Lorin, Aurelien
Lins, Laurence
Stroobant, Vincent
[UCL]
Brasseur, Robert
Charloteaux, Benoit
We had previously predicted successfully the minimal fusion peptides (FPs) of the human immunodeficiency virus 1 (HIV-1) gp41 and the bovine leukemia virus (BLV) gp30 using an original approach based on the obliquity/fusogenicity relationship of tilted peptides. In this paper, we have used the same method to predict the shortest FP capable of inducing optimal fusion in vitro of the simian immunodeficiency virus (SRT) mac isolate and of other SIVs and human immunodeficiency virus (HIV-2) isolates. In each case, the 11-residue-long peptide was predicted as the minimal FP. For the SfV mac isolate, liposome lipid-mixing and leakage assays confirmed that this peptide is the shortest peptide inducing optimal fusion in vitro, being therefore the minimal FP. These results are another piece of evidence that the tilted properties of FPs are important for the fusion process and that our method can be used to predict the minimal FPs of other viruses. Copyright (c) 2007 European Peptide Society and John Wiley & Sons, Ltd.
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Bibliographic reference |
Lorin, Aurelien ; Lins, Laurence ; Stroobant, Vincent ; Brasseur, Robert ; Charloteaux, Benoit. The minimal fusion peptide of simian immunodeficiency virus corresponds to the 11 first residues of gp32.2nd Workshop on Biophysics of Membrane-Active Peptides (Lisbon(Portugal), 2007). In: Journal of Peptide Science, Vol. 14, no. 4, p. 423-428 (2008) |
Permanent URL |
http://hdl.handle.net/2078.1/59296 |