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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: Rift Valley fever virus structural proteins: expression, characterization and assembly of recombinant proteins | BioMed Central Virology Journal Research Rift Valley fever virus structural proteins expression characterization and assembly of recombinant proteins Li Liu1 2 Cristina CP Celma1 and Polly Roy 1 Open Access Address Department of Infectious and Tropical Diseases London School of Hygiene and Tropical Medicine Keppel Street London WC1E 7HT UK and 2Present address Centre for Infectious Disease Institute of Cell and Molecular Science Barts and The London Queen Mary s School of Medicine and Dentistry The Blizard Building 4 Newark Street London E1 2AT UK Email Li Liu - li.liu@qmul.ac.uk Cristina CP Celma - cristina.celma@lshtm.ac.uk Polly Roy - polly.roy@lshtm.ac.uk Corresponding author Published 18 July 2008 Received 17 June 2008 Virology Journal 2008 5 82 doi 10.1186 1743-422X-5-82 Accepted 18 July 2008 This article is available from http www.virologyj.cOm content 5 1 82 2008 Liu 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 Studies on Rift Valley Fever Virus RVFV infection process and morphogenesis have been hampered due to the biosafety conditions required to handle this virus making alternative systems such as recombinant virus-like particles that may facilitate understanding of these processes are highly desirable. In this report we present the expression and characterization of RVFV structural proteins N Gn and Gc and demonstrate the efficient generation of RVFV viruslike particles VLPs using a baculovirus expression system. Results A recombinant baculovirus expressing nucleocapsid N protein of RVFV at high level under the control of the polyhedrin promoter was generated. Gel filtration analysis indicated that expressed N protein could form complex multimers. Further N protein complex when .
