Comparative study of structural stabylity of potato virus X coat protein molecules in solution and in the virus particles

• Published in: Molekuliarnaia biologiia Vol. 41; no. 4; p. 697
• Main Authors: Nemykh, M A, Novikov, V K, Arutiunian, A M, Kalmykov, P V, Drachev, V A, Dobrov, E N
• Format: Journal Article
• Language: Russian
• Published: Russia (Federation) 01-07-2007
• Subjects: Calorimetry, Differential Scanning; Capsid Proteins - chemistry; Protein Conformation; Protein Subunits; Solutions; Temperature; Virion - chemistry
• ISSN: 0026-8984

With help of several optical methods and differential scanning calorimetry we studied the structure and stability of molecules of coat protein (CP) of filamentous of potato virus X (PVX) in free state and in the virions. According to the results of all these methods, at room temperature (25 degrees C) free PVX CP subunits possess some fixed tertiary structure but this structure is highly unstable and is completely disrupted at temperatures as low as 35 degrees C. The free PVX CP tertiary structure was also disrupted by very low sodium dodecylsulfate and cetyltrimetylammonium bromide concentrations: 3 to 5 moleculs of the surfactants per the CP molecule were sufficient to induce its total disruption. At the same time, these treatments did not result in any changes in the PVX CP secondary structure. Incorporation of the CP subunits into the PVX virions resulted in a strong increase in their stability to effects of increased temperatures and surfactants. This combination of highly labile tertiary structure and rather stable secondary structure of free PVX CP subunits may represent a structural basis for recently observed capacity of the PVX CP moleculs to assume two different functional states in the virion.