Assessing the stability of assembled filamentous phage coat protein P8

Abstract

Assembly of viral protein coats is crucial to the protection of internal genetic cargo and is necessary for proper infection. Understanding the conditions for maintaining these supramolecular assemblies is of value for engineering-effective virus-based materials and related technologies. In this study, we examine the stability of the filamentous bacteriophage, fd-tet, in a variety of solvent and temperature conditions. On the basis of these results, we advise amenable reaction environments for modification of fd-tet. In particular, assessment of the temperature stability indicates that practical use of these viruses as reaction substrates is best performed at moderate temperatures, since loss in infectivity was found to occur within only 1-h incubation over 37°C. In addition, these findings reveal additional loss of infectivity after exposure to conditions near pH 4.5 which may be attributable to changes in the effective charge of the p8 major coat protein.

Keywords::

• virus
• assembly
• stability
• infectivity
• protein

Acknowledgements

This work was supported by the Priority Research Centers Program through the National Research Foundation of Korea funded by the Ministry of Education (2012R1A6A1029029) and by the research fund of Hanyang University (HY-2011-N).