Identification and Molecular Characterization of the RNA Polymerase-Binding Motif of Infectious Bursal Disease Virus Inner Capsid Protein VP3

Maraver, Antonio; Clemente, Roberto; Rodrı́guez, José F.; Lombardo, Eleuterio

doi:10.1128/jvi.77.4.2459-2468.2003

Cited by 44 publications

(50 citation statements)

References 27 publications

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“…The presence of M3 at the IBDV assembly factories might hamper the correct incorporation of the VP1 polypeptide into the newly formed particles. This hypothesis is supported by the previous observation that treatment of IBDV-infected cells with Trojan peptides containing the VP1-binding motif found in VP3 causes a significant reduction in infective-virus production (6).…”

supporting

confidence: 76%

“…This dramatic alteration in the M3 subcellular distribution strongly suggests that it participates in the assembly of the virus progeny. Previous studies have shown that although M3 is unable to form complexes with the virus-encoded RNA-dependent RNA polymerase (6), it retains the ability to oligomerize (7) and to interact with the virus genome (4). The presence of M3 at the IBDV assembly factories might hamper the correct incorporation of the VP1 polypeptide into the newly formed particles.…”

mentioning

confidence: 99%

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Intracellular Interference of Infectious Bursal Disease Virus

González

Rodrı́guez

Abaitua

2005

J Virol

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A search for dominant-negative mutant polypeptides hampering infectious bursal disease virus (IBDV) replication has been undertaken. We have found that expression of a mutant version of the VP3 structural polypeptide known as VP3/M3, partially lacking the domain responsible for the interaction with the virusencoded RNA polymerase, efficiently interferes with the IBDV replication cycle. Transformed cells stably expressing VP3/M3 show a significant reduction (up to 96%) in their ability to support IBDV growth. Our findings provide a new tool for the characterization of the IBDV replication cycle and might facilitate the generation of genetically modified chicken lines with a reduced susceptibility to IBDV infection.

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confidence: 76%

mentioning

confidence: 99%

Intracellular Interference of Infectious Bursal Disease Virus

González

Rodrı́guez

Abaitua

2005

J Virol

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“…VP2 and a variable amount of pVP2 assemble into 260 trimers to form the capsid structural units (accounting for Ϸ38 MDa); VP3 is a multifunctional protein that interacts with itself (14), pVP2 (11), VP1 (15,16), and with the dsRNA to make ribonucleoprotein complexes (17), a unique feature among dsRNA viruses.…”

mentioning

confidence: 99%

Infectious bursal disease virus is an icosahedral polyploid dsRNA virus

Luque¹,

Rivas

Alfonso

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

115

102

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Viruses are a paradigm of the economy of genome resources, reflected in their multiplication strategy and for their own structure. Although there is enormous structural diversity, the viral genome is always enclosed within a proteinaceous coat, and most virus species are haploid; the only exception to this rule are the highly pleomorphic enveloped viruses. We performed an in-depth characterization of infectious bursal disease virus (IBDV), a nonenveloped icosahedral dsRNA virus with a bisegmented genome. Up to 6 natural populations can be purified, which share a similar protein composition but show higher sedimentation coefficients as particle density increases. Stoichiometry analysis of their genome indicated that these biophysical differences correlate with the copy number of dsRNA segments inside the viral capsid. This is a demonstration of a functional polyploid icosahedral dsRNA virus. We show that IBDV particles with greater genome copy number have higher infectivity rates. Our results show an unprecedented replicative strategy for dsRNA viruses and suggest that birnaviruses are living viral entities encompassing numerous functional and structural characteristics of positive and negative ssRNA viruses.cargo volume ͉ IBDV ͉ icosahedral dsRNA viruses ͉ life cycle ͉ viral polyploidy

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“…The VP3 C terminus, which also participates in VP1 incorporation into the capsid, serves as a transcriptional activator (22) because it removes the inherent structural blockade of RNA polymerase activity. In addition, the VP3 oligomerization domain maps within the 42 C-terminal residues of the polypeptide (23). Finally, VP3 is also an RNA-binding protein associated with the dsRNA genome (34,45).…”

Section: Discussionmentioning

confidence: 99%

“…The released C-terminal segments remain associated with the capsid (15) and, by promoting the disruption of host cell membranes, appear to be involved in the entry mechanism (16,17). VP3 is a multifunctional protein that interacts with itself (18,19), pVP2 (20,21), VP1 (22)(23)(24), and the dsRNA (25,26).…”

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confidence: 99%

Electrostatic Interactions between Capsid and Scaffolding Proteins Mediate the Structural Polymorphism of a Double-stranded RNA Virus

Saugar

Irigoyen

Luque

et al. 2010

Journal of Biological Chemistry

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Capsid proteins that adopt distinct conformations constitute a paradigm of the structural polymorphism of macromolecular assemblies. We show the molecular basis of the flexibility mechanism of VP2, the capsid protein of the double-stranded RNA virus infectious bursal disease virus. The initial assembly, a procapsid-like structure, is built by the protein precursor pVP2 and requires VP3, the other infectious bursal disease virus major structural protein, which acts as a scaffold. The pVP2 C-terminal region, which is proteolyzed during virus maturation, contains an amphipathic ␣-helix that acts as a molecular switch. In the absence of VP3, efficient virus-like particle assembly occurs when the structural unit is a VP2-based chimeric protein with an N-terminal-fused His 6 tag. The His tag has a positively charged N terminus and a negatively charged C terminus, both important for virion-like structure assembly. The charge distributions of the VP3 C terminus and His tag are similar. We tested whether the His tag emulates the role of VP3 and found that the presence of a VP3 C-terminal peptide in VP2-based chimeric proteins resulted in the assembly of virus-like particles. We analyzed the electrostatic interactions between these two charged morphogenetic peptides, in which a single residue was mutated to impede the predicted interaction, followed by a compensatory double mutation to rescue electrostatic interactions. The effects of these mutations were monitored by following the virus-like and/or virus-related assemblies. Our results suggest that the basic face of the pVP2 amphipathic ␣-helix interacts with the acidic region of the VP3 C terminus and that this interaction is essential for VP2 acquisition of competent conformations for capsid assembly.

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Identification and Molecular Characterization of the RNA Polymerase-Binding Motif of Infectious Bursal Disease Virus Inner Capsid Protein VP3

Abstract: Infectious bursal disease virus (IBDV), a member of the

Cited by 44 publications

References 27 publications

Intracellular Interference of Infectious Bursal Disease Virus

Intracellular Interference of Infectious Bursal Disease Virus

Infectious bursal disease virus is an icosahedral polyploid dsRNA virus

Electrostatic Interactions between Capsid and Scaffolding Proteins Mediate the Structural Polymorphism of a Double-stranded RNA Virus

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