New preprint from the lab, plus loads of fabulous collaborators, describing how most poxviruses, including avipoxviruses, antagonise DNA-PK to block cGAS/STING-dependent interferon production during infection. These viruses disrupt the interaction between DNA-PK and DNA thereby inhibiting sesnsing of viral DNA. This immune evasion mechanism is conserved across a broader range of species than other poxvirus antagonists, which may reflect the difficulty in evolving escape mechanisms that interfere with a protein that is essential for maintenance of genomic stability. This could also be relevant to the severity of mpox, as the milder clade II virus has lost one of the genes that inhibits DNA-PK. The clade Ib virus has kept this gene and will therefore be able to block host immune responses more effectively. https://lnkd.in/ei-WeMZr
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The aldehyde dehydrogenase ALDH1B1 exerts antiviral effects through the aggregation of the adaptor MAVS Detection of RNA-based viruses by the receptor RIG-I induces the aggregation of the mitochondrial protein MAVS, which in turn stimulates the production of proinflammatory cytokines critical for host defenses. Sun et al. found that this antiviral response was enhanced by ALDH1B1, a mitochondrially localized aldehyde dehydrogenase involved in ethanol metabolism. ALDH1B1, whose abundance was increased by infection with clinically relevant RNA viruses, limited viral replication. Interaction of ALDH1B1 with MAVS enhanced its aggregation and its association with RIG-I. ALDH1B1-deficient mice had higher viral titers in the lung, developed more severe lung damage, and were less likely to survive infection with influenza A. Thus, ALDH1B1 promotes antiviral signaling pathways initiated by RIG-I and MAVS. #ALDH1B1 #AntiviralEffects #MAVSAggregation #RIGIReceptor #RNAVirusDetection #EthanolMetabolism #HostDefenses #ProinflammatoryCytokines #ViralReplicationControl #InfluenzaResearch #MitochondrialProtein #ViralTiters #LungDamage #AntiviralPathways #HostImmuneResponse
The aldehyde dehydrogenase ALDH1B1 exerts antiviral effects through the aggregation of the adaptor MAVS
science.org
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New Insights into SARS-CoV-2 and Host Cell Death New research from S Kesavardhana lab reveals that SARS-CoV-2 and related bat RNA viruses use viral RHIM motifs in the Nsp13 protein to interact with host proteins like ZBP1 and RIPK3, triggering regulated cell death. This process, which is more pronounced in human cells than in bat cells, highlights a species-specific mechanism. Additionally, Z-RNA segments in the SARS-CoV-2 genome amplify Nsp13-driven cell death, potentially contributing to cellular damage and cytokine storms seen during infection. These findings provide critical insights into how zoonotic RNA viruses drive host cell death and evade immune defenses, opening new avenues for therapeutic strategies. https://lnkd.in/gGKgwHyF #Virology #SARSCoV2 #CellDeath #Research
Bat RNA viruses employ viral RHIMs orchestrating species-specific cell death programs linked to Z-RNA sensing and ZBP1-RIPK3 signaling
sciencedirect.com
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"Many studies have shown that macrophages can internalize viruses and degrade them in lysosomes for clearance in vivo. Inspired by these natural behaviors and using SARS-CoV-2 as a testbed, researchers harvest lysosomes from activated macrophages and anchor the protein-receptor ACE2 as bait, thus constructing a lysosomal “TRAP” (lysoTRAP) that selectively captures, internalizes, and eventually degrades SARS-CoV-2. Through experiments with cells, female mice, female hamsters, and human lung organoids, we demonstrate that lysoTRAP effectively clears SARS-CoV-2." https://lnkd.in/eXybvhWX #lysosomes #virus clearance
Lysosomal “TRAP”: a neotype modality for clearance of viruses and variants - Nature Communications
nature.com
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New Article: Structure of the Nipah virus polymerase phosphoprotein complex The Nipah virus, known for its high fatality rate, has no approved vaccine or treatments. Here the authors present the cryoEM structure of the Nipah virus RNA polymerase machinery, comprising the large protein L and the phosphoprotein P. https://lnkd.in/gmGZscxJ
Structure of the Nipah virus polymerase phosphoprotein complex - Nature Communications
nature.com
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I am thrilled to publish my fourth first-author paper as a postdoc in under four years entitled " TFEB interaction with RagC is disrupted during EV-D68 infection. In this paper, we showed that TFEB, the master transcriptional regulator of autophagy and lysosomal biogenesis, regulates EV-D68 infection at two distinct steps of the viral lifecycle: RNA replication and nonlytic egress using different mechanisms. https://lnkd.in/evBKkSTu
Transcription factor EB (TFEB) interaction with RagC is disrupted during enterovirus D68 infection | Journal of Virology
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📃Scientific paper: Sialic acids and viruses Abstract: Let us study viruses and the role of sialic acids in their first step of reproduction, the attachment to cells. We begin our study with the help of the "Earth's virology course", created by Vincent Racaniello, with David Tuller and Gertrud U. Rey. The first virus that we will study is that of influenza A. Actually, "Earth's virology course" is a proper starting point for learning the mechanisms the virus uses to attach and enter the host cells. In the case of the influenza virus, its spike protein is used to attach the virion to sialic acid receptors of the host cells. Then we will consider coronaviruses, with the help of literature about the role of sialic acids in their attachment by means of spike proteins. In fact, there are seven human coronavirus, and they use sialic acid or angiotensin-converting enzyme 2 (ACE2) or other receptors or a combination of them. We can find in literature that Sars-Cov-2 virus can use sialic acid too for the attachment to cells, but its main target is considered the ACE2 receptor.;See please the new version. I have revised the discussion about hemmaglutinin esterase in coronaviruses. I have also added figures and references. --- The study in 10.1021/acscentsci.0c00855 used a glyco-nanoparticle platform, discovering that N-acetyl neuraminic acid has affinity toward the SARS-COV-2 spike glycoprotein, that is a glycan-binding function. However, a recent study, 10.1016/j.scib.2021.01.010, which has investigated the binding of the s... Continued on ES/IODE ➡️ https://etcse.fr/W3q ------- If you find this interesting, feel free to follow, comment and share. We need your help to enhance our visibility, so that our platform continues to serve you.
Sialic acids and viruses
ethicseido.com
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🎉 Exciting News! 🎉 I'm thrilled to share that my latest research paper, "Characterization of bi-segmented and tri-segmented recombinant Pichinde virus particles," has just been published in the Journal of Virology! In this study, we investigated the incorporation of host-cell proteins into new Pichinde virus (PICV) particles during viral egress. Our analysis revealed that bi-segmented and tri-segmented recombinant PICV particles contain a similar repertoire of host-cell proteins, including key components involved in virus assembly and release, such as those from the endosomal sorting complex required for transport (ESCRT) pathway. We also identified other proteins with potential yet unexplored roles in viral infection. These findings provide valuable insights into the molecular composition of mammarenavirus particles and offer a foundation for future research into antiviral strategies and the development of viral vector platforms. I'm incredibly proud of our achievements and deeply grateful to my lab mates and collaborators! ❤️ You can read the full paper here: https://lnkd.in/gYePE8UE
Characterization of bi-segmented and tri-segmented recombinant Pichinde virus particles | Journal of Virology
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📃Scientific paper: Sialic acids and viruses Year: 2021 Abstract: Let us study viruses and the role of sialic acids in their first step of reproduction, the attachment to cells. We begin our study with the help of the "Earth's virology course", created by Vincent Racaniello, with David Tuller and Gertrud U. Rey. The first virus that we will study is that of influenza A. Actually, "Earth's virology course" is a proper starting point for learning the mechanisms the virus uses to attach and enter the host cells. In the case of the influenza virus, its spike protein is used to attach the virion to sialic acid receptors of the host cells. Then, we will consider coronaviruses, with the help of literature about the role of sialic acids in their attachment by means of spike proteins. In fact, there are seven human coronavirus and they use sialic acid or angiotensin-converting enzyme 2 (ACE2) or other receptors or a combination of them. Let us review the literature to understand if Sars-Cov-2 virus can use sialic acid for the attachment to cells or not. Its main target is considered the ACE2 receptor. The study in 10.1021/acscentsci.0c00855 used a glyco-nanoparticle platform, discovering that N-acetyl neuraminic acid has affinity toward the SARS-COV-2 spike glycoprotein, that is a glycan-binding function. However, a recent study, 10.1016/j.scib.2021.01.010, which has investigated the binding of the spikes of the virus by means of micro-arrays, tells that no binding with sialic acid residues was detected. All the tested protein molecu... Continued on ES/IODE ➡️ https://etcse.fr/l6 ------- If you find this interesting, feel free to follow, comment and share. We need your help to enhance our visibility, so that our platform continues to serve you.
Sialic acids and viruses
ethicseido.com
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📃Scientific paper: Sialic acids and viruses Abstract: Let us study viruses and the role of sialic acids in their first step of reproduction, the attachment to cells. We begin our study with the help of the "Earth's virology course", created by Vincent Racaniello, with David Tuller and Gertrud U. Rey. The first virus that we will study is that of influenza A. Actually, "Earth's virology course" is a proper starting point for learning the mechanisms the virus uses to attach and enter the host cells. In the case of the influenza virus, its spike protein is used to attach the virion to sialic acid receptors of the host cells. Then, we will consider coronaviruses, with the help of literature about the role of sialic acids in their attachment by means of spike proteins. In fact, there are seven human coronavirus and they use sialic acid or angiotensin-converting enzyme 2 (ACE2) or other receptors or a combination of them. Let us review the literature to understand if Sars-Cov-2 virus can use sialic acid for the attachment to cells or not. Its main target is considered the ACE2 receptor. We will see that a study exists which detected that Sars-Cov-2 protein molecules can bind to heparan sulfate glycans in a sulfation-dependent manner. ;About the role of sialic acids in Sars-Cov-2 attachment: a) the study in 10.1021/acscentsci.0c00855 used a glyco-nanoparticle platform, discovering that N-acetyl neuraminic acid has affinity toward the SARS-COV-2 spike glycoprotein, that is a glycan-binding function. b) a recent study, 1... Continued on ES/IODE ➡️ https://etcse.fr/endsj ------- If you find this interesting, feel free to follow, comment and share. We need your help to enhance our visibility, so that our platform continues to serve you.
Sialic acids and viruses
ethicseido.com
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Delighted to share our new review paper titled "Viral deubiquitinating proteases and the promising strategies of their inhibition", published last week in Virus Research as part of the Nidoviruses special issue! In this review, we discuss the viral proteases with deubiquitinating activity known to date, their importance in viral replication and innate immune evasion, as well as ways in which we might inhibit such proteases to fight these viruses. Thanks to the co-authors for their contribution!
Viral deubiquitinating proteases and the promising strategies of their inhibition
sciencedirect.com
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