1TME

THREE-DIMENSIONAL STRUCTURE OF THEILER VIRUS

Summary for 1TME

• Entry DOI: 10.2210/pdb1tme/pdb
• Descriptor: THEILER'S MURINE ENCEPHALOMYELITIS VIRUS (SUBUNIT VP1), THEILER'S MURINE ENCEPHALOMYELITIS VIRUS (SUBUNIT VP2), THEILER'S MURINE ENCEPHALOMYELITIS VIRUS (SUBUNIT VP3), ... (5 entities in total)
• Functional Keywords: virus, icosahedral virus
• Biological source: Theiler's encephalomyelitis virus (STRAIN DA); More
• Cellular location: Protein VP2: Virion. Protein VP3: Virion. Protein VP1: Virion. Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Protein 3B: Virion (Potential). Picornain 3C: Host cytoplasm (Potential). RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential): P13899 P13899 P13899 P13899
• Total number of polymer chains: 4
• Total formula weight: 92861.66

Authors

Grant, R.A.,Filman, D.J.,Hogle, J.M. (deposition date: 1992-01-30, release date: 1994-01-31, Last modification date: 2024-02-14)

Primary citation

Grant, R.A.,Filman, D.J.,Fujinami, R.S.,Icenogle, J.P.,Hogle, J.M.
Three-dimensional structure of Theiler virus.
Proc.Natl.Acad.Sci.USA, 89:2061-2065, 1992

PubMed Abstract: Theiler murine encephalomyelitis virus strains are categorized into two groups, a neurovirulent group that rapidly kills the host, and a demyelinating group that causes a generally nonlethal infection of motor neurons followed by a persistent infection of the white matter with demyelinating lesions similar to those found in multiple sclerosis. The three-dimensional structure of the DA strain, a member of the demyelinating group, has been determined at 2.8 A resolution. As in other picornaviruses, the icosahedral capsid is formed by the packing of wedge-shaped eight-stranded antiparallel beta barrels. The surface of Theiler virus has large star-shaped plateaus at the fivefold axes and broad depressions spanning the twofold axes. Several unusual structural features are clustered near one edge of the depression. These include two finger-like loops projecting from the surface (one formed by residues 78-85 of VP1, and the other formed by residues 56-65 of VP3) and a third loop containing three cysteines (residues 87, 89, and 91 of VP3), which appear to be covalently modified. Most of the sequence differences between the demyelinating and neurovirulent groups that could play a role in determining pathogenesis map to the surface of the star-shaped plateau. The distribution of these sequence differences on the surface of the virion is consistent with models in which the differences in the pathogenesis of the two groups of Theiler viruses are the result of differences in immunological or receptor-mediated recognition processes.

PubMed: 1549565
DOI: 10.1073/pnas.89.6.2061

Experimental method

X-RAY DIFFRACTION (2.8 Å)