Abstract:
Viruses maintain high structural stability during the extracellular portions of their replicative cycles, yet are significantly dynamic during other stages in their life cycle. Despite the extensive studies that have characterized the various structural proteins found within the capsid layers of reovirus, little is still known with regards to the proteins within it and to the overall dynamics of the virus particle. This study serves to further characterize the interior particle protein [lambda]3, the RNA dependent RNA polymerase, and to offer evidence that reovirus has the capacity to undergo extensive conformational changes. In addition, the environmentally safe compound Vertrel XF was identified as a suitable substitute for the organic solvent Freon 113, extensively used in virus purification. Factors affecting protein configuration, specifically of the RdRp, can have detrimental effects on transcription. To examine such factors, temperature-sensitive mutants 'tsD'357 and 'tsG'453, along with reassortant analysis were used. To investigate the dynamic nature of the virus, purified virions and cores were analysed by MALDI QqTOF mass spectrometry. (Abstract shortened by UMI.)
