Istituto di Biofisica     
Massi C., Indino E., Lami C., Fissi A., Pieroni O., La Rosa C., Esposito F., Galoppini C., Rovero P., Bandecchi P., Bendinelli M., Garzelli C. The Antiviral Activity of a Synthetic Peptide Derived from the Envelope SU Glycoprotein of Feline Immunodeficiency Virus Maps in Correspondence of an Amphipathic Helical Segment. In: Biochemical and Biophysical Research Communications, vol. 246 (1) pp. 160 - 165. Elsevier, 1998.
In a previous paper (Lombardiet al., Virology220, 274-284, 1996), we reported that a 20-amino acid synthetic peptide derived from a conserved region of the SU glycoprotein of feline immunodeficiency virus (FIV), i.e.,225EGPTLGNWAREIWATLFKKA244, bound the surface of FIV-permissive cells and inhibited FIV infection of CrFK and lymphoid cells. In this paper, we report, by the use of N- and C-terminus deleted synthetic analogs and by glycine scanning experiments that the minimal sequence needed for the full antiviral activity of the peptide maps in correspondence of amino acids229LGNWAREIWATL240and that either tryptophans residues at sequence position 232 or 237 are essential for such activity. Circular dichroism (CD) studies indicate that in the presence of a hydrophobic environment the225E-A244peptide adopts a structure containing an amphipathic α-helical segment of approximately 7 residues, corresponding to 2 helical turns, likely in correspondence of the sequence231(N)WAREIW(A)238. Such a helical segment of FIV SU glycoprotein may play a role in viral envelope fusion role with the host cell membrane, thus proving critical for cell infection.
DOI: 10.1006/bbrc.1998.8580

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