Redefining NSP12 activity in SARS-CoV-2 and its regulation by NSP8 and NSP7 [PDF]
RdRp is a critical component of an RNA virus life cycle. Among coronaviruses, NSP12, along with one copy of NSP7 and two copies of NSP8, forms the RdRp holoenzyme and exhibits polymerase activity. While coronavirus RNA replication is sufficiently understood, the interplay among these NSPs and its influence on RNA binding and nascent strand synthesis ...
Krishna K Inampudi
exaly +5 more sources
Cellular eEF1G Inhibits Porcine Deltacoronavirus Replication by Binding Nsp12 and Disrupting Its Interaction with Viral Genomic RNA [PDF]
Porcine deltacoronavirus (PDCoV) is an emerging pathogen that causes severe, often fatal, diarrhea in suckling piglets and has zoonotic potential. Its nonstructural protein 12 (Nsp12), functioning as the RNA-dependent RNA polymerase (RdRp), is a central ...
Xin Guo +6 more
core +4 more sources
Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors [PDF]
Recent history is punctuated by the emergence of highly pathogenic coronaviruses such as SARS- and MERS-CoV into human circulation. Upon infecting host cells, coronaviruses assemble a multi-subunit RNA-synthesis complex of viral non-structural proteins (NSP) responsible for the replication and transcription of the viral genome. Here, we present the 3.1
Robert N Kirchdoerfer +2 more
exaly +4 more sources
The SARS-CoV nsp12 Polymerase Active Site Is Tuned for Large-Genome Replication
Positive-strand RNA viruses replicate their genomes using virally encoded RNA-dependent RNA polymerases (RdRP) with a common active-site structure and closure mechanism upon which replication speed and fidelity can evolve to optimize virus fitness ...
Campagnola, Grace +10 more
core +4 more sources
Lycorine Derivative Inhibits SARS‐CoV‐2 Replication by Reducing −1 Programmed Ribosomal Frameshifting via Targeting ZAP [PDF]
The present study evaluated the antiviral potential of various lycorine derivatives and identified compound 7 as a promising candidate. Compound 7 demonstrated strong antiviral efficacy against both the original SARS‐CoV‐2 and its variants in vitro and in vivo.
Tingfu Du +11 more
wiley +2 more sources
Arsenic trioxide could promote SARS-CoV-2 NSP12 protein degradation [PDF]
The global dissemination and infection of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have become a worldwide crisis with staggering confirmed cases and death tolls. Although prophylactic vaccines are widely applied to curb the spread of the virus, these protections are greatly weakened by the emergence of SARS-CoV-2 variants.
Yang, Tao +4 more
openaire +4 more sources
Investigation of protein-protein interactions and hotspot region on the NSP7-NSP8 binding site in NSP12 of SARS-CoV-2 [PDF]
Background: The RNA-dependent RNA polymerase (RdRp) complex, essential in viral transcription and replication, is a key target for antiviral therapeutics.
Shopnil Akash +11 more
core +4 more sources
Preclinical Screening Platform Identifies Azatadine‐Dimaleate as a Potent Repurposed Therapeutic Against SARS‐CoV‐2 Infection [PDF]
ABSTRACT The emergence of SARS‐CoV‐2 posed a major global public health threat, necessitating urgent development of therapeutics. Despite vaccine availability, continuous emergence of viral variants with enhanced transmissibility and immune escape capabilities, and consequential impacts on health services, requires effective antiviral therapeutics ...
Ahlam Ali +13 more
wiley +2 more sources
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) replication depends on the NSP12-NSP8-NSP7 complex, which plays a critical role in enhancing RNA-dependent RNA polymerase (RdRp) activity. NSP8 is particularly essential, stabilizing the RdRp complex and supporting viral replication across diverse variants. To disrupt this crucial interaction,
Seong Cheol Min, Young Ki Choi
exaly +4 more sources
SARS-CoV-2 NSP3/4 control formation of replication organelle and recruitment of RNA polymerase NSP12 [PDF]
β-coronavirus rearranges the host cellular membranes to form double-membrane vesicles (DMVs) via NSP3/4, which anchor replication–transcription complexes (RTCs), thereby constituting the replication organelles (ROs). However, the impact of specific domains within NSP3/4 on DMV formation and RO assembly remains largely unknown.
Jinping Yang +14 more
openaire +3 more sources

