tailieunhanh - Báo cáo sinh học: " Regulation of HTLV-1 Gag budding by Vps4A, Vps4B, and AIP1/Alix"

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: Regulation of HTLV-1 Gag budding by Vps4A, Vps4B, and AIP1/Alix | Virology Journal BioMed Central Research Open Access Regulation of HTLV-I Gag budding by Vps4A Vps4B and AIPI Alix Shuzo Urata1 2 3 Hideyoshi Yokosawa3 and Jiro Yasuda 1 2 Address 1First Department of Forensic Science National Research Institute of Police Science Kashiwa 277-0882 Japan 2CREST Japan Science and Technology Agency Saitama 332-0012 Japan and 3Department of Biochemistry Graduate School of Pharmaceutical Sciences Hokkaido University Sapporo 060-0812 Japan Email Shuzo Urata - urata@ HideyoshiYokosawa - yoko@ Jiro Yasuda - yasuda@ Corresponding author Published 2 July 2007 Received 18 June 2007 Accepted 2 July 2007 Virology Journal 2007 4 66 doi 1743-422X-4-66 This article is available from http content 4 1 66 2007 Urata 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 HTLV-1 Gag protein is a matrix protein that contains the PTAP and PPPY sequences as L-domain motifs and which can be released from mammalian cells in the form of virus-like particles VLPs . The cellular factors Tsg 101 and interact with PTAP and PPPY respectively within the HTLV-1 Gag polyprotein. Tsg101 forms a complex with Vps28 and Vps37 ESCRT-I complex and plays an important role in the class E Vps pathway which mediates protein sorting and invagination of vesicles into multivesicular bodies. is an E3 ubiquitin ligase that binds to the PPPY motif through its WW motif but its function is still unknown. In the present study to investigate the mechanism of HTLV-1 budding in detail we analyzed HTLV-1 budding using dominant negative DN forms of the class E proteins. Results Here we report that DN forms of Vps4A Vps4B and AIP1 inhibit HTLV-1 .

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