Scholar
• Gething, M. J., Doms, R. W., York, D. and White, J., 1986, Studies on the mechanism of membrane fusion: site-specific mutagenesis of hemagglutinin of influenza virus. Journal of Cell Biology, 102, 11 - 23.
   PubMed Web of Science ®Google Scholar
• Goormaghtigh, E., Cabiaux, V. and Ruysschaert J.-M., 1990, Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier Transform infrared spectroscopy on hydrated film. European Journal of Biochemistry, 193, 409 - 420.
   PubMedGoogle Scholar
• Gray, C., Tatulian, S. A., Wharton, S. A. and Tam, L. K., 1996, Effect of the N-terminal glycine on the secondary structure, orientation and interaction of the influenza hemagglutinin fusion peptide with lipid bilayers. Biophysical Journal, 70, 2275- 2286.
   PubMed Web of Science ®Google Scholar
• Horth, M., Lambrechts, B., Marinee, C., Bex, F., Thiriart, C., Ruysschaert, J.-M., Burny, A. and Brasseur, R., 1991, Theoretical and functional analysis of the SIV fusion peptide. EMBO Journal, 10, 2747- 2755.
   PubMed Web of Science ®Google Scholar
• Jonas, A., 1992, Lipid-binding properties of apolipoproteins. In Structure and function of apolipoproteins, M. Rosseneu, ed. (Boca Raton: CRC Press), pp. 217 - 250.
   Google Scholar
• Lambert, G., Decout, A., Vanloo, B., Rouy, D., Duverger, N., Kalopissis, A., Vandekerckhove, J., Chambaz, J., Brasseur, R. and Rosseneu, M., 1998, The C-terminal helix of human apolipoprotein A-II promotes the fusion of unilamellar liposomes and displaces apolipoprotein A-I from high-density lipoproteins. European Journal of Biochemistry, 253, 328 - 338.
   PubMedGoogle Scholar
• Lear, J. D. and DeGrado, W. F., 1987, Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA-2. Journal of Biological Chemistry, 262, 6500- 6505.
   PubMed Web of Science ®Google Scholar
• L üneberg, J., Martin, I., Nussler, F., Ruysschaert, J.-M. and Herrmann, A., 1995, Structure and topology of the Influenza virus fusion peptide in lipid bilayers. Journal of Biological Chemistry, 27, 27606- 27614.
   Google Scholar
• Martin, I., Defrise-Quertain, F., Decroly, E., Vandenbranden, M., Brasseur, R. and Ruysschaert, J.-M., 1993, Orientation and structure of the NH2-terminal HIV-1 gp41 peptide in fused and aggregated liposomes. Biochimica et Biophysica Acta, 1145, 124 - 133.
   PubMed Web of Science ®Google Scholar
• Martin, I., Dubois, M.-C., Defrise-Quertain, F., Saermark, T., Burny, A., Brasseur, R. and Ruysschaert, J.-M., 1994, Correlation between fusogenicity of synthetic modified peptides corresponding to the NH2-terminal extermity of Simian Immunodeficiency virus gp 32 and their mode of insertion into the lipid bilayer: an infrared spectroscopy study. Journal of Virology, 68, 1139- 1148.
   PubMed Web of Science ®Google Scholar
• Martin, I., Schaal, H., Scheid, A. and Ruysschaert, J.-M., 1996, Lipid membrane fusion induced by the human immunodeficiency virus type gp 41 N-terminal extremity is determined by its orientation in the lipid bilayer. Journal of Virology, 70, 298 - 304.
   PubMed Web of Science ®Google Scholar
• Muga, A., Neugebauer, W., Hirama, T. and Surewicz, W. K., 1994, Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion. Biochemistry, 33, 4444- 4448.
   PubMed Web of Science ®Google Scholar
• Nieva, J. L., Nir, S., Muga, A., Goni, F. M. and Wilschut, J., 1994, Interaction of the HIV-1 fusion peptide with phospholipid vesicles: different structural requirements for fusion and leakage. Biochemistry, 33, 3201- 3209.
   PubMed Web of Science ®Google Scholar
• Pécheur, E. I., Sainte-Marie, J., Bienvenue, A. and Hoekstra, D., 1999, Lipid headgroup spacing and peptide penetration but not peptide oligomerization, modulate peptide-induced fusion. Bio- chemistry, 38, 364 - 373.
   Google Scholar
• Pereira, F. B., Goni, F. M. and Nieva, J. L., 1995, Liposome destabilization induced by the HIV-1 fusion peptide effect of a single amino acid substitution. FEBS Letters, 362, 243 - 246.
   PubMed Web of Science ®Google Scholar
• Pereira, F. B., Goni, F. M., Muga, A., and Nieva, J. L., 1997, Permeabilization and fusion of uncharged lipid vesicles induced by the HIV-1 fusion peptide adopting an extended conformation: dose and sequence effects. Biophysical Journal, 73, 1977 - 1986.
   PubMed Web of Science ®Google Scholar
• Pérez-Méndez, O., Vanloo, B., Decout, A., Goethals, M., Peelman, F., Vandekerckhove, J., Brasseur, R. and Rosseneu, M., 1998, Contribution of the hydrophobicity gradient of an amphipathic peptide to its mode of association with lipids. European Journal of Biochemistry, 256, 570 - 579.
   PubMedGoogle Scholar
• Pillot, T., Goethals, M., Vanloo, B., Talussot, C., Brasseur, R., Vandekerckhove, J., Rosseneu, M. and Lins, L., 1996, Fusogenic properties of the C-terminal domain of the Alzheimer b-amyloid peptide. Journal of Biological Chemistry, 271, 28757- 28765.
   PubMed Web of Science ®Google Scholar
• Pillot, T., Lins, L., Goethals, M., Vanloo, B., Vandekerckhove, J., Baert, J., Rosseneu, M. and Brasseur, R., 1997, The 118-1135 peptide of the human prion protein promotes the fusion of unilamellar liposomes together with amyloid fibril formation. Journal of Molecular Biology, 274, 381 - 393.
   PubMedGoogle Scholar
• Rafalski, M., Lear, J. D. and DeGrado, W. F., 1990, Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp-41. Biochemistry, 29, 7917- 7922.
   PubMed Web of Science ®Google Scholar
• Rapaport, D. and Shai, Y., 1994, Interaction of fluorescently labeled analogues of the amino-terminal fusion peptide of Sendai Virus with phospholipid membranes. Journal of Biological Chemistry, 269, 15124- 15131.
   PubMed Web of Science ®Google Scholar
• Rodriguez-Crespo, I., Gomez-Gutierrez, J., Nieto, M., Peterson, D. L. and Gavilanes, F., 1994, Prediction of a putative fusion peptide in the S protein of hepatitis B virus. Journal of General Virology, 75, 637 - 639.
   Google Scholar
• Rodriguez-Crespo, I., Nunez, E., Gomez-Gutierrez, J., Yelamos, B., Albar, J. P., Peterson, D. L. and Gavilanes, F., 1995, Phospholipid interactions of the putative fusion peptide of hepatitis B surface antigen S protein. Journal of General Virology, 76, 301 - 308.
   Google Scholar
• Rodriguez-Crespo, I., Gomez-Gutierrez, J., Encinar, J. A., Gonzalez-Ros, J. M., Albar, J. P., Peterson, D. L. and Gavilanes, F., 1996, Structural properties of the putative fusion peptide of hepatitis B virus upon interaction with phospholipids. European Journal of Biochemistry, 242, 243 - 248.
   Google Scholar
• Stegmann, T., Delfino, J. M., Richards, F. M. and Helenius, A., 1991, The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion. Journal of Biological Chemistry, 266, 187 - 211.
   Google Scholar
• Tatulian, S. A., Hinterdorfer, P., Baker, G. and Tamm, L. K., 1995, Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy. EMBO Journal, 14, 5514- 5523.
   PubMed Web of Science ®Google Scholar
• Vonéche, V., Portetelle, D., Kettmann, R., Willems, L., Limbach, K., Paoletti, E., Ruysschaert, J.-M., Burny, A. and Brasseur, R., 1992, 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. Proceedings of the National Academy of Sciences, USA, 89, 3810- 3814.
   PubMed Web of Science ®Google Scholar
• White, J. M., 1990, Viral and cellular membrane fusion proteins. Annual Review of Physiology, 52, 675 - 697.
   PubMed Web of Science ®Google Scholar
• White, J. M., 1992, Membrane fusion. Science, 258, 917 - 924.
   PubMed Web of Science ®Google Scholar
• Wimley, W. C. and White, S. H., 1996, Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nature Structural Biology, 3, 842 - 848.
   PubMedGoogle Scholar
• Zimmerberg, J., Vogel, S. S. and Chernomordik, L. V., 1993, Mechanism of membrane fusion. Annual Review of Biomolecular Structure, 22, 433 - 466.
   PubMedGoogle Scholar