Publications
2007
Henriet S, Sinck L, Bec G, Gorelick R J, Marquet R, Paillart J C
Vif is a RNA chaperone that could temporally regulate RNA dimerization and the early steps of HIV-1 reverse transcription Article de journal
Dans: Nucleic Acids Res, vol. 35, no. 15, p. 5141-5153, 2007, ISBN: 17660191, (1362-4962 (Electronic) Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't).
Résumé | Liens | BibTeX | Étiquettes: Amino Acyl/metabolism RNA, Capsid Proteins/metabolism DNA, gag/metabolism Gene Products, Human Immunodeficiency Virus, Human Immunodeficiency Virus vif Gene Products, MARQUET, PAILLART, Single-Stranded/biosynthesis Dimerization Gene Products, Transfer, Unité ARN, vif/*metabolism HIV-1/*genetics Molecular Chaperones/*metabolism RNA, Viral/*metabolism *Reverse Transcription Viral Proteins/metabolism gag Gene Products
@article{,
title = {Vif is a RNA chaperone that could temporally regulate RNA dimerization and the early steps of HIV-1 reverse transcription},
author = {S Henriet and L Sinck and G Bec and R J Gorelick and R Marquet and J C Paillart},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17660191},
isbn = {17660191},
year = {2007},
date = {2007-01-01},
journal = {Nucleic Acids Res},
volume = {35},
number = {15},
pages = {5141-5153},
abstract = {HIV-1 Vif (viral infectivity factor) is associated with the assembly complexes and packaged at low level into the viral particles, and is essential for viral replication in non-permissive cells. Viral particles produced in the absence of Vif exhibit structural defects and are defective in the early steps of reverse transcription. Here, we show that Vif is able to anneal primer tRNA(Lys3) to the viral RNA, to decrease pausing of reverse transcriptase during (-) strand strong-stop DNA synthesis, and to promote the first strand transfer. Vif also stimulates formation of loose HIV-1 genomic RNA dimers. These results indicate that Vif is a bona fide RNA chaperone. We next studied the effects of Vif in the presence of HIV-1 NCp, which is a well-established RNA chaperone. Vif inhibits NCp-mediated formation of tight RNA dimers and hybridization of tRNA(Lys3), while it has little effects on NCp-mediated strand transfer and it collaborates with nucleocapsid (NC) to increase RT processivity. Thus, Vif might negatively regulate NC-assisted maturation of the RNA dimer and early steps of reverse transcription in the assembly complexes, but these inhibitory effects would be relieved after viral budding, thanks to the limited packaging of Vif in the virions.},
note = {1362-4962 (Electronic)
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't},
keywords = {Amino Acyl/metabolism RNA, Capsid Proteins/metabolism DNA, gag/metabolism Gene Products, Human Immunodeficiency Virus, Human Immunodeficiency Virus vif Gene Products, MARQUET, PAILLART, Single-Stranded/biosynthesis Dimerization Gene Products, Transfer, Unité ARN, vif/*metabolism HIV-1/*genetics Molecular Chaperones/*metabolism RNA, Viral/*metabolism *Reverse Transcription Viral Proteins/metabolism gag Gene Products},
pubstate = {published},
tppubtype = {article}
}
Bernacchi S, Henriet S, Dumas P, Paillart J C, Marquet R
RNA and DNA binding properties of HIV-1 Vif protein: a fluorescence study Article de journal
Dans: J Biol Chem, vol. 282, no. 36, p. 26361-26368, 2007, ISBN: 17609216.
Résumé | Liens | BibTeX | Étiquettes: 5' Untranslated Regions/genetics/immunology/metabolism Binding Sites/physiology Cytidine Deaminase Cytosine Deaminase/immunology/metabolism DNA, gag/genetics/immunology/metabolism Gene Products, Human Immunodeficiency Virus, MARQUET, Natural/physiology Nucleoside Deaminases/immunology/metabolism Oligonucleotides/genetics/immunology/metabolism Protein Binding/physiology Protein Biosynthesis/physiology RNA, PAILLART, Unité ARN, vif/genetics/immunology/*metabolism Genome, Viral/genetics/immunology/*metabolism DNA-Binding Proteins/genetics/immunology/*metabolism Gene Products, Viral/genetics/immunology/*metabolism RNA-Binding Proteins/genetics/immunology/*metabolism Repressor Proteins/genetics/immunology/*metabolism vif Gene Products, Viral/physiology HIV Long Terminal Repeat/physiology HIV-1/genetics/immunology/*metabolism/pathogenicity Humans Immunity
@article{,
title = {RNA and DNA binding properties of HIV-1 Vif protein: a fluorescence study},
author = {S Bernacchi and S Henriet and P Dumas and J C Paillart and R Marquet},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17609216},
isbn = {17609216},
year = {2007},
date = {2007-01-01},
journal = {J Biol Chem},
volume = {282},
number = {36},
pages = {26361-26368},
abstract = {The HIV-1 viral infectivity factor (Vif) is a small basic protein essential for viral fitness and pathogenicity. Some "non-permissive" cell lines cannot sustain replication of Vif(-) HIV-1 virions. In these cells, Vif counteracts the natural antiretroviral activity of the DNA-editing enzymes APOBEC3G/3F. Moreover, Vif is packaged into viral particles through a strong interaction with genomic RNA in viral nucleoprotein complexes. To gain insights into determinants of this binding process, we performed the first characterization of Vif/nucleic acid interactions using Vif intrinsic fluorescence. We determined the affinity of Vif for RNA fragments corresponding to various regions of the HIV-1 genome. Our results demonstrated preferential and moderately cooperative binding for RNAs corresponding to the 5'-untranslated region of HIV-1 (5'-untranslated region) and gag (cooperativity parameter omega approximately 65-80, and K(d) = 45-55 nM). In addition, fluorescence spectroscopy allowed us to point out the TAR apical loop and a short region in gag as primary strong affinity binding sites (K(d) = 9.5-14 nM). Interestingly, beside its RNA binding properties, the Vif protein can also bind the corresponding DNA oligonucleotides and their complementary counterparts with an affinity similar to the one observed for the RNA sequences, while other DNA sequences displayed reduced affinity. Taken together, our results suggest that Vif binding to RNA and DNA offers several non-exclusive ways to counteract APOBEC3G/3F factors, in addition to the well documented Vif-induced degradation by the proteasome and to the Vif-mediated repression of translation of these antiviral factors.},
keywords = {5' Untranslated Regions/genetics/immunology/metabolism Binding Sites/physiology Cytidine Deaminase Cytosine Deaminase/immunology/metabolism DNA, gag/genetics/immunology/metabolism Gene Products, Human Immunodeficiency Virus, MARQUET, Natural/physiology Nucleoside Deaminases/immunology/metabolism Oligonucleotides/genetics/immunology/metabolism Protein Binding/physiology Protein Biosynthesis/physiology RNA, PAILLART, Unité ARN, vif/genetics/immunology/*metabolism Genome, Viral/genetics/immunology/*metabolism DNA-Binding Proteins/genetics/immunology/*metabolism Gene Products, Viral/genetics/immunology/*metabolism RNA-Binding Proteins/genetics/immunology/*metabolism Repressor Proteins/genetics/immunology/*metabolism vif Gene Products, Viral/physiology HIV Long Terminal Repeat/physiology HIV-1/genetics/immunology/*metabolism/pathogenicity Humans Immunity},
pubstate = {published},
tppubtype = {article}
}