Open AccessUnderstanding and targeting a novel plant viral proteinase/substrate interaction. Final report, July 1, 1989--June 30, 1995
Author(s) -
William G. Dougherty
Publication year - 1995
Language(s) - English
Resource type - Reports
DOI - 10.2172/108096
Subject(s) - tobacco etch virus , function (biology) , biology , computational biology , recombinant dna , similarity (geometry) , fusion protein , virus , virology , microbiology and biotechnology , biochemistry , plant virus , computer science , artificial intelligence , potyvirus , gene , image (mathematics)
The past 3 years of funding have focused our efforts on trying to understand the molecular basis of a unique substrate interaction displayed by a viral proteinase. We have made good progress and during this funding period we have made four contributions to the scientific literature and have developed the application of the proteinase in the expression and purification of recombinant fusion proteins. A comprehensive review of virus-encoded proteinases, written during the funding period, emphazing the tremendous similarity of viral proteinases with their cellular counterparts and at the same time detail the unique characteristics which permit them to function in a cellular environment. The focus of the research effort was the tobacco etch virus (TEV) 27kDa NIa proteinase