Academic literature on the topic 'Viroplasm'

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Journal articles on the topic "Viroplasm"

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Jia, Dongsheng, Nianmei Guo, Hongyan Chen, et al. "Assembly of the viroplasm by viral non-structural protein Pns10 is essential for persistent infection of rice ragged stunt virus in its insect vector." Journal of General Virology 93, no. 10 (2012): 2299–309. http://dx.doi.org/10.1099/vir.0.042424-0.

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Rice ragged stunt virus (RRSV), an oryzavirus, is transmitted by brown planthopper in a persistent propagative manner. In this study, sequential infection of RRSV in the internal organs of its insect vector after ingestion of virus was investigated by immunofluorescence microscopy. RRSV was first detected in the epithelial cells of the midgut, from where it proceeded to the visceral muscles surrounding the midgut, then throughout the visceral muscles of the midgut and hindgut, and finally into the salivary glands. Viroplasms, the sites of virus replication and assembly of progeny virions, were
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Taraporewala, Zenobia F., Xiaofang Jiang, Rodrigo Vasquez-Del Carpio, Hariharan Jayaram, B. V. Venkataram Prasad, and John T. Patton. "Structure-Function Analysis of Rotavirus NSP2 Octamer by Using a Novel Complementation System." Journal of Virology 80, no. 16 (2006): 7984–94. http://dx.doi.org/10.1128/jvi.00172-06.

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ABSTRACT Viral inclusion bodies, or viroplasms, that form in rotavirus-infected cells direct replication and packaging of the segmented double-stranded RNA (dsRNA) genome. NSP2, one of two rotavirus proteins needed for viroplasm assembly, possesses NTPase, RNA-binding, and helix-unwinding activities. NSP2 of the rotavirus group causing endemic infantile diarrhea (group A) was shown to self-assemble into large doughnut-shaped octamers with circumferential grooves and deep clefts containing nucleotide-binding histidine triad (HIT)-like motifs. Here, we demonstrate that NSP2 of group C rotavirus,
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Vetter, Janine, Melissa Lee, and Catherine Eichwald. "The Role of the Host Cytoskeleton in the Formation and Dynamics of Rotavirus Viroplasms." Viruses 16, no. 5 (2024): 668. http://dx.doi.org/10.3390/v16050668.

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Rotavirus (RV) replicates within viroplasms, membraneless electron-dense globular cytosolic inclusions with liquid–liquid phase properties. In these structures occur the virus transcription, replication, and packaging of the virus genome in newly assembled double-layered particles. The viroplasms are composed of virus proteins (NSP2, NSP5, NSP4, VP1, VP2, VP3, and VP6), single- and double-stranded virus RNAs, and host components such as microtubules, perilipin-1, and chaperonins. The formation, coalescence, maintenance, and perinuclear localization of viroplasms rely on their association with
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Gaunt, Eleanor R., Qifeng Zhang, Winsome Cheung, Michael J. O. Wakelam, Andrew M. L. Lever, and Ulrich Desselberger. "Lipidome analysis of rotavirus-infected cells confirms the close interaction of lipid droplets with viroplasms." Journal of General Virology 94, no. 7 (2013): 1576–86. http://dx.doi.org/10.1099/vir.0.049635-0.

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Rotaviruses (RVs) cause acute gastroenteritis in infants and young children, and are globally distributed. Within the infected host cell, RVs establish replication complexes in viroplasms (‘viral factories’) to which lipid droplet organelles are recruited. To further understand this recently discovered phenomenon, the lipidomes of RV-infected and uninfected MA104 cells were investigated. Cell lysates were subjected to equilibrium ultracentrifugation through iodixanol gradients. Fourteen different classes of lipids were differentiated by mass spectrometry. The concentrations of virtually all li
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Sun, Liying, Li Xie, Ida Bagus Andika, Zilong Tan, and Jianping Chen. "Non-structural protein P6 encoded by rice black-streaked dwarf virus is recruited to viral inclusion bodies by binding to the viroplasm matrix protein P9-1." Journal of General Virology 94, no. 8 (2013): 1908–16. http://dx.doi.org/10.1099/vir.0.051698-0.

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Like other members of the family Reoviridae, rice black-streaked dwarf virus (RBSDV, genus Fijivirus) is thought to replicate and assemble within cytoplasmic viral inclusion bodies, commonly called viroplasms. RBSDV P9-1 is the key protein for the formation of viroplasms, but little is known about the other proteins of the viroplasm or the molecular interactions amongst its components. RBSDV non-structural proteins were screened for their association with P9-1 using a co-immunoprecipitation assay. Only P6 was found to directly interact with P9-1, an interaction that was confirmed by bimolecula
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Papa, Guido, Alexander Borodavka, and Ulrich Desselberger. "Viroplasms: Assembly and Functions of Rotavirus Replication Factories." Viruses 13, no. 7 (2021): 1349. http://dx.doi.org/10.3390/v13071349.

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Viroplasms are cytoplasmic, membraneless structures assembled in rotavirus (RV)-infected cells, which are intricately involved in viral replication. Two virus-encoded, non-structural proteins, NSP2 and NSP5, are the main drivers of viroplasm formation. The structures (as far as is known) and functions of these proteins are described. Recent studies using plasmid-only-based reverse genetics have significantly contributed to elucidation of the crucial roles of these proteins in RV replication. Thus, it has been recognized that viroplasms resemble liquid-like protein–RNA condensates that may be f
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Kim, Mikyeong, Hong Soo Choi, Jun Sung Lee, Myung-Kyu Song, Jeong Soo Kim, and Hae-Ryun Kwak. "Ultrastructural Characteristics and Viral Replication Sites in Chloroplasts of Kimchi Cabbage Cells infected with Turnip Yellow Mosaic Virus." Research in Plant Disease 30, no. 4 (2024): 432–41. https://doi.org/10.5423/rpd.2024.30.4.432.

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A significant number of vesicles developed at the inner edge of chloroplasts of kimchi cabbage cells infected with turnip yellow mosaic virus (TYMV). The vesicle found in the chloroplasts are typical ultrastructures resulting from infection of TYMV. The size and shape of the vesicles varied, but most were spherical. These vesiclesserved as sites for the multiplication of virus particles, functioning as viroplasm. Additionally, a new sausage-shaped ultrastructure was observed in the chloroplasts of TYMV-infected cells. Both the sausageshaped structures and the vesicles were composed of double m
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Zhang, Chaozheng, Yueyong Liu, Liyue Liu та ін. "Rice black streaked dwarf virus P9-1, an α-helical protein, self-interacts and forms viroplasms in vivo". Journal of General Virology 89, № 7 (2008): 1770–76. http://dx.doi.org/10.1099/vir.0.2008/000109-0.

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Replication and assembly of viruses from the family Reoviridae are thought to take place in discrete cytoplasmic inclusion bodies, commonly called viral factories or viroplasms. Rice black streaked dwarf virus (RBSDV) P9-1, a non-structural protein, has been confirmed to accumulate in these intracellular viroplasms in infected plants and insects. However, little is known about its exact function. In this study, P9-1 of RBSDV-Baoding was expressed in Escherichia coli as a His-tagged fusion protein and analysed using biochemical and biophysical techniques. Mass spectrometry and circular dichrois
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Buchwalter, Rebecca A., Sarah C. Ogden, Sara B. York, et al. "Coordination of Zika Virus Infection and Viroplasm Organization by Microtubules and Microtubule-Organizing Centers." Cells 10, no. 12 (2021): 3335. http://dx.doi.org/10.3390/cells10123335.

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Zika virus (ZIKV) became a global health concern in 2016 due to its links to congenital microcephaly and other birth defects. Flaviviruses, including ZIKV, reorganize the endoplasmic reticulum (ER) to form a viroplasm, a compartment where virus particles are assembled. Microtubules (MTs) and microtubule-organizing centers (MTOCs) coordinate structural and trafficking functions in the cell, and MTs also support replication of flaviviruses. Here we investigated the roles of MTs and the cell’s MTOCs on ZIKV viroplasm organization and virus production. We show that a toroidal-shaped viroplasm form
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Criglar, Jeanette M., Ramakrishnan Anish, Liya Hu, et al. "Phosphorylation cascade regulates the formation and maturation of rotaviral replication factories." Proceedings of the National Academy of Sciences 115, no. 51 (2018): E12015—E12023. http://dx.doi.org/10.1073/pnas.1717944115.

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The rotavirus (RV) genome is replicated and packaged into virus progeny in cytoplasmic inclusions called viroplasms, which require interactions between RV nonstructural proteins NSP2 and NSP5. How viroplasms form remains unknown. We previously found two forms of NSP2 in RV-infected cells: a cytoplasmically dispersed dNSP2, which interacts with hypophosphorylated NSP5; and a viroplasm-specific vNSP2, which interacts with hyperphosphorylated NSP5. Other studies report that CK1α, a ubiquitous cellular kinase, hyperphosphorylates NSP5, but requires NSP2 for reasons that are unclear. Here we show t
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Dissertations / Theses on the topic "Viroplasm"

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Contin, Roberta. "Studies on the assembly of rotavirus viroplasmas." Doctoral thesis, Scuola Normale Superiore, 2009. http://hdl.handle.net/11384/85937.

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The processes that regulate Rotavirus replication are not fully understood and the lack of a reverse genetic approach represent an obstacle for the investigations in Rotavirus biology. Viroplasms are cytoplasmic structures that form soon after infection, and constitute the site of virus replication. Structural proteins like the viral RNA-dependent RNA -polymerase VP1, the capping enzyme VP3, the scaffolding protein VP2,and the middle layer VP6 localize in viroplasms; in addition, also the non-structural proteins NSP5 and NSP2 have been demonstrated to be essential components for viroplasm form
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Cheung, W. K. S. "Rotavirus inclusion bodies ('viroplasms') are structurally and functionally associated with lipid droplet components." Thesis, University of Cambridge, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.597592.

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Rotaviruses are a leading cause of acute gastroenteritis in infants and young children worldwide and possess a genome of 11 double-stranded (ds) RNA segments. Early morphogenesis of RV particles and viral RNA replication occur in cytoplasmic inclusion bodies called ‘viroplasms’, of which the viral non-structural proteins NSP2 and NSP5 are essential components. Using confocal microscopy (CM), we demonstrated association of viroplasms with lipids and lipid droplet (LD)-associated proteins (perilipin A, ADRP). LD-associated proteins were found to co-localise with viroplasm-like structures (VLS) i
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Bessières, Emilie. "Caractérisation biochimique de structures macromoléculaires induites durant l'infection de cellules par le rotavirus." Paris 6, 2009. http://www.theses.fr/2009PA066349.

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L’infection de cellules par le rotavirus implique la formation de nombreux assemblages macromoléculaires qui recrutent, en plus des protéines virales, de nombreuses protéines cellulaires nécessaires à la morphogenèse virale, à la signalisation et à la mise en place de défenses anti-virales. Cette stratégie est commune à de nombreux virus. La connaissance de la composition, de la structure et du fonctionnement de ces complexes, dont certains ont été baptisés “usines virales“, est d’un intérêt majeur pour la biologie cellulaire fondamentale et pour la conception de stratégies thérapeutiques inno
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Dhillon, Poonam. "Rotavirus Viroplasm Structure (VS) : The First Insights into the Architectural Assembly of the Viral and Host Factors in the VS"." Thesis, 2017. http://etd.iisc.ac.in/handle/2005/4167.

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Rotavirus is a major cause of acute gastroenteritis in infants and young children and responsible for approximately 453,000 infantile deaths per year. Rotaviruses are non-enveloped RNA viruses belonging to the Reoviridae family. The rotavirus genome is composed of 11 segments of double-stranded RNA (dsRNA), enclosed in an icosahedral triple-layered protein capsid, and it encodes six structural proteins (VP) and six non-structural proteins (NSPs). Removal of the outer capsid from the triple-layered particle (TLP) during virus entry into the cell activates the synthesis and extrusion of the vira
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Tandra, Varsha. "Interactions between host cellular factors and Rotaviral viroplasmic non-structural proteins NSP5, NSP2 and their influence on virus replication." Thesis, 2019. https://etd.iisc.ac.in/handle/2005/5127.

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Overall, the present study demonstrates the dynamic nature of rotavirus viroplasm and how it manipulates the intracellular environment by intracellular relocalization of host proteins and their sequestration in viroplasms for its survival and to manifest the infection. This work demonstrates the mechanism by which the host proteins are recruited into the viral replication structures called viroplasms
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Wentzel, Johannes Frederik. "Investigating the importance of co-expressed rotavirus proteins in the development of a selection-free rotavirus reverse genetics system / Johannes Frederik Wentzel." Thesis, 2014. http://hdl.handle.net/10394/12270.

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Reverse genetics is an innovative molecular biology tool that enables the manipulation of viral genomes at the cDNA level in order to generate particular mutants or artificial viruses. The reverse genetics system for the influenza virus is arguably one of the best illustrations of the potential power of this technology. This reverse genetics system is the basis for the ability to regularly adapt influenza vaccines strains. Today, reverse genetic systems have been developed for many animal RNA viruses. Selection-free reverse genetics systems have been developed for the members of the Reoviridae
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Book chapters on the topic "Viroplasm"

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Netherton, Christopher, Katy Moffat, Elizabeth Brooks, and Thomas Wileman. "A Guide to Viral Inclusions, Membrane Rearrangements, Factories, and Viroplasm Produced During Virus Replication." In Advances in Virus Research. Elsevier, 2007. http://dx.doi.org/10.1016/s0065-3527(07)70004-0.

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Abdulaziz Othman Alkubaisi, Noorah, and Nagwa Mohammed Amin Aref. "Cytoplasmic Matrix and Viroplasms Inclusions in the Presence of Gold Nanoparticles (AuNPs)." In Atlas of Ultrastructure Interaction Proteome Between Barley Yellow Dwarf Virus and Gold Nanoparticles. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.97442.

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Cellular ultrastructure micrographs revealed striking changes resulting from the Barley Yellow Dwarf Virus (BYDV-PAV) infection in Electron microscopy. In the cytoplasm, the Gold nanoparticles (AuNPs) may bind with different cytoplasmic organelles and interfere with the treated site’s metabolic processes. The micrographs of the treated plant leave with AuNPs showing; Endosomes, amorphous bodies, slender filaments fibers, myelin bodies with a high concentration of virus particles, and Gold Nanoparticles distributed in a circulated shape in the cytoplasm with virus particles.
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