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: SAMHD1: a new insight into HIV-1 restriction in myeloid cells. | RETROVIROLOGY SAMHD1 a new insight into HIV-1 restriction in myeloid cells St Gelais and Wu St Gelais and Wu Retrovirology 2011 8 55 http content 8 1 55 8 July 2011 2 BioMed Central St Gelais and Wu Retrovirology 2011 8 55 http content 8 1 55 RETR0VIR0L0GY VIEWPOINTS Open Access SAMHD1 a new insight into HIV-1 restriction in myeloid cells Corine St Gelais and Li Wu Abstract Human myeloid-lineage cells are refractory to HIV-1 infection. The Vpx proteins from HIV-2 and sooty mangabey SIV render these cells permissive to HIV-1 infection through proteasomal degradation of a putative restriction factor. Two recent studies discovered the cellular protein SAMHD1 to be this restriction factor demonstrating that Vpx induces proteasomal degradation of SAMHD1 and enhances HIV-1 infection in myeloid-lineage cells. SAMHD1 functions as a myeloid-cell-specific HIV-1 restriction factor by inhibiting viral DNA synthesis. Here we discuss the implications of these findings in delineating the mechanisms of HIV-1 restriction in myeloid-lineage cells and the potential role of Vpx in lentiviral pathogenesis. Introduction Myeloid-lineage cells including monocytes dendritic cells DCs and macrophages play a multifaceted role in HIV-1 initial infection and viral dissemination however these cell types are restrictive to post-entry HIV-1 infection in vitro 1 2 . For gene therapy purposes transduction of human DCs with an HIV-1-derived lentiviral vector can be signific antly enhanced by preincubation with virus-like particles derived from SIV 3 . Subsequent studies indicated that Vpx proteins from sooty mangabey SIV SIVsm and HIV-2 lineages efficiently enhance HIV-1 infection in human DCs and promote the accumulation of full-length viral DNA 4 . Further studies from several laboratories suggested that Vpx similar to HIV-1 Vpr interacts with the DCAF1 component of the CUL4A DDB1 and E3 ubiquitin ligase complex reviewed in 5 6 . However only SIVsm .
