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Journal of Virology, November 2008, p. 10341-10348, Vol. 82, No. 21
0022-538X/08/$08.00+0     doi:10.1128/JVI.01191-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Three-Dimensional Organization of Rift Valley Fever Virus Revealed by Cryoelectron Tomography{triangledown}

Alexander N. Freiberg,1,{dagger} Michael B. Sherman,2,3,{dagger} Marc C. Morais,2,3 Michael R. Holbrook,1,4 and Stanley J. Watowich2,3*

Department of Pathology, Center for Biodefense and Emerging Infectious Diseases,1 Department of Biochemistry and Molecular Biology,2 Sealy Center for Structural Biology and Molecular Biophysics,3 Institute for Human Infections and Immunity, University of Texas Medical Branch, Galveston, Texas 775554

Received 8 June 2008/ Accepted 5 August 2008

Rift Valley fever virus (RVFV) is a member of the Bunyaviridae virus family (genus Phlebovirus) and is considered to be one of the most important pathogens in Africa, causing viral zoonoses in livestock and humans. Here, we report the characterization of the three-dimensional structural organization of RVFV vaccine strain MP-12 by cryoelectron tomography. Vitrified-hydrated virions were found to be spherical, with an average diameter of 100 nm. The virus glycoproteins formed cylindrical hollow spikes that clustered into distinct capsomeres. In contrast to previous assertions that RVFV is pleomorphic, the structure of RVFV MP-12 was found to be highly ordered. The three-dimensional map was resolved to a resolution of 6.1 nm, and capsomeres were observed to be arranged on the virus surface in an icosahedral lattice with clear T=12 quasisymmetry. All icosahedral symmetry axes were visible in self-rotation functions calculated using the Fourier transform of the RVFV MP-12 tomogram. To the best of our knowledge, a triangulation number of 12 had previously been reported only for Uukuniemi virus, a bunyavirus also within the Phlebovirus genus. The results presented in this study demonstrate that RVFV MP-12 possesses T=12 icosahedral symmetry and suggest that other members of the Phlebovirus genus, as well as of the Bunyaviridae family, may adopt icosahedral symmetry. Knowledge of the virus architecture may provide a structural template to develop vaccines and diagnostics, since no effective anti-RVFV treatments are available for human use.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555-0647. Phone: (409) 747-4749. Fax: (409) 747-4745. E-mail: watowich{at}xray.utmb.edu

{triangledown} Published ahead of print on 20 August 2008.

{dagger} A.N.F. and M.B.S. contributed equally to this work.

Journal of Virology, November 2008, p. 10341-10348, Vol. 82, No. 21
0022-538X/08/$08.00+0     doi:10.1128/JVI.01191-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Huiskonen, J. T., Overby, A. K., Weber, F., Grunewald, K. (2009). Electron Cryo-Microscopy and Single-Particle Averaging of Rift Valley Fever Virus: Evidence for GN-GC Glycoprotein Heterodimers. J. Virol. 83: 3762-3769 [Abstract] [Full Text]  


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