Tobacco mosaic virus particle structure and the initiation of disassembly.
The structure of an intact tobacco mosaic virus (TMV) particle was determined at 2.9 A resolution using fibre diffraction methods. All residues of the coat protein and the three nucleotides of RNA that are bound to each protein subunit were visible in the electron density map. Examination of the structures of TMV, cucumber green mottle mosaic virus and ribgrass mosaic virus, and site-directed mutagenesis experiments in which carboxylate groups were changed to the corresponding amides, showed that initial stages of disassembly are driven by complex electrostatic interactions involving at least seven carboxylate side-chains and a phosphate group. The locations of these interactions can drift during evolution, allowing the viruses to evade plant defensive responses that depend on recognition of the viral coat protein surface.
Stubbs
G
G
Department of Molecular Biology, Vanderbilt University, Nashville, TN 57235, USA.
D003198:Computer Simulation; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D010947:Plants, Toxic; D014026:Nicotiana / Q000821:virology; D014027:Tobacco Mosaic Virus / Q000235:genetics / Q000502:physiology / Q000648:ultrastructure*; D014771:Virion / Q000235:genetics / Q000502:physiology / Q000648:ultrastructure*; D019065:Virus Assembly / Q000235:genetics; D014961:X-Ray Diffraction