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: Mutational analysis of the potential catalytic residues of the VV G1L metalloproteinase | Virology Journal BioMed Central Short report Open Access Mutational analysis of the potential catalytic residues of the VV G1L metalloproteinase Kady M Honeychurch1 Chelsea M Byrd2 and Dennis E Hruby 1 2 Address department of Microbiology Oregon State University Corvallis Oregon 97331 USA and 2SIGA Technologies Inc Corvallis Oregon 97333 USA Email Kady M Honeychurch - honeychk@ Chelsea M Byrd - cbyrd@ Dennis E Hruby - dhruby@ Corresponding author Published 27 February 2006 Received 17 January 2006 Accepted 27 February 2006 Virology Journal2006 3 7 doi I743-422X-3-7 This article is available from http content 3 1 7 2006Honeychurch 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 The vaccinia virus G1L open-reading frame is predicted to be a metalloproteinase based upon the presence of a conserved zinc-binding motif. Western blot analysis demonstrates G1L undergoes proteolytic processing during the course of infection although the significance of this event is unknown. In order to determine which amino acid residues are important for G1L activity a plasmid-borne library of G1L constructs containing mutations in and about the active site was created. Transient expression analysis coupled with a trans complementation assay of a conditionally-lethal mutant virus suggest that of the mutants only glutamic acid 120 is non-essential for G1L processing to occur. Findings Vaccinia virus VV is among the largest of the DNA viruses and represents the prototypic member of the Orthopoxvirus genus. It is an enveloped virus and possesses a linear double-stranded genome containing greater than 200 mostly non-overlapping open reading frames. Throughout its life .
