Characterizing Virus Structure and Binding by Calorimetry

The self assembly of viral proteins and nucleic acids to form stable particles, and the mechanisms by which viruses bind to and penetrate host cells, represent two key issues to understanding the basis of viral infection. Both these issues can be studied using calorimetry. The thermal stability of virus coat proteins in solution, compared with the stability of the corresponding highly structured viral protein shell, can be most effectively characterized by differential scanning calorimetry (DSC), whereas fundamental information about the molecular interactions driving virus/cell binding processes can be obtained by measuring the heat evolved or absorbed during binding using isothermal titration calorimetry (ITC). This note reviews applications of DSC and ITC for studying the stability of virus particles and their binding to cells, as well as for the identification of viruses. Although the literature dealing with the thermodynamics of virus particle assembly and stability is not extensive, this is likely to change given increasing interest in the use of calorimetry for identifying viruses and for understanding viral structure and virulence.