Feline immunodeficiency virus (FIV) is a pathogen that causes an AIDS-like syndrome in domestic cats and is extensively used as a model system by which criteria for anti-lentiviral vaccines and drugs development can be tested. Despite little homology sequence, the surface and TM gp of FIV and HIV-1 exhibit a common structural framework and appear to play similar roles in Initiation of cell infection mediating the final event of membrane fusion and virus entry. Recently a 20-mer synthetic peptide spanning amino acids 767L-G786 of the membrane-proximal ectodomain of FIV (TM) gp - gp41(767-786)- was found to be endowed with potent antiviral activity. Testing deleted or substituted peptides, the 8-mer gp41(770-777), designated C8, including in the sequence three Trp residues was identified as the minimal sequence needed for full antiviral activity. NMR conformational analysis of gp41(770-777) evidenced the presence of a b-turn conformation centered on the residues 773-776. Here we report the conformational analysis of the 20-mer TM-767-786 by means of NMR spectroscopy. A comparison between structural properties of gp41(767-786) and of gp41(770-777) was carried out in order to define the role played by the sequence length and by the Trp side chains on the active fragments stability.
STRUCTURAL FEATURES OF PEPTIDES DERIVED FROM FELINE IMMUNODEFICIENCY VIRUS TM-GLYCOPROTEIN
RODRIQUEZ, Manuela;RANDINO, ROSARIO;GRIMALDI, MANUELA;PALISI, ANGELICA;D'URSI, Anna Maria
2014-01-01
Abstract
Feline immunodeficiency virus (FIV) is a pathogen that causes an AIDS-like syndrome in domestic cats and is extensively used as a model system by which criteria for anti-lentiviral vaccines and drugs development can be tested. Despite little homology sequence, the surface and TM gp of FIV and HIV-1 exhibit a common structural framework and appear to play similar roles in Initiation of cell infection mediating the final event of membrane fusion and virus entry. Recently a 20-mer synthetic peptide spanning amino acids 767L-G786 of the membrane-proximal ectodomain of FIV (TM) gp - gp41(767-786)- was found to be endowed with potent antiviral activity. Testing deleted or substituted peptides, the 8-mer gp41(770-777), designated C8, including in the sequence three Trp residues was identified as the minimal sequence needed for full antiviral activity. NMR conformational analysis of gp41(770-777) evidenced the presence of a b-turn conformation centered on the residues 773-776. Here we report the conformational analysis of the 20-mer TM-767-786 by means of NMR spectroscopy. A comparison between structural properties of gp41(767-786) and of gp41(770-777) was carried out in order to define the role played by the sequence length and by the Trp side chains on the active fragments stability.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
