Results 41 to 50 of about 5,845 (181)

A Gain-of-Function Cleavage of TonEBP by Coronavirus NSP5 to Suppress IFN-β Expression

Cells
Human coronaviruses (HCoVs) modify host proteins to evade the antiviral defense and sustain viral expansion. Here, we report tonicity-responsive enhancer (TonE) binding protein (TonEBP) as a cellular target of HCoVs.
Hyun Park, Sang Min Lee, Su Ji Jeong, Yeong Cheon Kweon, Go Woon Shin, Whi Young Kim, Whaseon Lee-Kwon, Chan Young Park, Hyug Moo Kwon   +8 more
doaj   +3 more sources

Porcine deltacoronavirus nsp5 antagonizes type I interferon signaling by cleaving IFIT3

Journal of Virology
Porcine deltacoronavirus (PDCoV) is a potential emerging zoonotic pathogen, and studies on the prevalence and pathogenesis of PDCoV are ongoing. The main protease (nsp5) of PDCoV provides an excellent target for antivirals due to its essential and conserved function in the viral replication cycle.
Haixin Huang, Wenchao Sun
exaly   +3 more sources

Functional studies on the rotavirus non-structural proteins NSP5 and NSP6 [PDF]

The rotavirus replication cycle has not been fully characterised, one vital\ud stage of virus replication involves large cytoplasmic occlusion bodies termed\ud viroplasms. These are the sites of synthesis and replication of dsRNA, packaging of\ud viral RNA into newly synthesized cores and the formation of double-shelled previrions.\ud The detailed ...
Rainsford, Edward
openaire   +1 more source

Transient SARS-CoV-2 RNA-Dependent RNA Polymerase Mutations after Remdesivir Treatment for Chronic COVID-19 in Two Transplant Recipients: Case Report and Intra-Host Viral Genomic Investigation

Microorganisms, 2023
Remdesivir is the first FDA-approved drug for treating severe SARS-CoV-2 infection and targets RNA-dependent RNA polymerase (RdRp) that is required for viral replication.
Shangxin Yang, Ashrit Multani, Jacob M. Garrigues, Michael S. Oh, Peera Hemarajata, Taylor Burleson, Nicole M. Green, Caspian Oliai, Pryce T. Gaynor, Omer E. Beaird, Drew J. Winston, Christopher S. Seet, Joanna M. Schaenman   +12 more
doaj   +1 more source

Studies on rotavirus NSP5 phosphorylation and its interaction with NSP2 [PDF]

, 2003
Rotavirus NSP5 is a non-structural protein that localises in cytoplasmic viroplasms of infected cells. NSP5 interacts with NSP2 and undergoes a complex posttranslational hyper-phosphorylation , generating species with reduced PAGE mobility. This process has been suggested to be due in part to autophosphorylation.
Eichwald, Catherine
openaire   +2 more sources

Analysis of Rotavirus Nonstructural Protein NSP5 Phosphorylation [PDF]

Journal of Virology, 1998
ABSTRACT The rotavirus nonstructural phosphoprotein NSP5 is encoded by a gene in RNA segment 11. Immunofluorescence analysis of fixed cells showed that NSP5 polypeptides remained confined to viroplasms even at a late stage when provirions migrated from these structures.
J, Blackhall, M, Muñoz, A, Fuentes, G, Magnusson   +3 more
openaire   +2 more sources

Gold-Based Metal Drugs as Inhibitors of Coronavirus Proteins: The Inhibition of SARS-CoV-2 Main Protease by Auranofin and Its Analogs

Biomolecules, 2022
Gold compounds have a long tradition in medicine and offer many opportunities for new therapeutic applications. Herein, we evaluated the lead compound Auranofin and five related gold(I) complexes as possible inhibitors of SARS-CoV-2 Main Protease (SARS ...
Lara Massai, Deborah Grifagni, Alessia De Santis, Andrea Geri, Francesca Cantini, Vito Calderone, Lucia Banci, Luigi Messori   +7 more
doaj   +1 more source

In vitro and in vivo characterization of SARS-CoV-2 resistance to ensitrelvir

Nature Communications, 2023
Ensitrelvir, an oral antiviral agent that targets a SARS-CoV-2 main protease (3CLpro or Nsp5), is clinically useful against SARS-CoV-2 including its omicron variants.
Maki Kiso, Seiya Yamayoshi, Shun Iida, Yuri Furusawa, Yuichiro Hirata, Ryuta Uraki, Masaki Imai, Tadaki Suzuki, Yoshihiro Kawaoka   +8 more
doaj   +1 more source

An attenuated herpesvirus vectored vaccine candidate induces T-cell responses against highly conserved porcine reproductive and respiratory syndrome virus M and NSP5 proteins that are unable to control infection

Frontiers in Immunology, 2023
Porcine reproductive and respiratory syndrome virus (PRRSV) remains a leading cause of economic loss in pig farming worldwide. Existing commercial vaccines, all based on modified live or inactivated PRRSV, fail to provide effective immunity against the ...
Rory C. F. de Brito, Kerry Holtham, Jessica Roser, Jack E. Saunders, Jack E. Saunders, Yvonne Wezel, Summer Henderson, Thekla Mauch, Beatriz Sanz-Bernardo, Jean-Pierre Frossard, Matthieu Bernard, Fabian Z. X. Lean, Alejandro Nunez, Simon Gubbins, Nicolás M. Suárez, Andrew J. Davison, Michael J. Francis, Michael Huether, Hafid Benchaoui, Jeremy Salt, Veronica L. Fowler, Michael A. Jarvis, Michael A. Jarvis, Simon P. Graham   +23 more
doaj   +1 more source

Hyperphosphorylation of the Rotavirus NSP5 Protein Is Independent of Serine 67 or NSP2, and the Intrinsic Insolubility of NSP5 Is Regulated by Cellular Phosphatases [PDF]

Journal of Virology, 2006
ABSTRACT The NSP5 protein is required for viroplasm formation during rotavirus infection and is hyperphosphorylated into 32- to 35-kDa isoforms. Earlier studies reported that NSP5 is not hyperphosphorylated without NSP2 coexpression or deleting the NSP5 N terminus and that serine 67 is essential for NSP5 hyperphosphorylation.
Adrish, Sen, Darin, Agresti, Erich R, Mackow   +2 more
openaire   +2 more sources