Results 61 to 70 of about 283 (118)

Ligand-induced Dimerization of Middle East Respiratory Syndrome (MERS) Coronavirus nsp5 Protease (3CLpro): IMPLICATIONS FOR nsp5 REGULATION AND THE DEVELOPMENT OF ANTIVIRALS.

The Journal of biological chemistry, 2015
All coronaviruses, including the recently emerged Middle East respiratory syndrome coronavirus (MERS-CoV) from the β-CoV subgroup, require the proteolytic activity of the nsp5 protease (also known as 3C-like protease, 3CL(pro)) during virus replication, making it a high value target for the development of anti-coronavirus therapeutics.
Tomar, Sakshi, Johnston, Melanie L., St. John, Sarah E., Osswald, Heather L., Nyalapatla, Prasanth R., Paul, Lake N., Ghosh, Arun K., Denison, Mark R., Mesecar, Andrew D.   +8 more
openaire   +2 more sources

PDCoV NSP5 cleaves the selective autophagy receptor CCDC50 to disrupt autophagic degradation of the viral envelope protein

mBio
Selective autophagy is a critical host defense mechanism that eliminates viral components through lysosomal degradation during coronavirus infection. Coronaviruses (CoVs), however, deploy countermeasures that disrupt this process, and several underlying ...
Ke Li, Hongyun Wei, Kangli Zhao, Dong Chen, Yu Sun, Peng Zhou, Hui Jin, Anan Jongkaewwattana, Sizhu Suolang, Dang Wang, Hongbo Zhou, Rui Luo   +11 more
doaj   +1 more source

Extending the Targets for Coronavirus Antivirals Beyond That of Approved Drugs: Insights From Preclinical Research

Microbial Biotechnology, Volume 19, Issue 5, May 2026.
Chemical structure of RIBOTAC inhibitor with metabolic handle binding as nucleotide analogue to SARS‐CoV‐2 RNA dependent RNA polymerase, its linker and the RNase L recruiter which binds RNase L monomers and mediates their dimerization that actives nuclease activity degrading the viral RNA.
Harald Brüssow
wiley   +1 more source

The Open Reading Frame 7b of the SARS‐CoV‐2 Disperse Trans‐Golgi and Activate the NLRP3 Inflammasome

Journal of Medical Virology, Volume 98, Issue 4, April 2026.
ABSTRACT Inflammasomes orchestrate the inflammatory response against bacterial and viral infections, thereby initiating the synthesis of pro‐inflammatory cytokines, mainly IL‐1β and IL‐18. SARS‐CoV‐2 infection induces an inflammatory response mediated by the activation of NLRP1 and NLRP3 inflammasomes.
Julio García‐Villalba, Laura Hurtado‐Navarro, Diego Angosto‐Bazarra, Alberto Baroja‐Mazo, Pablo Pelegrin   +4 more
wiley   +1 more source

Effects of intrabodies specific for rotavirus NSP5 during the virus replicative cycle

Journal of General Virology, 2004
Intracellular antibodies or intrabodies (ICAbs) have great potential in protein knockout strategies for intracellular antigens. In this study, they have been used to investigate the role of the rotavirus non-structural protein NSP5 in the virus replication cycle. Intracellular antibody-capture technology was used to select single-chain Fv format (scFv)
VASCOTTO F, CAMPAGNA M, VISINTIN M, CATTANEO, ANTONINO, BURRONE OR   +4 more
openaire   +4 more sources

Phosphorylation tunes strain-specific protein condensation during rotavirus replication organelle assembly

The EMBO Journal
In many viruses, intrinsically disordered proteins (IDPs) drive the formation of replicative organelles via liquid–liquid phase separation (LLPS). In species A rotaviruses, the disordered protein NSP5 forms condensates with NSP2, but its high sequence ...
Julia Acker, Xinyu Wang, Alonso J Pardal, Daniel Desirò, Tanushree Agarwal, Alice Colyer, Aidan Tollervey, Rob Scrutton, Cyril Haller, Lee Sherry, Kadi L Saar, Ksenia Fominykh, Margaret L L Y Johncock, Sai Hou Chong, Rosie Murray, Jamie Terry, Jeremy D Schmit, Antonio N Calabrese, Tuomas P J Knowles, Alexander Borodavka   +19 more
doaj   +1 more source

Interaction of Rotavirus Polymerase VP1 with Nonstructural Protein NSP5 Is Stronger than That with NSP2 [PDF]

Journal of Virology, 2007
ABSTRACT Rotavirus morphogenesis starts in intracellular inclusion bodies called viroplasms. RNA replication and packaging are mediated by several viral proteins, of which VP1, the RNA-dependent RNA polymerase, and VP2, the core scaffolding protein, were shown to be sufficient to provide replicase activity in vitro.
ARNOLDI, Francesca, M. Campagna, C. Eichwald, U. Desselberger, O. R. Burrone   +4 more
openaire   +4 more sources

Liquid–Liquid Phase Separation in Viral Infection and Immunology

MedComm, Volume 7, Issue 4, April 2026.
LLPS organizes viral replication and antiviral immunity. Viruses hijack LLPS to form replication factories and evade immune sensors, while hosts assemble LLPS‐driven signaling hubs (e.g., MAVS, RIG‐I, and SGs) to amplify interferon responses. Targeting these condensate interfaces offers novel therapeutic strategies against infectious diseases ...
Jiuzhi Xu, Lan Bai, Bin Wang, Hai Song, Long Zhang, Fangfang Zhou   +5 more
wiley   +1 more source

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

Cellular 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, Tong-Yun Wang, Huihui Yan, Zhoule Guo, Zhonghao Lian, Hailan Yao, Shuofeng Yuan, Xing-Yi Ge, Ye Qiu   +8 more
doaj   +1 more source

Antivirals Targeting Coronavirus RNA‐Dependent RNA Polymerase and Main Protease: From Mechanisms of Action to Outcomes in COVID‐19 Clinical Trials

Microbial Biotechnology, Volume 19, Issue 4, April 2026.
The target sites of COVID‐19 antivirals discussed in the present opinion paper, namely the RNA dependent RNA polymerase Nsp12 and of the main viral protease Nsp5, are indicated by a red star in the overview of the replication cycle of coronavirus SARS‐CoV‐2.
Harald Brüssow
wiley   +1 more source