Advisor(s) - Committee Chair
Claire Rinehart, Frank Toman, Valgene Dunham
Department of Biology
Master of Science
Southern Bean Mosaic Virus (SBMV) codes for a large polyprotein which is subsequently cleaved into smaller functional proteins. A virally encoded protease is suspected of mediating the cleavages. SBMV, picornaviruses and picornavirus-like viruses appear to have similar genomic organizations, which would place the protease region of the genome between the VPg and RNA dependen,, RNA polymerase regions. Protein sequence comparisons revealed homology between SBMV putative protease and the known proteases from foot and mouth disease virus, encephlamyocarditis virus, poliovirus, and cowpea mosaic virus. Experimental evidence provides little information on the exact location of the protease; however, protein sequence analysis suggests that the protease is indeed located between the VPg and RNA polymerase regions of SBMV.
Comparisons of known cleavages sites to SBMV suggests that the QS amino acid pairs, at postions 539-540 and 664-665, are the most likely site for cleavage. The QS pair is present on the surface, in a region with high flexibility, which is in a turn. This evidence, although circumstantial, is supported by the deletion of the C-terminal end of the protein.
Biology | Life Sciences
Shannon, Timothy, "Evidence for the Location of Aviral Protease & Protease Cleavage Sites in the 105 Kilodalton Protein of Southern Bean Mosaic Virus" (1992). Masters Theses & Specialist Projects. Paper 2846.