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M3i
Insect Models of Innate Immunity
Publications
2003
Goldschmidt V, Ehresmann C, Ehresmann B, Marquet R
Does the HIV-1 primer activation signal interact with tRNA3(Lys) during the initiation of reverse transcription? Journal Article
In: Nucleic Acids Res, vol. 31, no. 3, pp. 850-859, 2003, ISBN: 12560480, (1362-4962 Journal Article).
Abstract | Links | BibTeX | Tags: Amino Acyl/chemistry/*metabolism RNA, Base Sequence Binding Sites DNA Primers DNA, Genetic, MARQUET, Non-U.S. Gov't *Transcription, Transfer, Unité ARN, Viral HIV-1/*genetics HIV-1 Reverse Transcriptase/*metabolism Kinetics Molecular Sequence Data Mutation Nucleic Acid Conformation Oligoribonucleotides RNA, Viral/biosynthesis *Gene Expression Regulation, Viral/chemistry/genetics/metabolism Support
@article{,
title = {Does the HIV-1 primer activation signal interact with tRNA3(Lys) during the initiation of reverse transcription?},
author = {V Goldschmidt and C Ehresmann and B Ehresmann and R Marquet},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12560480},
isbn = {12560480},
year = {2003},
date = {2003-01-01},
journal = {Nucleic Acids Res},
volume = {31},
number = {3},
pages = {850-859},
abstract = {Reverse transcription of HIV-1 RNA is primed by a tRNA3(Lys) molecule bound at the primer binding site (PBS). Complex intermolecular interactions were proposed between tRNA3(Lys) and the RNA of the HIV-1 Mal isolate. Recently, an alternative interaction was proposed between the TPsiC stem of tRNA3(Lys) and a primer activation signal (PAS) of the Lai and Hxb2 RNAs, suggesting major structural variations in the reverse transcription complex of different HIV-1 strains. Here, we analyzed mutants of the Hxb2 RNA that prevent the interaction between the PAS and tRNA3(Lys) or/and a complementary sequence in the viral RNA. We compared the kinetics of reverse transcription of the wild type and mutant Hxb2 RNAs, using either tRNA3(Lys) or an 18mer oligoribonucleotide complementary to the PBS, which cannot interact with the PAS, as primers. We also used chemical probing to test the structure of the mutant and wild type RNAs, as well as the complex formed between the later RNA and tRNA3(Lys). These experiments, together with the analysis of long term replication data of mutant viruses obtained by C. Morrow and coworkers (Birmingham, USA) that use alternate tRNAs as primers, strongly suggest that the interaction between the Hxb2 PAS and tRNA3(Lys) does not exist. Instead, the effects of the vRNA mutations on reverse transcription seem to be linked to incorrect folding of the mutant RNAs.},
note = {1362-4962
Journal Article},
keywords = {Amino Acyl/chemistry/*metabolism RNA, Base Sequence Binding Sites DNA Primers DNA, Genetic, MARQUET, Non-U.S. Gov't *Transcription, Transfer, Unité ARN, Viral HIV-1/*genetics HIV-1 Reverse Transcriptase/*metabolism Kinetics Molecular Sequence Data Mutation Nucleic Acid Conformation Oligoribonucleotides RNA, Viral/biosynthesis *Gene Expression Regulation, Viral/chemistry/genetics/metabolism Support},
pubstate = {published},
tppubtype = {article}
}
Reverse transcription of HIV-1 RNA is primed by a tRNA3(Lys) molecule bound at the primer binding site (PBS). Complex intermolecular interactions were proposed between tRNA3(Lys) and the RNA of the HIV-1 Mal isolate. Recently, an alternative interaction was proposed between the TPsiC stem of tRNA3(Lys) and a primer activation signal (PAS) of the Lai and Hxb2 RNAs, suggesting major structural variations in the reverse transcription complex of different HIV-1 strains. Here, we analyzed mutants of the Hxb2 RNA that prevent the interaction between the PAS and tRNA3(Lys) or/and a complementary sequence in the viral RNA. We compared the kinetics of reverse transcription of the wild type and mutant Hxb2 RNAs, using either tRNA3(Lys) or an 18mer oligoribonucleotide complementary to the PBS, which cannot interact with the PAS, as primers. We also used chemical probing to test the structure of the mutant and wild type RNAs, as well as the complex formed between the later RNA and tRNA3(Lys). These experiments, together with the analysis of long term replication data of mutant viruses obtained by C. Morrow and coworkers (Birmingham, USA) that use alternate tRNAs as primers, strongly suggest that the interaction between the Hxb2 PAS and tRNA3(Lys) does not exist. Instead, the effects of the vRNA mutations on reverse transcription seem to be linked to incorrect folding of the mutant RNAs.
1992
Lavignon M, Tounekti N, Rayner B, Imbach J L, Keith G, Paoletti J, Malvy C
Inhibition of murine leukemia viruses by nuclease-resistant alpha-oligonucleotides Journal Article
In: Antisense Res Dev, vol. 2, no. 4, pp. 315-324, 1992, ISBN: 1292779, (1050-5261 Journal Article).
Abstract | Links | BibTeX | Tags: 3T3 Cells Animals Base Sequence Binding Sites Culture Media Friend murine leukemia virus/*drug effects/genetics/physiology Mice Molecular Sequence Data Moloney murine leukemia virus/*drug effects/genetics/physiology Oligonucleotides, Antisense/metabolism/*pharmacology RNA, Genetic/drug effects, Genetic/drug effects Translation, Messenger/chemistry/genetics/metabolism RNA, Non-U.S. Gov't Transcription, Unité ARN, Viral/chemistry/genetics/metabolism Support
@article{,
title = {Inhibition of murine leukemia viruses by nuclease-resistant alpha-oligonucleotides},
author = {M Lavignon and N Tounekti and B Rayner and J L Imbach and G Keith and J Paoletti and C Malvy},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1292779},
isbn = {1292779},
year = {1992},
date = {1992-01-01},
journal = {Antisense Res Dev},
volume = {2},
number = {4},
pages = {315-324},
abstract = {We studied the antiviral activity of nuclease-resistant alpha-anomeric oligonucleotides. An alpha-oligonucleotide (20-mer) targeted to the primer binding site (PBS) of murine retroviruses inhibited viral spreading. The inhibition only occurred when the cells had been electropermeabilized in the presence of the oligonucleotide. The PBS sequence is involved in reverse transcription and in translation. The data suggest that the oligonucleotide could perturb reverse transcription activity. Thus, either the oligonucleotide induced a decrease in initiation or it inhibited the extension of the minus or plus strands DNA during reverse transcription. These results show that reverse transcription may be an interesting target for antisense oligonucleotides.},
note = {1050-5261
Journal Article},
keywords = {3T3 Cells Animals Base Sequence Binding Sites Culture Media Friend murine leukemia virus/*drug effects/genetics/physiology Mice Molecular Sequence Data Moloney murine leukemia virus/*drug effects/genetics/physiology Oligonucleotides, Antisense/metabolism/*pharmacology RNA, Genetic/drug effects, Genetic/drug effects Translation, Messenger/chemistry/genetics/metabolism RNA, Non-U.S. Gov't Transcription, Unité ARN, Viral/chemistry/genetics/metabolism Support},
pubstate = {published},
tppubtype = {article}
}
We studied the antiviral activity of nuclease-resistant alpha-anomeric oligonucleotides. An alpha-oligonucleotide (20-mer) targeted to the primer binding site (PBS) of murine retroviruses inhibited viral spreading. The inhibition only occurred when the cells had been electropermeabilized in the presence of the oligonucleotide. The PBS sequence is involved in reverse transcription and in translation. The data suggest that the oligonucleotide could perturb reverse transcription activity. Thus, either the oligonucleotide induced a decrease in initiation or it inhibited the extension of the minus or plus strands DNA during reverse transcription. These results show that reverse transcription may be an interesting target for antisense oligonucleotides.