Minimal Sequence Requirements for Synthetic Peptides Derived from the V3 Loop of the Human Immunodeficiency Virus Type 1 (HIV-1) to Enhance HIV-1 Binding to Cells and Infection
Identifieur interne : 004158 ( Main/Exploration ); précédent : 004157; suivant : 004159Minimal Sequence Requirements for Synthetic Peptides Derived from the V3 Loop of the Human Immunodeficiency Virus Type 1 (HIV-1) to Enhance HIV-1 Binding to Cells and Infection
Auteurs : Carlo Zanotto [Italie] ; Francesca Calderazzo [Italie] ; Monica Dettin [Italie] ; Carlo Di Bello [Italie] ; Monica Autiero [Italie] ; John Guardiola [Italie] ; Luigi Chieco-Bianchi [Italie] ; Anita De Rossi [Italie]Source :
- Virology [ 0042-6822 ] ; 1995.
Abstract
Abstract: We previously demonstrated that a 23-mer peptide (DB3) derived from the V3 loop of the surface glycoprotein of HIV-1 MN strain was able to bind to soluble CD4 and enhance HIV-1 infection. The mechanism and structural features required for these biological activities were studied by using shortened DB3 derivatives and DB3 analogs carrying single amino acid substitutions. We found that peptides in which the aromatic amino acid in position 15 or 16 had been replaced by an uncharged hydrophobic residue (DB3-115 and DB3-116), analogs in which positively charged amino acids were replaced by corresponding D-enantiomers, and shortened DB3-derivatives lost both enhancing activity and ability to bind to soluble CD4. Other peptide variants in which a positively charged amino acid was replaced by asparagine at positions 3 (DB3-N3), 6 (DB3-N6), and 19 (DB3-N19), respectively, retained both enhancing and binding activities, although with different efficiencies. The CD4 binder peptides DB3 and DB3-N19, but none of the CD4 nonbinder peptides, enhanced CD4 expression on peptidetreated cells as well as gp120 binding to both CD4+ cells and soluble CD4. These findings strongly suggest that the peptide/CD4 interaction induced an increase in both CD4 expression and CD4/gp120 binding affinity, which in turn mediated the enhancement of viral infection. A model of the structural conformation of DB3 peptide required for its biological activities is discussed.
Url:
DOI: 10.1006/viro.1995.1003
Affiliations:
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<front><div type="abstract" xml:lang="en">Abstract: We previously demonstrated that a 23-mer peptide (DB3) derived from the V3 loop of the surface glycoprotein of HIV-1 MN strain was able to bind to soluble CD4 and enhance HIV-1 infection. The mechanism and structural features required for these biological activities were studied by using shortened DB3 derivatives and DB3 analogs carrying single amino acid substitutions. We found that peptides in which the aromatic amino acid in position 15 or 16 had been replaced by an uncharged hydrophobic residue (DB3-115 and DB3-116), analogs in which positively charged amino acids were replaced by corresponding D-enantiomers, and shortened DB3-derivatives lost both enhancing activity and ability to bind to soluble CD4. Other peptide variants in which a positively charged amino acid was replaced by asparagine at positions 3 (DB3-N3), 6 (DB3-N6), and 19 (DB3-N19), respectively, retained both enhancing and binding activities, although with different efficiencies. The CD4 binder peptides DB3 and DB3-N19, but none of the CD4 nonbinder peptides, enhanced CD4 expression on peptidetreated cells as well as gp120 binding to both CD4+ cells and soluble CD4. These findings strongly suggest that the peptide/CD4 interaction induced an increase in both CD4 expression and CD4/gp120 binding affinity, which in turn mediated the enhancement of viral infection. A model of the structural conformation of DB3 peptide required for its biological activities is discussed.</div>
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