tailieunhanh - Báo cáo sinh học: " Oligomerization of the human immunodeficiency virus type 1 (HIV-1) Vpu protein – a genetic, biochemical and biophysical analysis"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: Oligomerization of the human immunodeficiency virus type 1 (HIV-1) Vpu protein – a genetic, biochemical and biophysical analysis | Virology Journal BioMed Central Research Open Access Oligomerization of the human immunodeficiency virus type I HIV-1 Vpu protein - a genetic biochemical and biophysical analysis Amjad Hussain11 Suman R Das11 2 Charu Tanwar 1 and Shahid Jameel 1 Address 1Virology Group International Centre for Genetic Engineering and Biotechnology New Delhi India and 2Laboratory of Viral Diseases NIAID NIH Bethesda Md USA Email Amjad Hussain - amjadicgeb@ Suman R Das - sumanrd@ Charu Tanwar - tanwar_charu@ Shahid Jameel - shahid@ Corresponding author tEqual contributors Published 29 August 2007 Received 4 July 2007 Accepted 29 August 2007 Virology Journal 2007 4 81 doi 1743-422X-4-81 This article is available from http content 4 1 81 2007 Hussain et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background The human immunodeficiency virus type l HIV-l is a complex retrovirus and the causative agent of acquired immunodeficiency syndrome AIDS . The HIV-1 Vpu protein is an oligomeric integral membrane protein essential for particle release viral load and CD4 degradation. In silico models show Vpu to form pentamers with an ion channel activity. Results Using Vpu proteins from a primary subtype C and the pNL4-3 subtype B isolates of HIV- 1 we show oligomerization of the full-length protein as well as its transmembrane TM domain by genetic biochemical and biophysical methods. We also provide direct evidence of the presence of Vpu pentamers in a stable equilibrium with its monomers in vitro. This was also true for the TM domain of Vpu. Confocal microscopy localized Vpu to the endoplasmic reticulum and Golgi regions of the cell as well as to post-Golgi vesicles. In .