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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:"The control of viral infection by tripartite motif proteins and cyclophilin A. | Retrovirology BioMed Central Open Access Review The control of viral infection by tripartite motif proteins and cyclophilin A Greg J Towers Address MRC Centre for Medical Molecular Virology Department of Infection Royal Free and University College London Medical School 46 Cleveland Street London W1T4JF UK Email Greg J Towers - g.towers@ucl.ac.uk Corresponding author Published 12 June 2007 Retrovirology 2007 4 40 doi 10.1186 1742-4690-4-40 Received 3 May 2007 Accepted 12 June 2007 This article is available from http www.retrovirology.cOm content 4 1 40 2007 Towers licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http creativecommons.org licenses by 2.0 which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract The control of retroviral infection by antiviral factors referred to as restriction factors has become an exciting area in infectious disease research. TRIM5a has emerged as an important restriction factor impacting on retroviral replication including HIV-1 replication in primates. TRIM5a has a tripartite motif comprising RING B-Box and coiled coil domains. The antiviral a splice variant additionally encodes a B30.2 domain which is recruited to incoming viral cores and determines antiviral specificity. TRIM5 is ubiquitinylated and rapidly turned over by the proteasome in a RING dependent way. Protecting restricted virus from degradation by inhibiting the proteasome rescues DNA synthesis but not infectivity indicating that restriction of infectivity by TRIM5a does not depend on the proteasome but the early block to DNA synthesis is likely to be mediated by rapid degradation of the restricted cores. The peptidyl prolyl isomerase enzyme cyclophilin A isomerises a peptide bond on the surface of the HIV-1 capsid and impacts on .
