Design and testing for a nontagged F1-V fusion protein as vaccine antigen against bubonic and pneumonic plague

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