This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Red clover necrotic mosaic virus is a small, icosahedral plant virus (Tombusviridae family) with a single-stranded RNA genome. RCNMV virions were analyzed by cryo-electron microscopy (cryoEM) and three-dimensional reconstruction at 8 resolution. The virion capsids have prominent protrusions; inside the capsid there is an inner cage formed by complexes of genomic RNA and amino terminal portion of the coat protein. Separate reconstructions were obtained at 12 and 16 resolution, respectively, for virion samples that had Ca2+ alone or both Mg2+ and Ca2+ divalent cations selectively extracted. Virions treated in this way exhibited dramatic conformational changes, as obtained from NMFF, in both capsid and inner cage, though the particle diameters remained unchanged. Removal of Ca2+ ions alone appears to trigger movement and rotation of the S and P domains at the quasi 3-fold axis of symmetry. Additional removal of Mg2+ led to the formation of 11-13 diameter channels that extend through the virion shell at the quasi 3-fold axis of symmetry and noticeably alter the inner cage conformation. Despite their relatively small size, these channels are sufficiently large to allow RNA to pass through the protein capsid shell. Structural and infectivity studies suggest the divalent cation induced dynamics may be involved in viral reorganization, which renders the viral RNA accessible for translation early in infection.
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| Arthur, Evan J; King, John T; Kubarych, Kevin J et al. (2014) Heterogeneous preferential solvation of water and trifluoroethanol in homologous lysozymes. J Phys Chem B 118:8118-27 |
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