In a previous paper (Lombardi et at., Virology 220, 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 (FTV), i.e., (225)EGPTLGNWAREIWATLFKRA(244), 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 acids (229)LGNWAREIWATL(240) and 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 the E-225-A(244) peptide adopts a structure containing an amphipathic alpha-helical segment of approximately 7 residues, corresponding to 2 helical turns, likely ire correspondence of the sequence (231)(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. (C) 1998 Academic Press.
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
BANDECCHI, PATRIZIA;GARZELLI, CARLO
1998-01-01
Abstract
In a previous paper (Lombardi et at., Virology 220, 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 (FTV), i.e., (225)EGPTLGNWAREIWATLFKRA(244), 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 acids (229)LGNWAREIWATL(240) and 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 the E-225-A(244) peptide adopts a structure containing an amphipathic alpha-helical segment of approximately 7 residues, corresponding to 2 helical turns, likely ire correspondence of the sequence (231)(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. (C) 1998 Academic Press.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
