The human immunodeficiency virus (HIV-1) genome encodes for 15 viral proteins and exploits host cellular proteins to complete its life cycle [ 1, 2], which includes viral entry, uncoating, reverse transcription, nuclear import, integration, transcription, translation, viral assembly, and virus budding [ 3- 6].
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Although of crucial importance for the coordination of HIV-1 intracellular transport, nuclear import, and integration, the exact oligomerization state of IN in viruses and viral cellular complexes has been under debate for years, mostly due to a lack of methods to probe IN oligomerization in a spatiotemporally resolved manner during replication.
We and others [15], [16]] have not observed a pre-integration block in 3T3 cells, suggesting that the localization of integrase protein is unrelated to successful nuclear import or integration.
Di Nunzio, F. et al. Human nucleoporins promote HIV-1 docking at the nuclear pore, nuclear import and integration.
Schaller, T. et al. HIV-1 capsid-cyclophilin interactions determine nuclear import pathway, integration targeting and replication efficiency.
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