title: Single-particle cryo-electron microscopy of Rift Valley fever virus.
abstract: Rift Valley fever virus (RVFV; Bunyaviridae; Phlebovirus) is an emerging human and veterinary pathogen causing acute hepatitis in ruminants and has the potential to cause hemorrhagic fever in humans. We report a three-dimensional reconstruction of RVFV vaccine strain MP-12 (RVFV MP-12) by cryo-electron microcopy using icosahedral symmetry of individual virions. Although the genomic core of RVFV MP-12 is apparently poorly ordered, the glycoproteins on the virus surface are highly symmetric and arranged on a T=12 icosahedral lattice. Our RVFV MP-12 structure allowed clear identification of inter-capsomer contacts and definition of possible glycoprotein arrangements within capsomers. This structure provides a detailed model for phleboviruses, opens new avenues for high-resolution structural studies of the bunyavirus family, and aids the design of antiviral diagnostics and effective subunit vaccines.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555-0647, USA.
authors.forename: Michael B
authors.initials: MB
authors.lastname: Sherman
authors.forename: Alexander N
authors.initials: AN
authors.lastname: Freiberg
authors.forename: Michael R
authors.initials: MR
authors.lastname: Holbrook
authors.forename: Stanley J
authors.initials: SJ
authors.lastname: Watowich
mesh_terms: D020285:Cryoelectron Microscopy / Q000379:methods*; D006023:Glycoproteins / Q000378:metabolism / Q000648:ultrastructure; D007091:Image Processing, Computer-Assisted; D008563:Membrane Lipids / Q000378:metabolism; D012296:Rift Valley fever virus / Q000648:ultrastructure*; D014759:Viral Envelope Proteins / Q000378:metabolism / Q000648:ultrastructure
chemical_list: D006023:Glycoproteins; D008563:Membrane Lipids; D014759:Viral Envelope Proteins; C050629:viral envelope lipids