tailieunhanh - báo cáo hóa học:"Packaging of actin into Ebola virus VLPs"

Tuyển tập các báo cáo nghiên cứu về hóa học được đăng trên tạp chí sinh học đề tài :Packaging of actin into Ebola virus VLPs | Virology Journal BioMed Central Short report Packaging of actin into Ebola virus VLPs Ziying Han and Ronald N Harty Open Access Address Department of Pathobiology School of Veterinary Medicine University of Pennsylvania 3800 Spruce St. Philadelphia PA 19104 USA Email Ziying Han - ziyinghan@ Ronald N Harty - rharty@ Corresponding author Published 20 December 2005 Received 05 August 2005 Accepted 20 December 2005 Virology Journal 2005 2 92 doi 1743-422X-2-92 This article is available from http content 2 1 92 2005 Han and Harty 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 The actin cytoskeleton has been implicated in playing an important role assembly and budding of several RNA virus families including retroviruses and paramyxoviruses. In this report we sought to determine whether actin is incorporated into Ebola VLPs and thus may play a role in assembly and or budding of Ebola virus. Our results indicated that actin and Ebola virus VP40 strongly colocalized in transfected cells as determined by confocal microscopy. In addition actin was packaged into budding VP40 VLPs as determined by a functional budding assay and protease protection assay. Co-expression of a membrane-anchored form of Ebola virus GP enhanced the release of both VP40 and actin in VLPs. Lastly disruption of the actin cytoskeleton with latrunculin-A suggests that actin may play a functional role in budding of VP40 GP VLPs. These data suggest that VP40 may interact with cellular actin and that actin may play a role in assembly and or budding of Ebola VLPs. Introduction Ebola virus VP40 is known to bud from cells as a virus-like particle VLP independent of additional virus proteins 1-4 . The most .