tailieunhanh - Báo cáo sinh học: " An ectromelia virus profilin homolog interacts with cellular tropomyosin and viral A-type inclusion protein"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: An ectromelia virus profilin homolog interacts with cellular tropomyosin and viral A-type inclusion protein | Virology Journal BioMed Central Research An ectromelia virus profilin homolog interacts with cellular tropomyosin and viral A-type inclusion protein Christine Butler-Cole Mary J Wagner Melissa Da Silva Gordon D Brown Robert D Burke and Chris Upton Open Access Address Department of Biochemistry and Microbiology University of Victoria Victoria BC V8W 3P6 Canada Email Christine Butler-Cole - Mary J Wagner - wagnerm@ Melissa Da Silva - mdasilva@ Gordon D Brown - gdbrown@ Robert D Burke - rburke@ Chris Upton - cupton@ Corresponding author Published 24 July 2007 Received 14 May 2007 Accepted 24 July 2007 Virology journal 2007 4 76 doi 186 1743-422X-4-76 This article is available from http content 4 1 76 2007 Butler-Cole 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 Background Profilins are critical to cytoskeletal dynamics in eukaryotes however little is known about their viral counterparts. In this study a poxviral profilin homolog ectromelia virus strain Moscow gene 141 ECTV-PH was investigated by a variety of experimental and bioinformatics techniques to characterize its interactions with cellular and viral proteins. Results Profilin-like proteins are encoded by all orthopoxviruses sequenced to date and share over 90 amino acid aa identity. Sequence comparisons show highest similarity to mammalian type 1 profilins however a conserved 3 aa deletion in mammalian type 3 and poxviral profilins suggests that these homologs may be more closely related. Structural analysis shows that ECTV-PH can be successfully modelled onto both the profilin 1 .