Journal
CHEMMEDCHEM
Volume 16, Issue 8, Pages 1290-1296Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cmdc.202000892
Keywords
gp120 V3 loop; HIV-1; human pegivirus; peptides; viral interference
Categories
Funding
- ReForM A program of the Faculty of Medicine, University of Regensburg
- German Research Foundation [GRK 1910]
- NIH AIDS Research and Reference Reagent Program [2G12, VRC01, F425 B4e8, ID6, F240, 17B]
- Projekt DEAL
Ask authors/readers for more resources
Co-infection with HPgV-1 can benefit disease progression in HIV-1-infected individuals, with the peptide P6-2 showing inhibitory activity against HIV-1 by interacting with the envelope glycoprotein gp120.
Co-infection with the human pegivirus 1 (HPgV-1) often has a beneficial effect on disease progression in HIV-1-infected individuals. Several HPgV-1 proteins and peptides, including a 20-mer peptide (P6-2) derived from the N-terminal region of the HPgV-1 surface protein E2, have been associated with this phenomenon, which is referred to as viral interference. We identified the cysteine residues, the hydrophobic core tetrapeptide, as well as the C-terminal negative charge as key factors for the HIV-1 inhibitory activity of P6-2. Analysis of mutations in P6-2-resistant HIV-1 indicated a binding site for the peptide in the HIV-1 envelope glycoprotein gp120. In fact, P6-2 was shown to bind to soluble gp120, as well as to a peptide presenting the gp120 V3 loop. Furthermore, the HIV-1 inhibitory activity of P6-2 could be revoked by the V3 loop peptide, thus indicating a molecular mechanism that involves interaction of P6-2 with the gp120 V3 loop.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available