Journal article
HIV-1 Vpr exhibits high affinity for LTR sequences commonly encountered during late stage disease and HIVD
Journal of neurovirology, Vol.12, pp.40-40
01 May 2006
Abstract
Human immunodeficiency virus type 1 (HIV-1) viral protein R (Vpr) is a virion-associated protein that transactivates the HIV-1 long terminal repeat (LTR), as well as other eukaryotic promoters. We have used the electrophoretic mobility shift assay to demonstrate the direct binding of purified Vpr (strain pNL4-3) to HIV-1 LTR sequences that span the adjacent CCAAT/enhancer binding protein (C/EBP) site I, NF-kappa B site II, and ATF/CREB binding site (nt -95 to -130, relative to the start of transcription). We also observed binding between HIV-1 Vpr and the LTR C/EBP site II (nt -167 to -175). A total of 94.7% of LTRs derived from peripheral blood displayed high relative Vpr binding affinity at C/EBP site I, while only 5.3% exhibited a low relative Vpr binding affinity phenotype at this site. All LTRs derived from peripheral blood exhibited a high relative Vpr binding phenotype at C/EBP site II. These results suggest a preference for the maintenance of two cis-acting elements with high affinity for Vpr within LTRs derived from peripheral blood in late stage disease and during development of HIVD. Additional studies have also demonstrated that naturally occurring sequence variation within C/EBP site I and II that correlates with disease progression can dramatically alter the relative affinity of Vpr for these cis-acting elements. Additional studies have also suggested a competitive interaction between Vpr and C/EBP factors for binding sites I and II. These studies suggest that Vpr may regulate the interaction of members of the C/EBP transcription factor family with the viral LTR.
Metrics
3 Record Views
Details
- Title
- HIV-1 Vpr exhibits high affinity for LTR sequences commonly encountered during late stage disease and HIVD
- Creators
- E KilareskiYujie LiuS WebsterM NonnemacherB Wigdahl
- Publication Details
- Journal of neurovirology, Vol.12, pp.40-40
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Microbiology and Immunology
- Identifiers
- 991019170133804721