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: " The formation of cysteine-linked dimers of BST-2/tetherin is important for inhibition of HIV-1 virus release but not for sensitivity to Vpu. | Retrovirology BioMed Central Research The formation of cysteine-linked dimers of BST-2 tetherin is important for inhibition of HIV-1 virus release but not for sensitivity to Vpu Amy J Andrew Eri Miyagif Sandra Kao and Klaus Strebel Address Laboratory of Molecular Microbiology Viral Biochemistry Section National Institute of Allergy and Infectious Diseases NIH Bethesda Maryland 20892-0460 USA Email Amy J Andrew - andrewa@ Eri Miyagi - emiyagi@ Sandra Kao - skao@ Klaus Strebel - kstrebel@ Corresponding author tEqual contributors Open Access Published 8 September 2009 Received 21 July 2009 Retrovirology 2009 6 80 doi 1742-4690-6-80 Accepted 8 September 2009 This article is available from http content 6 1 80 2009 Andrew 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 1 HIV-1 Vpu protein enhances virus release from infected cells and induces proteasomal degradation of CD4. Recent work identified BST-2 CD317 as a host factor that inhibits HIV-1 virus release in a Vpu sensitive manner. A current working model proposes that BST-2 inhibits virus release by tethering viral particles to the cell surface thereby triggering their subsequent endocytosis. Results Here we defined structural properties of BST-2 required for inhibition of virus release and for sensitivity to Vpu. We found that BST-2 is modified by N-linked glycosylation at two sites in the extracellular domain. However N-linked glycosylation was not important for inhibition of HIV-1 virus release nor did it affect surface expression or sensitivity to Vpu. Rodent BST-2 was previously found to form cysteine-linked dimers. Analysis of
