Partially disordered structure in intravirus coat protein of potyvirus potato virus A

• Published in: PloS one Vol. 8; no. 7; p. e67830
• Main Authors: Ksenofontov, Alexander L, Paalme, Viiu, Arutyunyan, Alexander M, Semenyuk, Pavel I, Fedorova, Natalia V, Rumvolt, Reet, Baratova, Ludmila A, Järvekülg, Lilian, Dobrov, Eugeny N
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 03.07.2013; Public Library of Science (PLoS)
• Subjects: Biology; Calorimetry; Calorimetry, Differential Scanning; Cancer; Capsid Proteins - chemistry; Chemistry; Circular dichroism; Coat protein; Dichroism; Differential scanning calorimetry; Fluorescence; Leaves; Medical research; Medicine; Melting; Methods; Microscopy; Molecular weight; Physicochemical properties; Plant viruses; Potatoes; Potyvirus - chemistry; Potyvirus - isolation & purification; Potyvirus - ultrastructure; Protein Conformation; Protein Folding; Protein structure; Proteins; Spectrum Analysis; Studies; Thermal stability; Thermodynamics; Tobacco; Ultraviolet absorption; Virion - chemistry; Virion - isolation & purification; Virion - ultrastructure; Virions; Virology; Viruses; Estonia; Russia
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0067830

Potyviruses represent the most biologically successful group of plant viruses, but to our knowledge, this work is the first detailed study of physicochemical characteristics of potyvirus virions. We measured the UV absorption, far and near UV circular dichroism spectra, intrinsic fluorescence spectra, and differential scanning calorimetry (DSC) melting curves of intact particles of a potato virus A (PVA). PVA virions proved to have a peculiar combination of physicochemical properties. The intravirus coat protein (CP) subunits were shown to contain an unusually high fraction of disordered structures, whereas PVA virions had an almost normal thermal stability. Upon heating from 20 °C to 55 °C, the fraction of disordered structures in the intravirus CP further increased, while PVA virions remained intact at up to 55 °C, after which their disruption (and DSC melting) started. We suggest that the structure of PVA virions below 55 °C is stabilized by interactions between the remaining structured segments of intravirus CP. It is not improbable that the biological efficiency of PVA relies on the disordered structure of intravirus CP.