Cryo-Electron Microscopy Structure of the Macrobrachium rosenbergii Nodavirus Capsid at 7 Angstroms Resolution

Ho, Ken; Kueh, Chare Li; Beh, Poay Ling; Tan, Wen Siang; Bhella, David

doi:10.1038/s41598-017-02292-0

Cited by 27 publications

(58 citation statements)

References 42 publications

(52 reference statements)

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“…Imposing icosahedral symmetry averages different regions of the genome into common secondary structural motifs visible only at a lower resolution. A similar RNA cage was reported for the nodaviruses (40,41), suggesting a common strategy for viral RNA folding. Inside the pentagonal face of the cage, five small densities under the density corresponding to the VP4 protein were visible.…”

Section: Resultssupporting

confidence: 72%

Cryo-Electron Microscopy Structure of Seneca Valley Virus Procapsid

Strauß

Jayawardena

Sun

et al. 2018

J Virol

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Seneca Valley Virus, like some other members of the picornaviridae, forms naturally occurring empty capsids, known as procapsids. The procapsid has the same antigenicity as the full virion, so they present an interesting possibility for the formation of stable virus-like particles. Interestingly, although SVV is a livestock pathogen, it has also been found to preferentially infect tumour cells, and is being explored for use as a therapeutic agent in the treatment of small cell lung cancers. Here we used cryo-electron microscopy to investigate the procapsid structure and describe the transition of capsid protein VP0 to the cleaved forms of VP4 and VP2. We show that the SVV receptor binds the procapsid, as evidence of its native antigenicity. In comparing the procapsid structure to that of the full virion, we also show that a cage of RNA serves to stabilize the inside surface of the virus, thereby making it more acid-stable.Viruses are extensively studied to help us understand infection and disease. One of the by-products of some virus infections are the naturally occurring empty virus capsids (containing no genome), termed procapsids, whose function remains unclear. Here we investigate the structure and formation of the procapsids of Seneca Valley Virus, to better understand how they form, what causes them to form, how they behave, and how we can make use of them. One potential benefit of this work is the modification of the procapsid to develop it for targeted delivery of therapeutics or to make a stable vaccine against SVV, which could be of great interest to the agricultural industry.

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Section: Resultssupporting

confidence: 72%

Cryo-Electron Microscopy Structure of Seneca Valley Virus Procapsid

Strauß

Jayawardena

Sun

et al. 2018

J Virol

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“…However, even though phylogenetic analysis of the MrNV capsid affiliates MrNV to betanodavirus (Bonami & Widada, 2011), but the secondary structure analysis of MrNV capsid was found to be highly homolog with cucumber necrosis virus subunit, rather than nodaviruses (Somrit et al, 2017). Moreover, the recently published cryo-electron microscopy structure of the MrNV is reported to have a noteworthy difference in the viral capsid protein from the insect-and fish-infecting nodaviruses (Ho, Kueh, Beh, Tan, & Bhella, 2017), which further strengthens the assertion of…”

Section: Virus Bindingmentioning

confidence: 63%

Molecular biology of Macrobrachium rosenbergii nodavirus infection in giant freshwater prawn

Low

Yusoff²,

Kuppusamy³

et al. 2018

Journal of Fish Diseases

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Macrobrachium rosenbergii nodavirus (MrNV) has been threatening the giant freshwater prawn aquaculture since 1997, causing white tail disease in the prawn species that leads to 100% lethality of the infected postlarvae. Comprehension of the viral infectivity and pathogenesis at molecular biology level has recently resolved the viral capsid protein and evidenced the significant difference in the viral structural protein compared to other nodaviruses that infect fish and insect. Cumulative researches have remarked the proposal to assert MrNV as a member of new genus, gammanodavirus to the Nodaviridae family. The significance of molecular biology in MrNV infection is being highlighted in this current review, revolving the viral life cycle from virus binding and entry into host, virus replication in host cell, to virus assembly and release. The current review also highlights the emerging aptamers technology that is also known as synthetic antibody, its application in disease diagnosis, and its prophylactic and therapeutic properties. The future perspective of synthetic virology technology in understanding viral pathogenesis, as well as its potential in viral vaccine development, is also discussed.

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“…injection of MCTV (10 4 copies/g of body weight), whereas the controls received PBS. Nine crabs were selected randomly at each time point (4,12,24,48,72, and 96 h postinoculation), and total RNA was extracted according to the manufacturer's instructions. Reverse transcription was performed using the PrimeScript RT reagent kit (TaKaRa, Japan) according to the manufacturer's instructions.…”

Section: Methodsmentioning

confidence: 99%

Cryo-electron Microscopy Structures of Novel Viruses from Mud Crab Scylla paramamosain with Multiple Infections

Gao

Liu

Huang

et al. 2019

J Virol

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Viruses associated with sleeping disease (SD) in crabs cause great economic losses to aquaculture, and no effective measures are available for their prevention. In this study, to help develop novel antiviral strategies, single-particle cryoelectron microscopy was applied to investigate viruses associated with SD. The results not only revealed the structure of mud crab dicistrovirus (MCDV) but also identified a novel mud crab tombus-like virus (MCTV) not previously detected using molecular biology methods. The structure of MCDV at a 3.5-Å resolution reveals three major capsid proteins (VP1 to VP3) organized into a pseudo-Tϭ3 icosahedral capsid, and affirms the existence of VP4. Unusually, MCDV VP3 contains a long C-terminal region and forms a novel protrusion that has not been observed in other dicistrovirus. Our results also reveal that MCDV can release its genome via conformation changes of the protrusions when viral mixtures are heated. The structure of MCTV at a 3.3-Å resolution reveals a Tϭ 3 icosahedral capsid with common features of both tombusviruses and nodaviruses. Furthermore, MCTV has a novel hydrophobic tunnel beneath the 5-fold vertex and 30 dimeric protrusions composed of the P-domains of the capsid protein at the 2-fold axes that are exposed on the virion surface. The structural features of MCTV are consistent with a novel type of virus. IMPORTANCE Pathogen identification is vital for unknown infectious outbreaks, especially for dual or multiple infections. Sleeping disease (SD) in crabs causes great economic losses to aquaculture worldwide. Here we report the discovery and identification of a novel virus in mud crabs with multiple infections that was not previously detected by molecular, immune, or traditional electron microscopy (EM) methods. High-resolution structures of pathogenic viruses are essential for a molecular understanding and developing new disease prevention methods. The three-dimensional (3D) structure of the mud crab tombus-like virus (MCTV) and mud crab dicistrovirus (MCDV) determined in this study could assist the development of antiviral inhibitors. The identification of a novel virus in multiple infections previously missed using other methods demonstrates the usefulness of this strategy for investigating multiple infectious outbreaks, even in humans and other animals.

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Cryo-Electron Microscopy Structure of the Macrobrachium rosenbergii Nodavirus Capsid at 7 Angstroms Resolution

Cited by 27 publications

References 42 publications

Cryo-Electron Microscopy Structure of Seneca Valley Virus Procapsid

Cryo-Electron Microscopy Structure of Seneca Valley Virus Procapsid

Molecular biology of Macrobrachium rosenbergii nodavirus infection in giant freshwater prawn

Cryo-electron Microscopy Structures of Novel Viruses from Mud Crab Scylla paramamosain with Multiple Infections

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