Large conformational changes in the maturation of a simple RNA virus, Nudaurelia capensis ω virus (NωV) 1 1Edited by D. Rees

Canady, Mary A.; Tihova, Mariana; Hanzlik, Terry N.; Johnson, John E.; Yeager, Mark

doi:10.1006/jmbi.2000.3723

Cited by 101 publications

(113 citation statements)

References 47 publications

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“…The viral capsid of FHV consists of 180 copies of α, whereas the viral capsid of NωV has 240. Upon maturation, α undergoes an autocatalytic cleavage in its C-terminal region to form β, comprising the main structural capsid component, and γ, a short hydrophobic peptide required for endosome penetration that remains associated with the viral capsid (13)(14)(15). VLPs of FHV and NωV spontaneously form in Spodoptera frugiperda cell lines (e.g., Sf21) when RNA 2 is expressed from a baculovirus vector (16,17).…”

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confidence: 99%

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Host RNAs, including transposons, are encapsidated by a eukaryotic single-stranded RNA virus

Routh

Domitrovic

Johnson

2012

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

106

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Next-generation sequencing is a valuable tool in our growing understanding of the genetic diversity of viral populations. Using this technology, we have investigated the RNA content of a purified nonenveloped single-stranded RNA virus, flock house virus (FHV). We have also investigated the RNA content of virus-like particles (VLPs) of FHV and the related Nudaurelia capensis omega virus. VLPs predominantly package ribosomal RNA and transcripts of their baculoviral expression vectors. In addition, we find that 5.3% of the packaged RNAs are transposable elements derived from the Sf21 genome. This observation may be important when considering the therapeutic use of VLPs. We find that authentic FHV virions also package a variety of host RNAs, accounting for 1% of the packaged nucleic acid. Significant quantities of host messenger RNAs, ribosomal RNA, noncoding RNAs, and transposable elements are readily detected. The packaging of these host RNAs elicits the possibility of horizontal gene transfer between eukaryotic hosts that share a viral pathogen. We conclude that the genetic content of nonenveloped RNA viruses is variable, not just by genome mutation, but also in the diversity of RNA transcripts that are packaged.deep-sequencing | virus evolution | virus assembly N ext-generation sequencing (NGS) is a powerful tool in the investigation of viral diversity from many different perspectives. NGS has been applied in directed approaches to investigate the prevalence of polymorphism or quasispecies present in a population of known viruses within a host, e.g., foot-and-mouth disease virus (1) or to follow the evolution of a viral genome and the frequency of known polymorphisms during the course of an infection, e.g., human rhinovirus (2) and HIV (3). The total genetic content of biological or clinical samples have been sequenced to uncover viruses present even at very low titers, for example, the presence of porcine circovirus-1 in Rotarix samples (4) and the identification of influenza virus subtypes and norovirus from nasopharyngeal and fecal samples collected during outbreaks (5).NGS has also been applied in unbiased approaches aimed at the discovery of new viral species without any advance genetic information. For example, the Merkel cell polyomavirus was discovered to be the causative agent of its eponymous carcinoma by deep sequencing the transcriptome of tumor cells and analyzing nonhost transcripts (6). Similarly, it has been possible to uncover the history of viral pathogens that have plagued an organism through the de novo assembly of the sequenced siRNAs that would have been generated to tackle viral infections. This approach has revealed the viral genomes of familiar miscreants as well as of new viruses, for example, in fruit flies, mosquitoes, and nematode worms (7).In this report, we employ NGS to investigate the total RNA encapsidated by authentic flock house virus (FHV) virions and by virus-like particles (VLPs) of FHV and of the related tetravirus, Nudaurelia capensis omega virus (NωV). Our analysis emplo...

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confidence: 99%

“…However, we also find that a number of transposable elements are packaged. Many VLPs, are structurally and biochemically indistinguishable from their parent virus (13,16,17). Consequently, it is likely that they can deliver their genomic cargo in the same way as an authentic virion.…”

mentioning

confidence: 99%

Host RNAs, including transposons, are encapsidated by a eukaryotic single-stranded RNA virus

Routh

Domitrovic

Johnson

2012

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

106

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“…Another fact that remains to be clarified in the sophisticated succession of interactions between VP3 and (p)VP2 refers to the high flexibility exhibited by the VP2 C-terminal end (21). It is likely that the conformational change originates from a rearrangement of some helical regions in the procapsid internal VP2 S domains as described for the Nudaurelia capensis virus conformational change (14,17,38).…”

Section: Discussionmentioning

confidence: 96%

“…This maturation mechanism is reminiscent of the post-assembly proteolytic maturation that takes place during the morphogenesis of some ssRNA icosahedral viruses, and in particular to those of noda-and tetraviruses (14,15). The capsid protein (CP) precursor, the ␣-protein, associates as a trimer, building a quasi-spherical provirion (16).…”

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confidence: 99%

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Autoproteolytic Activity Derived from the Infectious Bursal Disease Virus Capsid Protein

Irigoyen

Garriga

Navarro

et al. 2009

Journal of Biological Chemistry

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Viral capsids are envisioned as vehicles to deliver the viral genome to the host cell. They are nonetheless dynamic protective shells, as they participate in numerous processes of the virus cycle such as assembly, genome packaging, binding to receptors, and uncoating among others. In so doing, they undergo large scale conformational changes. Capsid proteins with essential enzymatic activities are being described more frequently. Here we show that the precursor (pVP2) of the capsid protein VP2 of the infectious bursal disease virus (IBDV), an avian double-stranded RNA virus, has autoproteolytic activity. The pVP2 C-terminal region is first processed by the viral protease VP4. VP2 Asp-431, lying in a flexible loop preceding the C-terminal most ␣-helix, is responsible for the endopeptidase activity that cleaves the Ala-441-Phe-442 bond to generate the mature VP2 polypeptide. The D431N substitution abrogates the endopeptidase activity without introducing a significant conformational change, as deduced from the three-dimensional structure of the mutant protein at 3.1 Å resolution. Combinations of VP2 polypeptides containing mutations affecting either the cleavage or the catalytic site revealed that pVP2 proteolytic processing is the result of a monomolecular cis-cleavage reaction. The D431N mutation does not affect the assembly of the VP2 trimers that constitute the capsid building block. Although VP2 D431N trimers are capable of assembling both pentamers and hexamers, expression of a polyprotein gene harboring the D431N mutation does not result in the assembly of IBDV virus-like particles. Reverse genetics analyses demonstrate that pVP2 self-processing is essential for the assembly of an infectious IBDV progeny.

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Transmembrane ?-helices in the gap junction membrane channel: Systematic search of packing models based on the pair potential function

Nunn

Macke

Olson

et al. 2001

Microsc. Res. Tech.

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Large conformational changes in the maturation of a simple RNA virus, Nudaurelia capensis ω virus (NωV) 1 1Edited by D. Rees

Cited by 101 publications

References 47 publications

Host RNAs, including transposons, are encapsidated by a eukaryotic single-stranded RNA virus

Host RNAs, including transposons, are encapsidated by a eukaryotic single-stranded RNA virus

Autoproteolytic Activity Derived from the Infectious Bursal Disease Virus Capsid Protein

Transmembrane ?-helices in the gap junction membrane channel: Systematic search of packing models based on the pair potential function

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