tailieunhanh - Báo cáo y học: " TRIM5α and TRIMCyp form apparent hexamers and their multimeric state is not affected by exposure to restriction-sensitive viruses or by treatment with pharmacological inhibitors"

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: " TRIM5α and TRIMCyp form apparent hexamers and their multimeric state is not affected by exposure to restriction-sensitive viruses or by treatment with pharmacological inhibitors. | Retrovirology BioMed Central Open Access Short report TRIM5a and TRIMCyp form apparent hexamers and their multimeric state is not affected by exposure to restriction-sensitive viruses or by treatment with pharmacological inhibitors Marie-Édith Nepveu-Traversy Julie Bérubé and Lionel Berthoux Address Laboratory of retrovirology University of Québec Trois-Rivières QC G9A 5H7 Canada Email Marie-Édith Nepveu-Traversy - nepveutr@ Julie Bérubé - Lionel Berthoux - lionel_berthoux@ Corresponding author Published 3 November 2009 Received 27 August 2009 Retrovirology 2009 6 100 doi 1742-4690-6-100 Accepted 3 November 2009 This article is available from http content 6 1 100 2009 Nepveu-Traversy 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 Proteins of the TRIM5 family such as TRIM5a and the related TRIMCyp are cytoplasmic factors that can inhibit incoming retroviruses. This type of restriction requires a direct interaction between TRIM5 proteins and capsid proteins that are part of mature intact retroviral cores. In such cores capsids are arranged as hexameric units. Multiple lines of evidence imply that TRIM5 proteins themselves interact with retroviral cores as multimers. Accordingly stabilization by crosslinking agents has revealed that TRIM5a and TRIMCyp are present as trimers in mammalian cells. We report here that TRIM5 proteins seem to form dimers trimers hexamers and multimers of higher complexity in mammalian cells. The hexameric form in particular seems to be the most abundant multimer. Multimerization did not involve disulfide bridges and was not affected by infection with restriction-sensitive viruses or by treatment with the known TRIM5 .