AFM Study of Potato Virus X Disassembly Induced by Movement Protein

• Published in: Journal of molecular biology 2003-09, Vol.332 (2), p.321-325
• Main Authors: Kiselyova, Olga I., Yaminsky, Igor V., Karpova, Olga V., Rodionova, Nina P., Kozlovsky, Stanislav V., Arkhipenko, Marina V., Atabekov, Joseph G.
• Format: Article
• Language: English
• Subjects: atomic force microscopy; Capsid Proteins - chemistry; Capsid Proteins - metabolism; Capsid Proteins - ultrastructure; linear destabilization; Macromolecular Substances; Microscopy, Atomic Force; movement protein; Plant Viral Movement Proteins; potato virus X; Potexvirus - chemistry; Potexvirus - metabolism; Protein Binding; Protein Conformation; RNA, Viral; Viral Proteins - chemistry; Viral Proteins - metabolism; Viral Proteins - ultrastructure; Virion - genetics; Virion - metabolism
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1016/S0022-2836(03)00835-0

Recently we have reported that a selective binding of potato virus X (PVX)-coded movement protein (termed TGBp1 MP) to one end of a polar coat protein (CP) helix converted viral RNA into a translatable form and induced a linear destabilization of the whole helical particle. Here, the native PVX virions, RNase-treated (PVX RNA-DEG) helical particles lacking intact RNA and their complexes with TGBp1 (TGBp1–PVX and TGBp1–PVX RNA-DEG), were examined by atomic force microscopy (AFM). When complexes of the TGBp1 MP with PVX were examined by means of AFM in liquid, no structural reorganization of PVX particles was observed. By contrast, the products of TGBp1-dependent PVX degradation termed “beads-on-string” were formed under conditions of AFM in air. The AFM images of PVX RNA-DEG were indistinguishable from images of native PVX particles; however, the TGBp1-dependent disassembly of the CP-helix was triggered when the TGBp1–PVX RNA-DEG complexes were examined by AFM, regardless of the conditions used (in air or in liquid). Our data supported the idea that binding of TGBp1 to one end of the PVX CP-helix induced linear destabilization of the whole helical particle, which may lead to its disassembly under conditions of AFM.