Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài:Efficient trapping of HIV-1 envelope protein by hetero-oligomerization with an N-helix chimera | Retrovirology BioMed Central Research Efficient trapping of HIV-1 envelope protein by hetero-oligomerization with an N-helix chimera Wu Ou and Jonathan Silver Open Access Address Laboratory of Molecular Microbiology National Institute of Allergy and Infectious Diseases National Institutes of Health Building 4 Room 336 Bethesda MD 20892 USA Email Wu Ou - wou@ Jonathan Silver - jsilver@ Corresponding author Published 10 August 2005 Received 22 June 2005 Retrovirology 2005 2 51 doi 1742-4690-2-51 Accepted 10 August 2005 This article is available from http content 2 1 51 2005 Ou and Silver 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 N-heptad repeat region of the HIV-1 Transmembrane Envelope protein is a trimerization domain that forms part of a six helix bundle crucial to Envelope-mediated membrane fusion. N-heptad repeat peptides have been used as extracellular reagents to inhibit virus fusion. Results When expressed intracellularly with wild-type HIV-1 Envelope protein the N-heptad repeat domain efficiently hetero-oligomerized with Envelope and trapped it in the endoplasmic reticulum or early Golgi as indicated by lack of transport to the cell surface absent proteolytic processing and aberrant glycosylation. Conclusion Post-translational processing of HIV Envelope is very sensitive to an agent that binds to the N-heptad repeat during synthesis suggesting that it might be possible to modify drugs that bind to this region to have transport-blocking properties. Background Retroviral envelope proteins Env are synthesized as precursor proteins in the secretory pathway. After co-transla-tional transfer to the endoplasmic reticulum ER the envelope .
