Results 21 to 30 of about 5,845 (181)

Swine acute diarrhoea syndrome coronavirus (SADS-CoV) Nsp5 antagonizes type I interferon signaling by cleaving DCP1A [PDF]

open access: yesFrontiers in Immunology, 2023
Swine acute diarrhoea syndrome coronavirus (SADS-CoV), which is a recently discovered enteric coronavirus, is the major aetiological agent that causes severe clinical diarrhoea and intestinal pathological damage in pigs, and it has caused significant ...
Hai-xin Huang   +12 more
doaj   +2 more sources

Porcine Deltacoronavirus nsp5 Cleaves DCP1A To Decrease Its Antiviral Activity [PDF]

open access: yesJournal of Virology, 2020
Interferon (IFN)-stimulated gene (ISG) induction through IFN signaling is important to create an antiviral state and usually directly inhibits virus infection. The present study first demonstrated that PDCoV nsp5 can cleave mRNA-decapping enzyme 1a (DCP1A) to attenuate its antiviral activity.
Jiyao Chen, Yanrong Zhou, Shangen Xu
exaly   +3 more sources

Involvement of PRRSV NSP3 and NSP5 in the autophagy process

open access: yesVirology Journal, 2019
Background Autophagy is an essential process in eukaryotic cells in which autophagosomes form to deliver cellular organelles and long-lived proteins to lysosomes for degradation. Many studies have recently identified the regulatory mechanisms involved in
Wei Zhang   +4 more
doaj   +3 more sources

PRRSV evades innate immune cGAS-STING antiviral function via its Nsp5 to deter STING translocation and activation [PDF]

open access: yesVirulence
Porcine Reproductive and Respiratory Syndrome Virus (PRRSV) is an important pathogen that seriously endangers pig breeding, causing significant economic losses to the global swine industry.
Yulin Xu   +11 more
doaj   +2 more sources

A structural roadmap for the formation of the coronavirus nsp3/nsp4 double membrane vesicle pore and its implications for polyprotein processing and replication/transcription [PDF]

open access: yesJournal of Virology
Coronavirus replication is understood to occur within double membrane vesicles (DMVs) that arise during viral infection. Prior work has determined that these DMVs have characteristic pores formed from the non-structural viral proteins nsp3 and nsp4 ...
Jason K. Perry   +3 more
doaj   +2 more sources

The P132H mutation of SARS-CoV-2 NSP5 relieves its inhibition on interferon-β activation via blocking MAVS degradation [PDF]

open access: yesCellular and Molecular Life Sciences
The prevalence of the Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an important transition in the epidemic of coronavirus disease 2019 (COVID-19).
Yuxin Zhang   +8 more
doaj   +2 more sources

Rotavirus Nonstructural Protein NSP5 Interacts with Major Core Protein VP2 [PDF]

open access: yesJournal of Virology, 2003
ABSTRACTRotavirus is a nonenveloped virus with a three-layered capsid. The inner layer, made of VP2, encloses the genomic RNA and two minor proteins, VP1 and VP3, with which it forms the viral core. Core assembly is coupled with RNA viral replication and takes place in definite cellular structures termed viroplasms.
Berois, Mabel   +4 more
openaire   +5 more sources

The hope and hype of ellagic acid and urolithins as ligands of SARS-CoV-2 Nsp5 and inhibitors of viral replication

open access: yesJournal of Enzyme Inhibition and Medicinal Chemistry, 2023
Non-structural protein 5 (Nsp5) is a cysteine protease that plays a key role in SARS-CoV-2 replication, suppressing host protein synthesis and promoting immune evasion.
Elisa Bianconi   +11 more
doaj   +2 more sources

Comparative analysis of NSP5/VP2-induced viroplasm-like structures in rotavirus species A to J [PDF]

open access: yesJournal of Virology
Rotavirus (RV) is classified into nine species, A–D and F–J, with RV species A (RVA) being the most extensively studied. While RVA infects infants and young animals, non-RVA species infect adult humans, various mammals, and birds.
Ariana Cosic   +5 more
doaj   +2 more sources

Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2.

open access: yesJournal of General Virology, 1998
We have previously shown that a number of isoforms of the non-structural rotavirus protein NSP5 are found in virus-infected cells. These isoforms differ in their level of phosphorylation which, at least in part, appears to occur through autophosphorylation. NSP5 co-localizes with another non-structural protein, NSP2, in the viroplasms of infected cells
I, Afrikanova   +3 more
openaire   +3 more sources

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