HIV-1 exploits importin 7 to maximize nuclear import of its DNA genome
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* Corresponding author: Ariberto Fassati a.fassati@ucl.ac.uk
Retrovirology 2009, 6:11 doi:10.1186/1742-4690-6-11
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BioMed Central: 4 citations
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Research
Mutations affecting interaction of integrase with TNPO3 do not prevent HIV-1 cDNA nuclear import Alexandra Cribier, Emmanuel Segeral, Olivier Delelis, Vincent Parissi, Aurelie Simon, Marc Ruff, Richard Benarous, Stephane Emiliani Retrovirology 2011, 8:104 (16 December 2011) The functional analysis of HIV-1 IN mutants reveals distinct structural basis for TNPO3 interaction and suggests that the interaction between IN and TNPO3 is not a major determinant of nuclear import but could take place at a nuclear step prior to integration.
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Research
Interplay between HIV Entry and Transportin-SR2 Dependency Wannes Thys, Stéphanie De Houwer, Jonas Demeulemeester, Oliver Taltynov, Renée Vancraenenbroeck, Melanie Gérard, Jan De Rijck, Rik Gijsbers, Frauke Christ, Zeger Debyser Retrovirology 2011, 8:7 (30 January 2011) Analysis of viral specificity reveals that TRN-SR2 is not used to the same extent by all lentiviruses. The DNA flap does not determine the TRN-SR2 requirement of HIV-1. The HIV-1 N74D capsid mutant is independent of TRN-SR2 when pseudotyped with the vesicular stomatitis virus glycoprotein (VSV-G). The dependency on TRN-SR2 is lost when the HIV N74D capsid mutant is pseudotyped with envelopes mediating pH-dependent endocytosis, such as the VSV-G and Ebola virus envelopes.
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Review
Host hindrance to HIV-1 replication in monocytes and macrophages Anna Bergamaschi, Gianfranco Pancino Retrovirology 2010, 7:31 (7 April 2010) |
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Research
Aviad Levin, Ayelet Armon-Omer, Joseph Rosenbluh, Naomi Melamed-Book, Adolf Graessmann, Elisabeth Waigmann, Abraham Loyter Retrovirology 2009, 6:112 (5 December 2009) |