scholarly journals Antiviral Activity and Conformational Features of an Octapeptide Derived from the Membrane-Proximal Ectodomain of the Feline Immunodeficiency Virus Transmembrane Glycoprotein

2003 ◽  
Vol 77 (6) ◽  
pp. 3724-3733 ◽  
Author(s):  
Simone Giannecchini ◽  
Armida Di Fenza ◽  
Anna Maria D'Ursi ◽  
Donatella Matteucci ◽  
Paolo Rovero ◽  
...  
Keyword(s):  
Antiviral Activity ◽  
Feline Immunodeficiency Virus ◽  
Control Strategies ◽  
Present Report ◽  
Lymphoid Cells ◽  
Structural Studies ◽  
Terminal Portion ◽  
Short Segment ◽  
Transmembrane Glycoprotein ◽  
Immunodeficiency Virus

ABSTRACT Feline immunodeficiency virus (FIV) provides a valuable animal model by which criteria for lentivirus control strategies can be tested. Previous studies have shown that a 20-mer synthetic peptide of the membrane-proximal ectodomain of FIV transmembrane glycoprotein, designated peptide 59, potently inhibited the growth of tissue culture-adapted FIV in feline fibroblastoid CrFK cells. In the present report we describe the potential of this peptide to inhibit the replication of primary FIV isolates in lymphoid cells. Because antiviral activity of peptide 59 was found to map to a short segment containing three conserved Trp residues, further analyses focused on a derivative of eight amino acids (770W-I777), designated C8. Peptide C8 activity was found to be dependent on conservation of the Trp motif, to be removed from solution by FIV absorbed onto substrate cells, and to be blocked by a peptide derived from the N-terminal portion of FIV transmembrane glycoprotein. Structural studies showed that peptide C8 possesses a conformational propensity highly uncommon for peptides of its size, which may account for its considerable antiviral potency in spite of small size.

scholarly journals Dissection of seroreactivity against the tryptophan-rich motif of the feline immunodeficiency virus transmembrane glycoprotein

Virology ◽  
2004 ◽  
Vol 322 (2) ◽  
pp. 360-369 ◽  
Author(s):  
Giulia Freer ◽  
Simone Giannecchini ◽  
Alain Tissot ◽  
Martin F Bachmann ◽  
Paolo Rovero ◽  
...  
Keyword(s):  
Feline Immunodeficiency Virus ◽  
Transmembrane Glycoprotein ◽  
Immunodeficiency Virus

scholarly journals Role of Env in Resistance of Feline Immunodeficiency Virus (FIV)-Infected Cats to Superinfection by a Second FIV Strain as Determined by Using a Chimeric Virus

2007 ◽  
Vol 81 (19) ◽  
pp. 10474-10485 ◽  
Author(s):  
Simone Giannecchini ◽  
Mauro Pistello ◽  
Patrizia Isola ◽  
Donatella Matteucci ◽  
Paola Mazzetti ◽  
...  
Keyword(s):  
Feline Immunodeficiency Virus ◽  
Neutralizing Antibodies ◽  
Viral Envelope ◽  
Lymphoid Cells ◽  
Time Interval ◽  
Complete Protection ◽  
Challenge Virus ◽  
Immunodeficiency Virus

ABSTRACT A more or less pronounced resistance to superinfection by a second strain of the infecting virus has been observed in many lentivirus-infected hosts. We used a chimeric feline immunodeficiency virus (FIV), designated FIVχ, containing a large part of the env gene of a clade B virus (strain M2) and all the rest of the genome of a clade A virus (a p34TF10 molecular clone of the Petaluma strain modified to grow in lymphoid cells), to gain insights into such resistance. FIVχ was infectious and moderately pathogenic for cats and in vitro exhibited the neutralization specificity of the env donor. The experiments performed were bidirectional, in that cats preinfected with either parental virus were challenged with FIVχ and vice versa. The preinfected animals were partially or completely protected relative to what was observed in naïve control animals, most likely due, at least in part, to the circumstance that in all the preinfecting/challenge virus combinations examined, the first and the second virus shared significant viral components. Based on the proportions of complete protection observed, the role of a strongly matched viral envelope appeared to be modest and possibly dependent on the time interval between the first and the second infection. Furthermore, complete protection and the presence of measurable neutralizing antibodies capable of blocking the second virus in vitro were not associated.

Development of Antiviral Fusion Inhibitors: Short Modified Peptides Derived from the Transmembrane Glycoprotein of Feline Immunodeficiency Virus

ChemBioChem ◽  
2006 ◽  
Vol 7 (5) ◽  
pp. 774-779 ◽  
Author(s):  
Anna Maria D'Ursi ◽  
Simone Giannecchini ◽  
Cinzia Esposito ◽  
Maria Claudia Alcaro ◽  
Olimpia Sichi ◽  
...  
Keyword(s):  
Feline Immunodeficiency Virus ◽  
Fusion Inhibitors ◽  
Transmembrane Glycoprotein ◽  
Immunodeficiency Virus ◽  
Modified Peptides

scholarly journals C-Terminal gp40 Peptide Analogs Inhibit Feline Immunodeficiency Virus: Cell Fusion and Virus Spread

2002 ◽  
Vol 76 (18) ◽  
pp. 9079-9086 ◽  
Author(s):  
R. J. Medinas ◽  
D. M. Lambert ◽  
W. A. Tompkins
Keyword(s):  
Cell Fusion ◽  
Feline Immunodeficiency Virus ◽  
Synthetic Peptides ◽  
Acute Infection ◽  
Surface Glycoprotein ◽  
Heptad Repeat ◽  
Transmembrane Glycoprotein ◽  
Immunodeficiency Virus ◽  
Hiv 1

ABSTRACT The envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1), gp160, is synthesized as a protein precursor that when proteolytically cleaved yields two subunits, gp120 and gp41. gp120 is the surface glycoprotein on HIV-1 responsible for binding to CD4, and gp41 is the transmembrane glycoprotein involved in the membrane fusion process. gp41 is divided into the N-terminal fusion peptide, the heptad repeat 1 (HR1) and HR2 regions, and the C-terminal transmembrane region, which are collectively responsible for virus fusion and entry into the cell. Synthetic peptides derived from the HR2 and HR1 regions of HIV-1LAI have been shown to prevent virus-cell fusion and infection in vitro. In phase II clinical trials in HIV patients, data revealed that T20 has antiviral efficacy and is well tolerated. Similar results were obtained in vitro with HIV-2 and simian immunodeficiency virus, supporting the conservation of the gp41 ectodomain among lentiviruses. Feline immunodeficiency virus (FIV) infection in the cat has been used as a model to develop potential antivirals for HIV. To determine if synthetic gp40 analogs capable of inhibiting FIV infection could be identified, 15 overlapping 35-amino-acid peptides derived from the C-terminal HR2 domain of FIV gp40 were synthesized. These peptides were tested for efficacy against FIV in a syncytium-forming assay with FIV-infected CrFK cells and HeLa cells expressing the FIV receptor CXCR4. Several peptides exhibited activity at the nanogram level. Antiviral activity was confirmed by suppression of reverse transcriptase in a FIV feline CD4+-T-cell (FCD4-E) acute-infection assay. These data demonstrate that synthetic peptides derived from the HR2 domain of the FIV gp41 protein are effective inhibitors of FIV infection.

scholarly journals The membrane-proximal tryptophan-rich region in the transmembrane glycoprotein ectodomain of feline immunodeficiency virus is important for cell entry

Virology ◽  
2004 ◽  
Vol 320 (1) ◽  
pp. 156-166 ◽  
Author(s):  
Simone Giannecchini ◽  
Francesca Bonci ◽  
Mauro Pistello ◽  
Donatella Matteucci ◽  
Olimpia Sichi ◽  
...  
Keyword(s):  
Feline Immunodeficiency Virus ◽  
Cell Entry ◽  
Rich Region ◽  
Transmembrane Glycoprotein ◽  
Immunodeficiency Virus
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