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The minimal fusion peptide of simian immunodeficiency virus corresponds to the 11 first residues of gp32

✍ Scribed by Aurélien Lorin; Laurence Lins; Vincent Stroobant; Robert Brasseur; Benoit Charloteaux


Book ID
105360766
Publisher
John Wiley and Sons
Year
2008
Tongue
English
Weight
258 KB
Volume
14
Category
Article
ISSN
1075-2617

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✦ Synopsis


Abstract

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 (SIV) 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 SIV 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 © 2007 European Peptide Society and John Wiley & Sons, Ltd.


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