Heating-induced transition of Potyvirus Potato Virus A coat protein into β-structure

J Biomol Struct Dyn. 2016;34(2):250-8. doi: 10.1080/07391102.2015.1022604. Epub 2015 Apr 8.

Abstract

In our previous communication, we have reported that virions of plant Potyvirus Potato Virus A (PVA) have a peculiar structure characterized by high content of disordered regions in intravirus coat protein (CP). In this report, we describe unusual properties of the PVA CP. With the help of a number of physicochemical methods, we have observed that the PVA CP just released from the virions by heating at 60-70 °C undergoes association into oligomers and transition to β- (and even cross-β-) conformation. Transition to β-structure on heating has been recently reported for a number of viral and non-viral proteins. The PVA CP isolated by LiCl method was also transformed into cross-β-structure on heating to 60 °C. Using the algorithms for protein aggregation prediction, we found that the aggregation-prone segments should be located in the central region of a PVA CP molecule. Possibly this transition mimics some functions of PVA CP in the virus life cycle in infected plants.

Keywords: PVA coat protein; Potato Virus A; amyloid structures; disordered and β-structures; heating-induced transition.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Capsid Proteins / chemistry*
  • Hot Temperature*
  • Potyvirus / chemistry*
  • Protein Structure, Secondary
  • Spectrum Analysis, Raman

Substances

  • Capsid Proteins