How Tupanvirus Degrades the Ribosomal RNA of Its Amoebal Host? The Ribonuclease T2 Track

Rolland, Clara; Scola, Bernard La; Levasseur, Anthony

doi:10.3389/fmicb.2020.01691

Cited by 7 publications

(5 citation statements)

References 45 publications

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“…Simultaneously, the nucleus is also a target of degradation which would help the eventual separation of ribosomes. The ribosomal RNA degradation was denominated ribosomal shutdown (Abrahão et al, 2008;Rolland et al, 2020). In our work, a similar cytotoxicity effect due to exposition to the viruses was witnessed for A549 cells as exposure to both APMV and TPV, even in the apparent absence of replication.…”

Section: Discussionsupporting

confidence: 78%

Paving the way towards understanding the inflammatory pathways triggered by giant viruses in mammalian cells: effect of mimivirus-cell interactions on IκBα degradation

Oliveira

Essus

et al. 2021

Preprint

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Even after two decades since the identification of the first giant virus, the Acanthamoeba polyphaga mimivirus (APMV), it still elude scientists. Their gigantic size and genome are unique in the whole virosphere, and many aspects of their biology are still unknown, including their possible hosts. They are cultivated in laboratories using Acanthamoeba cells as hosts, but little is known about the infectivity of these giant viruses in vertebrate cells. However, there is evidence of the possible involvement of APMV in pneumonia and activation of inflammatory pathways. Among the hundreds of prospected giant viruses members is Tupanvirus, isolated in Brazil. Its particles have a characteristically large size varying between 1.2 to 2 μm and are covered by fibrils. In the present work, we aim to study the consequences of the incubation of APMV and Tupanvirus with mammalian cells. These cells express Toll-like receptors (TLR) that are capable of recognizing lipopolysaccharides, favoring the internalization of the antigen and activation of the inflammatory system. We used a lineage of human lung adenocarcinoma cells (A549) to evaluate possible effects of TLR activation by the giant viruses and if we could detect the probable cause of the said giant-virus dependent pneumonia. Our results show that APMV and Tupanvirus (TPV) activate cellular receptors related to the Toll-like 4 type-induced inflammatory response and that the A549 cells are capable of internalizing the latter virus. Therefore, this study brings new insights into the possible interactions established between mimiviruses (here represented by APMV and Tupanvirus) and members of the innate cellular immune response.

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Section: Discussionsupporting

confidence: 78%

Paving the way towards understanding the inflammatory pathways triggered by giant viruses in mammalian cells: effect of mimivirus-cell interactions on IκBα degradation

Oliveira

Essus

et al. 2021

Preprint

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“…Nicotinamide/nicotinate mononucleotide adenylyl transferase (NMNAT) and NADAR (NAD + and ADP-ribose) participate in NAD + biosynthesis and NAD + -utilization pathway, whereas cystathionine gammasynthase and dihydrofolate reductase are involved in the synthesis of cystathionine and purines, respectively. Interestingly, we also identified a homolog of RNase T2, which has been recently described in Tupanvirus soda lake and discovered in Fadolivirus (Rolland et al, 2020;Schulz et al, 2020a).…”

Section: Genomic Characterization Of Clandestinovirusmentioning

confidence: 60%

Clandestinovirus: A Giant Virus With Chromatin Proteins and a Potential to Manipulate the Cell Cycle of Its Host Vermamoeba vermiformis

et al. 2021

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For several decades, the vast world of DNA viruses has been expanding constantly. Various discoveries in this field have broadened our knowledge and revealed that DNA viruses encode many functional features, which were once thought to be exclusive to cellular life. Here, we report the isolation of a giant virus named “clandestinovirus,” grown on the amoebal host Vermamoeba vermiformis. This virus was discovered in a mixed co-culture associated with another giant virus, Faustovirus ST1. Clandestinovirus possesses a linear dsDNA genome of 581,987 base pairs containing 617 genes. Phylogenetically, clandestinovirus is most closely related to Acanthamoeba castellanii medusavirus and was considered a member of the proposed Medusaviridae family. However, clandestinovirus genome is 65% larger than that of medusavirus, emphasizing the considerable genome size variation within this virus family. Functional annotation of the clandestinovirus genes suggests that the virus encodes four core histones. Furthermore, clandestinovirus appears to orchestrate the cell cycle and mitochondrial activities of the infected host by virtue of encoding a panel of protein kinases and phosphatases, and a suite of functionally diverse mitochondrial protein homologs, respectively. Collectively, these observations illuminate a strategy employed by clandestinovirus to optimize the intracellular environment for efficient virus propagation.

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“…To infer the evolutionary history of the RNase T2 protein, sequences were obtained from the GenBank protein database for conserved domains using the queries “taxid 238513” and “taxid 238220”, literature searches 86,87 , these were supplemented with structurally homologous protein clusters identified using the AlphaFold database FoldSeek clusters server 88 .…”

Section: Methodsmentioning

confidence: 99%

Mapping glycoprotein structure reveals defining events in the evolution of theFlaviviridae

Mifsud,

Lytras,

Oliver

et al. 2024

Preprint

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SummaryViral glycoproteins drive membrane fusion in enveloped viruses and determine host range, tissue tropism and pathogenesis. Despite their importance, there is a fragmentary understanding of glycoproteins within theFlaviviridae; for many species the glycoproteins have not yet been identified, for others, such as the hepaciviruses, the molecular mechanisms of membrane fusion remain uncharacterised. Here, we combine comprehensive phylogenetic analyses with systematic protein structure prediction to survey glycoproteins across the entireFlaviviridae. We discover class-II fusion systems, homologous to the orthoflavivirus E glycoprotein, in most species, including highly-divergent jingmenviruses and large genome flaviviruses. However, the E1E2 glycoproteins of the hepaci-, pegi- and pestiviruses are structurally distinct, may represent a novel class of fusion mechanism, and are strictly associated with infection of vertebrate hosts. By mapping glycoprotein distribution onto the underlying phylogeny we reveal a complex history of evolutionary events that have shaped the diverse virology and ecology of theFlaviviridae.

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How Tupanvirus Degrades the Ribosomal RNA of Its Amoebal Host? The Ribonuclease T2 Track

Cited by 7 publications

References 45 publications

Paving the way towards understanding the inflammatory pathways triggered by giant viruses in mammalian cells: effect of mimivirus-cell interactions on IκBα degradation

Paving the way towards understanding the inflammatory pathways triggered by giant viruses in mammalian cells: effect of mimivirus-cell interactions on IκBα degradation

Clandestinovirus: A Giant Virus With Chromatin Proteins and a Potential to Manipulate the Cell Cycle of Its Host Vermamoeba vermiformis

Mapping glycoprotein structure reveals defining events in the evolution of theFlaviviridae

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