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Published October 1, 2008 | Published
Journal Article Open

Structure of Flexible Filamentous Plant Viruses

Abstract

Flexible filamentous viruses make up a large fraction of the known plant viruses, but by comparison with other viruses, very little is known about their structures. We have used fiber diffraction, cryo-electron microscopy, and scanning transmission electron microscopy to determine the symmetry of a potyvirus, soybean mosaic virus, to confirm the symmetry of a potexvirus, potato virus X, and to determine low resolution structures of both viruses. We conclude that these viruses and, by implication, most or all flexible filamentous plant viruses share a common coat protein fold and helical symmetry, with slightly less than 9 subunits per helical turn.

Additional Information

Copyright © 2008, American Society for Microbiology. Received 29 April 2008/ Accepted 17 July 2008. Published ahead of print on 30 July 2008. We thank the staff of BioCAT for help with fiber diffraction data collection, David Friedman and Dawn Overstreet of the Vanderbilt University Mass Spectrometry Research Center for the mass spectrometry data, Martha Simon for help with the STEM data acquisition, Ian McCullough for help with PVX purification, Hayden Box for help with molecular graphics, and Ed Egelman for help with IHRSR. IHRSR computations were carried out using the resources of the Advanced Computing Center for Research and Education at Vanderbilt University. This work was supported by NSF grant MCB-0235653 to G.S. and USDA-NRI grant 2006-01854 to S.A.G. Fiber diffraction data analysis software was from FiberNet (www.fiberdiffraction.org), supported by NSF grant MCB-0234001. Use of the Advanced Photon Source was supported by the U.S. Department of Energy under contract W-31-109-ENG-38. BioCAT is an NIH-supported Research Center (RR-08630). The content is solely the responsibility of the authors and does not necessarily reflect the official views of the National Center for Research Resources or the NIH.

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