Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Retrovirology cung cấp cho các bạn kiến thức về ngành y đề tài: Changes in the accessibility of the HIV-1 Integrase C-terminus in the presence of cellular proteins. | Benkhelifa-Ziyyat et al. Retrovirology 2010 7 27 http content 7 1 27 RETR0VIR0L0GY RESEARCH Open Access Changes in the accessibility of the HIV-1 Integrase C-terminus in the presence of cellular proteins 1 1 1 I P s 13 Sofia Benkhelifa-Ziyyat Stephanie Bucher Maria-Antonietta Zanta-Boussif Julie Pasquet Olivier Danos Abstract Background Following entry uncoating and reverse transcription a number of cellular proteins become associated with the Human Immunodeficiency Virus type 1 HIV-1 pre-integration complex PIC . With the goal of obtaining reagents for the analysis of the HIV-1 PIC composition and localisation we have constructed functional integrase IN and matrix MA proteins that can be biotinylated during virus production and captured using streptavidin-coated beads. Results Although the labelled C-terminus allows for the sensitive detection of virion-associated IN it becomes inaccessible in the presence of cellular proteins. This masking is not dependent on the nature of the tag and does not occur with the tagged MA. It was not observed either with an IN mutant unable to interact with LEDGF p75 or when LEDGF p75 was depleted from cells. Conclusion Our observation suggests that a structural rearrangement or oligomerization of the IN protein occurs during the early steps of infection and that this process is related to the presence of LEDGF p75. Background Integration of the Human Immunodeficiency Virus HIV DNA into the host cell chromosome mediated by the integrase IN protein is an obligatory step of the virus life cycle. This endonuclease encoded by the pol gene generates active CA-3 -hydroxyl ends on the viral cDNA and catalyses strand transfer with the chromosomal DNA. IN is also involved in the processing and trafficking of the viral genome throughout the preintegration phase including reverse transcription and nuclear import 1-3 . The IN protein is organized in three domains an N-terminal domain NTD involved in higher order .
