One more probable structural transition in potato virus X virions and a revised model of the virus coat protein structure.
We found that a 2-h incubation of potato virus X (PVX) virions in 10 mM Tris-HCl buffer pH 7.5 at -20 degrees C results in a strong but reversible drop in virion stability. Under these conditions, the PVX virions are completely disrupted by low (starting from 50 mM) concentrations of LiCl and CaCl(2) but not of NaCl. Incubation of PVX samples with 0.05-2 M LiCl at +4 degrees C did not result in virion disassembly and the virions were not disrupted upon incubation at -20 degrees C in 10 mM Tris-HCl buffer pH 7.5 without LiCl. We suggest that a 2-h incubation of the PVX virions at -20 degrees C in 10 mM Tris-HCl pH 7.5 results in a structural transition in the virus particles. A revised model of the three-dimensional organization of coat protein subunits in the PVX virions is proposed. This two-domain model explains better the high plasticity of the PVX CP structure.
D002021:Buffers; D002152:Calorimetry, Differential Scanning; D036022:Capsid Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D002942:Circular Dichroism; D005453:Fluorescence; D006851:Hydrochloric Acid / Q000494:pharmacology; D008956:Models, Chemical; D017863:Potexvirus / Q000737:chemistry* / Q000378:metabolism; D014771:Virion / Q000737:chemistry* / Q000378:metabolism; D014773:Virology / Q000379:methods; D019065:Virus Assembly
D002021:Buffers; D036022:Capsid Proteins; C058750:coat protein, Potato virus X; D006851:Hydrochloric Acid