Abstract
Preventing cell entry of human immunodeficiency virus 1 (HIV-1) is of interest for the development of innovative therapies. We previously reported a specific interaction between HIV-1 envelope glycoprotein 120 (gp120) and Tat at the cell surface, which enhances virus attachment and entry. We also identified a gp120-mimicking peptide, CT319, that competes with gp120 for Tat binding, thus inhibiting HIV-1 infection. Here we report a molecular dissection of gp120 regions involved in this mechanism. Our findings identify the V1/V2 loop of gp120 as involved in Tat binding, and define this interaction as functionally relevant for HIV-1 entry into host cells.
Original language | English |
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Pages (from-to) | 2943-2951 |
Number of pages | 9 |
Journal | FEBS Letters |
Volume | 587 |
Issue number | 18 |
DOIs | |
Publication status | Published - Sep 17 2013 |
Keywords
- gp120
- HIV-1
- Peptide
- Tat
- Virus entry
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Cell Biology
- Genetics
- Molecular Biology
- Structural Biology