Little is known concerning the timing of the interaction of cellular proteins with IN. Accepting that INI1 IBD interacts with IN in the same way as the full-length protein, the observation that a reliable ternary complex between IN, LEDGF and INI1 IBD can be produced suggests that the two cellular proteins may interact with the PIC during the same temporal window. The connection of INI1 with the PIC is probably c-Met inhibitor an earlier event because it was shown that INI1 is incorporated in mature virions, that HIV 1 infection triggers the nuclear export of INI1 which associates with the incoming HIV 1 PICs and that INI1 exists in the reverse transcription complex. The very fact that INI1 expression in a cell line removed for your gene encoding INI1 improves viral replication in a dose-dependent fashion suggests that IN interacts with these newly produced INI1 molecules. Taken together, these observations suggest that the relationship between INI1 IBD and IN we discover in our construction is likely to arise between Organism reverse transcription and 39 processing and before nuclear translocation. After nuclear internalization, both LEDGF and INI1 will likely stabilize the highly flexible IN. LEDGF probably balances the IN tetramer while INI1 may stop car integration and non specific protein interactions along the way to nucleosomes. More over, INI1, as part of the SWI/SNF chromatin remodeling complex, is thought to play a role in the control of viral integration through the reorganization of the host genome. Certainly, in vitro tests showed that secure nucleosomes reconstituted on clearly positioning DNA sequences inhibit the integration of viral DNA and that purified SWI/SNF complexes recover integration, suggesting an efficient HIV 1 integration and coupling between nucleosome remodeling. Hence, SWI/SNF is considered to promote integration in target nucleosomes through its relaxing activity, by creating a ideal nucleosomal DNA for the strand transfer reaction. We imagine that INI1 might be released from IN through the nucleosome remodeling process as a way to stimulate its integration function. In comparison, after launch, LEDGF is likely to remain attached with IN in order to preserve its tetramer organization and to enhance the efficiency of integration. In the context, it’s been shown that the IN LEDGF connections and IN INI1 are useful for viral infection. The INI1 and LEDGF cellular proteins would have two major functions in the first state of HIV 1 replication. One function would be to nucleosome remodeling through INI1, an integral part of the SWI/SNF complex and to target the PIC to chromatin and nucleosomes through the PWWP domain of LEDGF. Their 2nd function will be a chaperon function.