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Báo cáo y học: "Targeting APOBEC3A to the viral nucleoprotein complex confers antiviral activity"

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: "Targeting APOBEC3A to the viral nucleoprotein complex confers antiviral activity. | Retrovirology BioMed Central Research Open Access Targeting APOBEC3A to the viral nucleoprotein complex confers antiviral activity Ritu Goila-Gaur Mohammad A Khan Eri Miyagi Sandra Kao and Klaus Strebel Address Laboratory of Molecular Microbiology Viral Biochemistry Section National Institute of Allergy and Infectious Diseases NIH Building 4 Room 310 4 Center Drive MSC 0460 Bethesda MD 20892-0460 USA Email Ritu Goila-Gaur - rgaur@niaid.nih.gov Mohammad A Khan - mkhan@niaid.nih.gov Eri Miyagi - emiyagi@niaid.nih.gov Sandra Kao - skao@niaid.nih.gov Klaus Strebel - kstrebel@niaid.nih.gov Corresponding author Published 29 August 2007 Received 26 June 2007 Accepted 29 August 2007 Retrovirology 2007 4 61 doi 10.1186 1742-4690-4-61 This article is available from http www.retrovirology.cOm content 4 1 61 2007 Goila-Gaur et al 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 Background APOBEC3 A3 proteins constitute a family of cytidine deaminases that provide intracellular resistance to retrovirus replication and to transposition of endogenous retroelements. A3A has significant homology to the C-terminus of A3G but has only a single cytidine deaminase active site CDA unlike A3G which has a second N-terminal CDA previously found to be important for Vif sensitivity and virus encapsidation. A3A is packaged into HIV-1 virions but unlike A3G does not have antiviral properties. Here we investigated the reason for the lack of A3A antiviral activity. Results Sequence alignment of A3G and A3A revealed significant homology of A3A to the C-terminal region of A3G. However while A3G co-purified with detergent-resistant viral nucleoprotein complexes NPC virus-associated A3A was highly detergent-sensitive leading us to speculate that the