4.7 Article

Crystal Structure of the Coat Protein of the Flexible Filamentous Papaya Mosaic Virus

Journal

JOURNAL OF MOLECULAR BIOLOGY
Volume 422, Issue 2, Pages 263-273

Publisher

ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2012.05.032

Keywords

Plant virus; Alphaflexiviridae; protein structure; cryo-EM; X-ray crystallography

Funding

  1. BNLLDRD [10-016, NIHGM74985]
  2. Natural Sciences and Engineering Research Council of Canada [227041]
  3. Office of Biological and Environmental Research and the Office of Basic Energy Sciences of the U.S. Department of Energy
  4. National Center for Research Resources [P41RR012408]
  5. National Institute of General Medical Sciences of the National Institutes of Health [P41GM103473]

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Papaya mosaic virus (PapMV) is a filamentous plant virus that belongs to the Alphaflexiviridae family. Flexible filamentous viruses have defied more than two decades of effort in fiber diffraction, and no high-resolution structure is available for any member of the Alphaflexiviridae family. Here, we report our structural characterization of PapMV by X-ray crystallography and cryoelectron microscopy three-dimensional reconstruction. We found that PapMV is 135 angstrom in diameter with a helical symmetry of similar to 10 subunits per turn. Crystal structure of the C-terminal truncated PapMV coat protein (CP) reveals a novel all-helix fold with seven alpha-helices. Thus, the PapMVCP structure is different from the four-helix-bundle fold of tobacco mosaic virus in which helix bundling dominates the subunit interface in tobacco mosaic virus and conveys rigidity to the rod virus. PapMV CP was crystallized as an asymmetrical dimer in which one protein lassoes the other by the N-terminal peptide. Mutation of residues critical to the inter-subunit lasso interaction abolishes CP polymerization. The crystal structure suggests that PapMV may polymerize via the consecutive N-terminal loop lassoing mechanism. The structure of PapMV will be useful for rational design and engineering of the PapMV nanoparticles into innovative vaccines. (C) 2012 Elsevier Ltd. All rights reserved.

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