Three-dimensional structure of Theiler murine encephalomyelitis virus (BeAn strain).

Luo, Ming; He, Cun-Heng; Toth, K.S.; Zhang, Carl X.; Lipton, Howard L.

doi:10.1073/pnas.89.6.2409

Cited by 68 publications

(80 citation statements)

References 23 publications

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“…Thus, the already known VP1 structure of Mengo virus could be used as a substitution analogy for a BJC3 VP1 molecular model. In addition, the structural comparison between Mengo virus and TMEV, a well-investigated virus for CNS disease models, showed a similar conformation of loop II (residues 94-112 in TMEV and 90-110 in Mengo virus) on the external surface of the virion [18]. Based on the reported structures for Mengo, molecular modeling analysis by Collaborative Computational Project No.…”

Section: Selection Of Animal Model and Position For Site-directed Mutmentioning

confidence: 99%

Alteration of encephalomyocarditis virus pathogenicity due to a mutation at position 100 of VP1

Zhu

Gong

et al. 2011

Sci. China Life Sci.

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Encephalomyocarditis virus (EMCV) infection leads to many diseases including encephalitis, myocarditis and diabetes in its natural host, the mouse. In this study, we generated four cDNA clones with a point mutation at position 100 of VP1. The amino acids isoleucine, alanine, serine and proline were substituted with threonine in the four different clones of EMCV strain BJC3 by site-specific mutagenesis, and viable viruses were rescued. Although all mutants and wild-type viruses display different plaque morphologies, they replicate comparably in BHK-21 cells. The pathogenicity of the mutated viruses was systematically analyzed to investigate the importance of this amino acid in the viral pathogenicity and disease phenotype of EMCV infection in mice. The results showed that the isoleucine-(T1100I) and proline-mutated viruses (T1100P) exhibited a reduced mortality, lower cerebral virus loads and alleviated brain damage while the viruses with serine (T1100S) and alanine (T1100A) substitutions displayed similar properties as the wild-type virus. These findings indicate that the amino acid at position 100 of VP1 is important for EMCV in vivo infection, and its mutation alters the pathogenicity of viral infection in mice. encephalomyocarditis virus (EMCV), VP1, mutation, pathogenicity Citation:Zhu S, Ge X N, Gong X W, et al. Alteration of encephalomyocarditis virus pathogenicity due to a mutation at position 100 of VP1. Sci China Life Sci, 2011, 54: 535 -543,

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Section: Selection Of Animal Model and Position For Site-directed Mutmentioning

confidence: 99%

Alteration of encephalomyocarditis virus pathogenicity due to a mutation at position 100 of VP1

Zhu

Gong

et al. 2011

Sci. China Life Sci.

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“…Since then, structures of several other picornaviruses have been described (1,34,35,41,48,56,62,(65)(66)(67)84,85,104,112,121,122). The protein shell of the virion is composed of 60 copies of the 4 capsid proteins, VP1, VP2, VP3, and VP4, that are arranged on an icosahedral surface.…”

Section: The Virionmentioning

confidence: 99%

Poliovirus Cell Entry: Common Structural Themes in Viral Cell Entry Pathways

Hogle

2002

Annu. Rev. Microbiol.

311

305

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Structural studies of polio-and closely related viruses have provided a series of snapshots along their cell entry pathways. Based on the structures and related kinetic, biochemical, and genetic studies, we have proposed a model for the cell entry pathway for polio-and closely related viruses. In this model a maturation cleavage of a capsid protein precursor locks the virus in a metastable state, and the receptor acts like a transition-state catalyst to overcome an energy barrier and release the mature virion from the metastable state. This initiates a series of conformational changes that allow the virus to attach to membranes, form a pore, and finally release its RNA genome into the cytoplasm. This model has striking parallels with emerging models for the maturation and cell entry of more complex enveloped viruses such as influenza virus and HIV.

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“…The 3-dimensional structures of several poliovirus and of several related picornaviruses have been determined at near atomic resolution by X-ray crystallographic methods (Hogle et al, 1985;Rossmann et al, 1985;Luo et al, 1987Luo et al, , 1992Acharya et al, 1988;Grant et al, 1992). These studies have shown that the major capsid proteins VPl, VP2, and VP3 share a common "core" structure, composed of a wedge-shaped 8-stranded antiparallel @-barrel, but have dissimilar connecting loops, and long dissimilar extensions at their amino-termini.…”

mentioning

confidence: 99%

Role and mechanism of the maturation cleavage of VP0 in poliovirus assembly: Structure of the empty capsid assembly intermediate at 2.9 Å resolution

et al. 1994

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The crystal structure of the Pl/Mahoney poliovirus empty capsid has been determined at 2.9 A resolution. The empty capsids differ from mature virions in that they lack the viral RNA and have yet to undergo a stabilizing maturation cleavage of VPO to yield the mature capsid proteins VP4 and VP2. The outer surface and the bulk of the protein shell are very similar to those of the mature virion. The major differences between the 2 structures are focused in a network formed by the N-terminal extensions of the capsid proteins on the inner surface of the shell. In the empty capsids, the entire N-terminal extension of V P l , as well as portions corresponding to VP4 and the N-terminal extension of VP2, are disordered, and many stabilizing interactions that are present in the mature virion are missing. In the empty capsid, the VPO scissile bond is located some 20 A away from the positions in the mature virion of the termini generated by VPO cleavage. The scissile bond is located on the rim of a trefoilshaped depression in the inner surface of the shell that is highly reminiscent of an RNA binding site in bean pod mottle virus. The structure suggests plausible (and ultimately testable) models for the initiation of encapsidation, for the RNA-dependent autocatalytic cleavage of VPO, and for the role of the cleavage in establishing the ordered N-terminal network and in generating stable virions.Keywords: capsid proteins; empty capsid; encapsidation initiation; maturation cleavage; poliovirus; viral RNA; virion stability Poliovirus is a member of the picornavirus family. This family includes a large number of related small spherical viruses consisting entirely of a protein shell (approximately 300 A in diameter) and a single-stranded RNA genome (-7,500 nucleotides) of positive polarity. The family is subdivided into several genera, including the enteroviruses (polioviruses, coxsackieviruses,

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Three-dimensional structure of Theiler murine encephalomyelitis virus (BeAn strain).

Cited by 68 publications

References 23 publications

Alteration of encephalomyocarditis virus pathogenicity due to a mutation at position 100 of VP1

Alteration of encephalomyocarditis virus pathogenicity due to a mutation at position 100 of VP1

Poliovirus Cell Entry: Common Structural Themes in Viral Cell Entry Pathways

Role and mechanism of the maturation cleavage of VP0 in poliovirus assembly: Structure of the empty capsid assembly intermediate at 2.9 Å resolution

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