U.S. Army Medical Research Institute of Infectious Diseases
During discovery and testing of the F1-V fusion protein, proposed for development as the new plague vaccine antigen, the purified protein was observed to form soluble aggregates under certain conditions. Dr. Powell and colleagues used the DAWN EOS and Optilab DSP to characterize the molecular structures of pure F1-V and its constituent subunits, the Yersinia pestis F1 and V proteins. Their investigation showed that aggregation was caused by the F1 subcomponent which forms soluble aggregates 10-times larger than the fusion protein under physiological temperature and salt. SEC-MALS studies also showed that the F1-V fusion protein structure is more stable to cold temperature, high salt, or reducing conditions than the individual subcomponent proteins.
Powell, B. S.; Andrews, G. P.; Enama, J. T.; Jendrek, S.; Bolt, C.; Worsham, P.; Pullen, J. K.; Ribot, W.; Hines, H.; Smith, L.; Heath, D. G.; Adamovicz, J. J. Biotechnology Progress 2005, 21, 1490-1510. DOI: 10.1021/bp050098r