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16th International AIDS ConferenceToronto, Canada - August 13 - 18, 2006 |
Int Conf AIDS. 2006 Aug 13-18;16 Abstract No. TuAa0103
Song R., Kafaie J., Laughrea M.
McGill AIDS Centre, Experimental Medicine, McGill; Lady Davis Institute, Jewish General Hospital, Montreal, Canada
BACKGROUND: The Human Immunodeficiency Virus type 1 (HIV-1) genome consists of 2 identical genomic RNAs (gRNA) linked to each other noncovalently. The 5´UTR (untranslated region) of the HIV-1 genome is believed to play an important role in gRNA dimerization.
METHODS: We designed site-directed mutations in the 5´UTR to characterize its role in HIV-1 genome dimerization.
RESULTS: 1) The deltaDIS (deletion of the dimerization initiation site) mutation decreased gRNA dimerization levels and changed the gRNA dimer conformations. The deltaPBSh (deletion of the primer bindng site stem-loop) mutation inhibited dimerization more than deltaDIS. So, the PBSh includes a more important gRNA dimerization signal than the DIS and/or it completely destroys the structure of the 5´UTR.
2) Mutating the nucleotides of the putative U5-AUG duplex inhibited gRNA dimerization, and so far our results neither rule out nor support that this putative duplex formation promotes dimerization.
3) Our results show that the term "immature dimer" may represent a spectrum of different conformations. We call "transition dimer" (TD) one unique conformation within this spectrum. The gRNA dimerization level increases faster in viruses produced by HeLa cells than in viruses produced by 293T cells.
CONCLUSIONS: The 5´ Terminal Dimerization Domain of HIV-1 consists of the DIS hairpin (also called SL1 or Kissing-Loop-Domain) and other regions, such as the PBSh. The immature gRNA dimer is a collection of TDs. And the immature gRNA dimer can adopt a spectrum of different conformations during the gRNA dimer maturation process, a process which is also affected by cellular factor(s).
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2006-08-13
TuAa0103
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