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Báo cáo hóa học: " Characterization of vaccinia virus A12L protein proteolysis and its participation in virus assembly"

Tham khảo tài liệu 'báo cáo hóa học: " characterization of vaccinia virus a12l protein proteolysis and its participation in virus assembly"', luận văn - báo cáo phục vụ nhu cầu học tập, nghiên cứu và làm việc hiệu quả | Virology Journal BioMed Central Research Characterization of vaccinia virus A12L protein proteolysis and its participation in virus assembly Su Jung Yang Open Access Address Department of Microbiology Oregon State University Corvallis Oregon 97331-3804 USA Email Su Jung Yang - sujung.yangs@gmail.com Corresponding author Published I August 2007 Virology Journal 2007 4 78 doi I0.II86 1743-422X-4-78 Received 25 June 2007 Accepted I August 2007 This article is available from http www.virologyj.eom content 4 I 78 2007 Yang 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 Vaccinia virus VV undergoes a proteolytic processing to evolve from immature virus particles into intracellular mature virus particles. Most of structural core protein precursors such as p4a p4b and p25K are assembled into previrions and then proteolytically processed to yield core proteins 4a 4b and 25 K which become components of a mature virus particle. These structural rearrangements take place at a conserved cleavage motif Ala-Gly-X where X is any amino acid and catalyzed by a VV encoded proteinase the I7L gene product. The VV AI2L gene product a 25 kDa protein synthesized at late times during infection is cleaved at an N-terminal AG A site resulting in a I7 kDa cleavage product. However due to the distinct characteristics of AI2L proteolysis such as the localization of both the AI2L full-length protein and its cleavage product in mature virions and two putative cleavage sites Ala-Gly-Lys located at internal and C-terminal region of AI2L ORF it was of interest to examine the AI2L proteolysis for better understanding of regulation and function of VV proteolysis. Here we attempted to examine the in vivo AI2L processing by determining the kinetics of .