Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Respiratory Research cung cấp cho các bạn kiến thức về ngành y đề tài: Modulation of HIV-1-host interaction: role of the Vpu accessory protein. | Dubé et al. Retrovirology 2010 7 114 http content 7 1 114 RETR0VIR0L0GY REVIEW Open Access Modulation of HIV-1-host interaction role of the Vpu accessory protein Mathieu DubéH Mariana G BegoH Catherine PaquayH Éric A Cohen1 2 Abstract Viral protein U Vpu is a type 1 membrane-associated accessory protein that is unique to human immunodeficiency virus type 1 HIV-1 and a subset of related simian immunodeficiency virus SIV . The Vpu protein encoded by HIV-1 is associated with two primary functions during the viral life cycle. First it contributes to HIV-1-induced CD4 receptor downregulation by mediating the proteasomal degradation of newly synthesized CD4 molecules in the endoplasmic reticulum ER . Second it enhances the release of progeny virions from infected cells by antagonizing Tetherin an interferon IFN -regulated host restriction factor that directly cross-links virions on host cell-surface. This review will mostly focus on recent advances on the role of Vpu in CD4 downregulation and Tetherin antagonism and will discuss how these two functions may have impacted primate immunodeficiency virus cross-species transmission and the emergence of pandemic strain of HIV-1. Introduction HIV-1 interaction with host target cells is complex with nearly every step of the virus infection cycle relying on the recruitment of cellular proteins and basic machineries by viral proteins 1 . For instance the Tat regulatory protein recruits the pTEFb complex during viral transcription to enhance host RNA polymerase II proces-sivity and promote efficient elongation of viral transcripts reviewed in 2 . Similarly the p6 domain of the Gag structural protein interacts with the ESCRT complex during viral assembly to direct the budding of progeny virions reviewed in 3 . Recent discoveries have shed light on an additional level of complexity involving host proteins that provide considerable resistance to infection by HIV-1 and other viruses via cell-autonomous mechanisms
