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MeSH Disease

HGNC Genes

SARS-CoV-2 proteins

NSP16 (14)

NSP3 (5)

ProteinS (4)

ComplexRdRp (4)

NSP15 (4)


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    How the replication and transcription complex of SARS-CoV-2 functions in leader-to-body fusion

    Authors: Xin Li; Qiang Zhao; Jia Chang; Guangyou Duan; Jinlong Bei; Tung On Yau; Jianyi Yang; Jishou Ruan; Bingjun He; Gao Shan

    doi:10.1101/2021.02.17.431652 Date: 2021-02-17 Source: bioRxiv

    Background: Coronavirus disease 2019 MESHD ( COVID-19 MESHD) is caused by severe acute respiratory syndrome coronavirus 2 MESHD (SARS-CoV-2). Although unprecedented efforts are underway to develop therapeutic strategies against this disease, scientists have acquired only a little knowledge regarding the structures and functions of the CoV replication and transcription complex (RTC) and 16 non-structural proteins, named NSP1 HGNC-16. Results: In the present study, we determined the theoretical arrangement of NSP12 PROTEIN-16 in the global RTC structure. This arrangement answered how the CoV RTC functions in the "leader-to-body fusion" process. More importantly, our results revealed the associations between multiple functions of the RTC, including RNA synthesis, NSP15 PROTEIN cleavage, RNA methylation, and CoV replication and transcription at the molecular level. As the most important finding, transcription regulatory sequence (TRS) hairpins were reported for the first time to help understand the multiple functions of CoV RTCs and the strong recombination abilities of CoVs. Conclusions: TRS hairpins can be used to identify recombination regions in CoV genomes. We provide a systematic understanding of the structures and functions of the RTC, leading to the eventual determination of the global CoV RTC structure. Our findings enrich fundamental knowledge in the field of gene expression and its regulation, providing a basis for future studies. Future drug design targeting SARS-CoV-2 needs to consider protein-protein and protein-RNA interactions in the RTC, particularly the complex structure of NSP15 PROTEIN and NSP16 PROTEIN with the TRS hairpin.

    SARS-CoV-2 Nsp16 activation mechanism and a cryptic pocket with pan-coronavirus antiviral potential

    Authors: Neha Vithani; Michael D Ward; Maxwell I Zimmerman; Borna Novak; Jonathan H. Borowsky; Sukrit Singh; Gregory R. Bowman; Guangyong Zheng; Guoping Zhao; Yixue Li; Zefeng Wang; Guoqing Zhang; Johan Neyts; Anthony Kelleher; Warwick Britton; Stuart Turville; James A Triccas

    doi:10.1101/2020.12.10.420109 Date: 2020-12-10 Source: bioRxiv

    Coronaviruses have caused multiple epidemics in the past two decades, in addition to the current COVID-19 pandemic MESHD that is severely damaging global health and the economy. Coronaviruses employ between twenty and thirty proteins to carry out their viral replication cycle including infection, immune evasion, and replication. Among these, nonstructural protein 16 PROTEIN (Nsp16), a 2-O-methyltransferase, plays an essential role in immune evasion. Nsp16 achieves this by mimicking its human homolog, CMTr1 HGNC, which methylates mRNA to enhance translation efficiency and distinguish self from other. Unlike human CMTr1 HGNC, Nsp16 requires a binding partner, Nsp10, to activate its enzymatic activity. The requirement of this binding partner presents two questions that we investigate in this manuscript. First, how does Nsp10 activate Nsp16? While experimentally-derived structures of the active Nsp16/Nsp10 complex exist, structures of inactive, monomeric Nsp16 have yet to be solved. Therefore, it is unclear how Nsp10 activates Nsp16. Using over one millisecond of molecular dynamics simulations of both Nsp16 and its complex with Nsp10, we investigate how the presence of Nsp10 shifts Nsp16s conformational ensemble in order to activate it. Second, guided by this activation mechanism and Markov state models (MSMs), we investigate if Nsp16 adopts inactive structures with cryptic pockets that, if targeted with a small molecule, could inhibit Nsp16 by stabilizing its inactive state. After identifying such a pocket in SARS-CoV-2 Nsp16, we show that this cryptic pocket also opens in SARS-CoV-1 and MERS, but not in human CMTr1 HGNC. Therefore, it may be possible to develop pan-coronavirus antivirals that target this cryptic pocket. Statement of SignificanceCoronaviruses are a major threat to human health. These viruses employ molecular machines, called proteins, to infect host MESHD cells and replicate. Characterizing the structure and dynamics of these proteins could provide a basis for designing small molecule antivirals. In this work, we use computer simulations to understand the moving parts of an essential SARS-CoV-2 protein, understand how a binding partner turns it on and off, and identify a novel pocket that antivirals could target to shut this protein off. The pocket is also present in other coronaviruses but not in the related human protein, so it could be a valuable target for pan-coronavirus antivirals.

    Gene Expression Meta-Analysis Identifies Molecular Changes Associated with SARS-CoV Infection in Lungs

    Authors: Amber Park; Laura Harris; Tanushka Doctor; Neda Nasheri; Hua Wang; Xuemei Feng; Gennadiy Zelinskyy; Mirko Trilling; Kathrin Sutter; Mengji Lu; Baoju Wang; Dongliang Yang; Xin Zheng; Jia Liu; Davey Smith; Daniela Weiskopf; Alessandro Sette; Shane Crotty; Jian Jin; Xian Chen; Andrew Pekosz; Sabra Klein; Irina Burd

    doi:10.1101/2020.11.14.382697 Date: 2020-11-16 Source: bioRxiv

    Background: Severe Acute Respiratory Syndrome MESHD (SARS) corona virus ( SARS-CoV) infections MESHD are a serious public health threat because of their pandemic-causing potential. This work uses mRNA expression data to predict genes associated with SARS-CoV infection MESHD through an innovative meta-analysis examining gene signatures (i. e., gene PROTEIN lists ranked by differential gene expression between SARS and mock infection MESHD). Methods: This work defines 29 gene signatures representing SARS infection MESHD across seven strains with established mutations that vary virulence (infectious clone SARS (icSARS), Urbani, MA15, {Delta} ORF6 PROTEIN, BAT-SRBD, {Delta} NSP16 PROTEIN, and ExoNI) and host (human lung cultures and/or mouse lung samples) and examines them through Gene Set Enrichment Analysis (GSEA). To do this, first positive and negative icSARS gene panels were defined from GSEA-identified leading-edge genes between 500 genes from positive or negative tails of the GSE47960-derived icSARSvsmock signature and the GSE47961-derived icSARSvsmock signature, both from human cultures. GSEA then was used to assess enrichment and identify leading-edge icSARS panel genes in the other 27 signatures. Genes associated with SARS-CoV infection MESHD are predicted by examining membership in GSEA-identified leading-edges across signatures. Results: Significant enrichment (GSEA p<0.001) was observed between GSE47960-derived and GSE47961-derived signatures, and those leading-edges defined the positive (233 genes) and negative (114 genes) icSARS panels. Non-random (null distribution p<0.001) significant enrichment (p<0.001) was observed between icSARS panels and all verification icSARSvsmock signatures derived from human cultures, from which 51 over- and 22 under-expressed genes were shared across leading-edges with 10 over-expressed genes already being associated with icSARS infection MESHD. For the icSARSvsmock mouse signature, significant, non-random enrichment (both p<0.001) held for only the positive icSARS panel, from which nine genes were shared with icSARS infection MESHD in human cultures. Considering other SARS strains, significant (p<0.01), non-random (p<0.002) enrichment was observed across signatures derived from other SARS strains for the positive icSARS panel. Five positive icSARS panel genes, CXCL10, OAS3, OASL, IFIT3, and XAF1, were found in mice and human signatures. Conclusion: The GSEA-based meta-analysis approach used here identified genes with and without reported associations with SARS-CoV infections MESHD, highlighting this approachs predictability and usefulness in identifying genes that have potential as therapeutic targets to preclude or overcome SARS infections MESHD.

    A high throughput RNA displacement assay for screening SARS-CoV-2 nsp10-nsp16 PROTEIN complex towards developing therapeutics for COVID-19 MESHD

    Authors: Sumera Perveen; Aliakbar Khalili Yazdi; Kanchan Devkota; Fengling Li; Pegah Ghiabi; Taraneh Hajian; Peter Loppnau; Albina Bolotokova; Masoud Vedadi; Srinivas Murthy; Marie-Pierre Preziosi; Srinath Reddy; Mirta Roses; Vasee Sathiyamoorthy; John-Arne Rottingen; Soumya Swaminathan; Qingyuan Yang; David Hines; William Clarke; Richard Eric Rothman; Andrew Pekosz; Katherine Fenstermacher; Zitong Wang; Scott L Zeger; Antony Rosen

    doi:10.1101/2020.10.14.340034 Date: 2020-10-15 Source: bioRxiv

    SARS-CoV-2, the coronavirus that causes COVID-19 MESHD, evades the human immune system by capping its RNA. This process protects the viral RNA and is essential for its replication. Multiple viral proteins are involved in this RNA capping process including the nonstructural protein 16 PROTEIN (nsp16) which is an S-adenosyl-L-methionine (SAM)-dependent 2'-O-methyltransferase. Nsp16 is significantly active when in complex with another nonstructural protein, nsp10, which plays a key role in its stability and activity. Here we report the development of a fluorescence polarization (FP)-based RNA displacement assay for nsp10-nsp16 PROTEIN complex in 384-well format with a Z'-Factor of 0.6, suitable for high throughput screening. In this process, we purified the nsp10-nsp16 PROTEIN complex to higher than 95% purity and confirmed its binding to the methyl donor SAM, product of the reaction, SAH MESHD, and a common methyltransferase inhibitor, sinefungin using Isothermal Titration Calorimetry (ITC). The assay was further validated by screening a library of 1124 drug-like compounds. This assay provides a cost-effective high throughput method for screening nsp10-nsp16 PROTEIN complex for RNA-competitive inhibitors towards developing COVID-19 MESHD therapeutics.

    Global BioID-based SARS-CoV-2 proteins proximal interactome unveils novel ties between viral polypeptides and host factors involved in multiple COVID19 MESHD-associated mechanisms

    Authors: Estelle MN Laurent; Yorgos Sofianatos; Anastassia Komarova; Jean-Pascal Gimeno; Payman Samavarchi Tehrani; Dae-Kyum Kim; Hala Abdouni; Marie Duhamel; Patricia Cassonnet; Jennifer J Knapp; Da Kuang; Aditya Chawla; Dayag Sheykhkarimli; Ashyad Rayhan; Roujia Li; Oxana Pogoutse; David E Hill; Mike E Calderwood; Pascal Falter-Braun; Patrick Aloy; Ulrich Stelzl; Marc Vidal; Anne-Claude Gingras; Georgios A Pavlopoulos; Sylvie Van Der Werf; Isabelle Fournier; Frederick P Roth; Michel Salzet; Caroline Demeret; Yves Jacob; Etienne Coyaud; Joseph Newman; Amin S Asfor; Alison Burman; Sylvia Crossley; John Hammond; Elma Tchilian; Bryan Charleston; Dalan Bailey; Tobias J Tuthill; Simon Graham; Tomas Malinauskas; Jiandong Huo; Julia Tree; Karen Buttigieg; Ray Owens; Miles Carroll; Rod Daniels; John McCauley; Kuan-Ying A Huang; Mark Howarth; Alain Townsend

    doi:10.1101/2020.08.28.272955 Date: 2020-08-29 Source: bioRxiv

    The worldwide SARS-CoV-2 outbreak poses a serious challenge to human societies and economies. SARS-CoV-2 proteins orchestrate complex pathogenic mechanisms that underlie COVID-19 MESHD disease. Thus, understanding how viral polypeptides rewire host protein networks enables better-founded therapeutic research. In complement to existing proteomic studies, in this study we define the first proximal interaction network of SARS-CoV-2 proteins, at the whole proteome level in human cells. Applying a proximity-dependent biotinylation (BioID)-based approach greatly expanded the current knowledge by detecting interactions within poorly soluble compartments, transient, and/or of weak affinity in living cells. Our BioID study was complemented by a stringent filtering and uncovered 2,128 unique cellular targets (1,717 not previously associated with SARS-CoV-1 or 2 proteins) connected to the N- and C-ter BioID-tagged 28 SARS-CoV-2 proteins by a total of 5,415 (5,236 new) proximal interactions. In order to facilitate data exploitation, an innovative interactive 3D web interface was developed to allow customized analysis and exploration of the landscape of interactions (accessible at http://www.sars-cov-2-interactome.org/). Interestingly, 342 membrane proteins including interferon and interleukin pathways factors, were associated with specific viral proteins. We uncovered ORF7a PROTEIN and ORF7b PROTEIN protein proximal partners that could be related to anosmia and ageusia symptoms. Moreover, comparing proximal interactomes in basal and infection-mimicking conditions (poly(I:C) treatment) allowed us to detect novel links with major antiviral response pathway components, such as ORF9b PROTEIN with MAVS HGNC and ISG20 HGNC; N with PKR HGNC and TARB2; NSP2 PROTEIN NSP2 HGNC with RIG-I HGNC and STAT1 HGNC; NSP16 PROTEIN with PARP9 HGNC- DTX3L HGNC. Altogether, our study provides an unprecedented comprehensive resource for understanding how SARS-CoV-2 proteins orchestrate host proteome remodeling and innate immune response evasion, which can inform development of targeted therapeutic strategies.

    Virion Structure and Mechanism of Propagation of Coronaviruses including SARS-CoV 2 (COVID -19 ) and some Meaningful Points for Drug or Vaccine Development

    Authors: Swapan Ghosh

    id:10.20944/preprints202008.0312.v1 Date: 2020-08-14 Source: Preprints.org

    SARS-CoV-2 or COVID-19 MESHD, a new seventh human corona virus, has out-broken in Wuhan, China since 31st December 2019, and quickly escalated to take the form of pandemic which killed many human beings throughout almost all countries across continents. The rapidity of its transmission from human to human is far greater than all previous human corona viruses which came into existence like SARS-CoV MESHD, MERS-CoV, etc. The nucleotide sequence of SARS-CoV-2 (isolates Wuhan-Hu-1) is 29,875 bp in ss-RNA. Symptoms of SARS-CoV-2 infected pneumonia MESHD include from asymptomatic to high fever and/or respiratory illnesses. Coronavirus virion (spherical/round /elliptical in shape) consists of three parts- outer membrane or envelope, nucleocapsid and genome (RNA). SARS-CoV-2 was shown to use receptor, angiotensin converting enzyme 2 HGNC ( ACE2 HGNC) for attachment to the cells through its surface spike (S) protein PROTEIN (S1), and the virion enters into the host cell through two routes- direct membrane fusion and endocytotic pathway. The RNA of SARS-CoV acts MESHD directly as mRNA and here minus(-) 1 programmed ribosomal frameshift (-1PRF) is being operated by slippery sequence and pseudoknot, so it translates 16 nonstructural proteins PROTEIN including RNA dependent RNA replicase. Then genomic RNA replicated continuously on – strand RNA template and subgenomic RNA transcribed discontinuously on –RNA template to sgmRNA. Subgenomic RNAs/sgmRNAs synthesize all structural proteins. This article takes into consideration the details of established theories of viral structure, viral attachment, mode of entry into human cells, different models of replication and transcription of virus genome proposed by eminent scientists over the years, and makes an in depth examination highlighting meaningful points or important target cites of viral propagation or synthesis, which are conserved, for prompt development of potent drugs or vaccine to counter COVID-19 MESHD for which human race is anxiously and eagerly waiting.

    A Combination of Ivermectin and Doxycycline Possibly Blocks the Viral Entry and Modulate the Innate Immune Response in COVID-19 MESHD Patients

    Authors: Dharmendra Kumar Maurya

    doi:10.26434/chemrxiv.12630539.v1 Date: 2020-07-09 Source: ChemRxiv

    The current outbreak of the corona virus disease 2019 ( COVID-19 MESHD), has affected almost entire world and become pandemic now. Currently, there is neither any FDA approved drugs nor any vaccines available to control it. Very recently in Bangladesh, a group of doctors reported astounding success in treating patients suffering from COVID-19 MESHD with two commonly used drugs, Ivermectin and Doxycycline. In the current study we have explored the possible mechanism by which these drugs might have worked for the positive response in the COVID-19 MESHD patients. To explore the mechanism we have used molecular docking and molecular dynamics simulation approach. Effectiveness of Ivermectin and doxycycline were evaluated against Main Protease PROTEIN ( Mpro PROTEIN), Spike (S) protein PROTEIN, Nucleocapsid (N PROTEIN), RNA-dependent RNA polymerase PROTEIN ( RdRp PROTEIN, NSP12 PROTEIN), ADP Ribose Phosphatase ( NSP3 HGNC NSP3 PROTEIN), Endoribonuclease ( NSP15 PROTEIN) and methyltransferase ( NSP10 PROTEIN- NSP16 PROTEIN complex) of SARS-CoV-2 as well as human angiotensin converting enzyme 2 HGNC ( ACE2 HGNC) receptor. Our study shows that both Ivermectin and doxycycline have significantly bind with SARS-CoV-2 proteins but Ivermectin was better binding than doxycycline. Ivermectin showed a perfect binding site to the Spike-RBD and ACE2 HGNC interacting region indicating that it might be interfering in the interaction of spike with ACE2 HGNC and preventing the viral entry in to the host cells. Ivermectin also exhibited significant binding affinity with different SARS-CoV-2 structural and non-structural proteins (NSPs) which have diverse functions in virus life cycle. Significant binding of Ivermectin with RdRp PROTEIN indicate its role in the inhibition of the viral replication and ultimately impeding the multiplication of the virus. Ivermectin also possess significant binding affinity with NSP3 HGNC NSP3 PROTEIN, NSP10 PROTEIN, NSP15 PROTEIN and NSP16 PROTEIN which helps virus in escaping from host immune system. Molecular dynamics simulation study shows that binding of the Ivermectin with Mpro PROTEIN, Spike, NSP3 HGNC NSP3 PROTEIN, NSP16 PROTEIN and ACE2 HGNC was quiet stable. Thus, our docking and simulation studies reveal that combination of Ivermectin and doxycycline might be executing the effect by inhibition of viral entry and enhance viral load clearance by targeting various viral functional proteins.

    Computational Investigation of Structural Dynamics of SARS-CoV-2 Methyltransferase-Stimulatory Factor Heterodimer Nsp16/nsp10 Bound to the Cofactor SAM

    Authors: Md Fulbabu Sk; Nisha Amarnath Jonniya; Rajarshi Roy; Sayan Poddar; Parimal Kar

    doi:10.26434/chemrxiv.12608795.v1 Date: 2020-07-06 Source: ChemRxiv

    Recently, a highly contagious novel coronavirus ( COVID-19 MESHD or SARS-CoV-2) has emerged as a global threat in people's health and global economies. Identification of the potential targets and development of a vaccine or antiviral drugs is an urgent demand. The 5’-capping mechanism of eukaryotic mRNA and some viruses such as coronaviruses (CoVs) are essential for maintaining the RNA stability, protein translation, and for viral immune escape. SARSCoV encodes S-adenosyl-L-methionine dependent (SAM) methyltransferase (MTase PROTEIN) enzyme characterized by nsp16 (2’-O-MTase PROTEIN) for generating the capped structure. The present article highlights the binding mechanisms of nsp16 and nsp10 PROTEIN to identify the role of nsp10 in MTase activity. Furthermore, the conformational dynamics and energetic behind the SAM binding to nsp16 in its monomer and dimer form was analyzed by using an extensive molecular dynamics simulation along with the Molecular Mechanics Poisson-Boltzmann Surface Area (MM/PBSA). Our results show that the presence of nsp10 increases the favorable van der Waal and electrostatic interactions between the SAM and nsp16, thus nsp10 PROTEIN acts as a stimulator for its strong binding. The interaction profile suggests that hydrophobic interactions were predominately identified for protein-protein interactions. Also, the stable hydrogen bond between Ala83 (nsp16) and Tyr96 (nsp10), and between Gln87 (nsp16) and Leu45 (nsp10) plays a vital role in the nsp16-nsp10 PROTEIN interface. Further, Computational Alanine Scanning ( CAS HGNC) mutagenesis was performed, which revealed hotspot mutants, namely I40A, V104A, and R86A for the dimer association. Therefore, the dimer interface of nsp16/nsp10 PROTEIN could also be a potential target to suppress the 2’-O-MTase activity of SARS-CoV-2. Overall, our study provides a comprehensive understanding of the dynamic and thermodynamic process of binding of nsp16 and nsp10 PROTEIN that will contribute to the novel design of peptide inhibitors based on nsp16.

    The enzymatic activity of the nsp14 exoribonuclease PROTEIN is critical for replication of Middle East respiratory syndrome-coronavirus

    Authors: Natacha S. Ogando; Jessika Zevenhoven-Dobbe; Clara C Posthuma; Eric J. Snijder

    doi:10.1101/2020.06.19.162529 Date: 2020-06-20 Source: bioRxiv

    AO_SCPLOWBSTRACTC_SCPLOWCoronaviruses (CoVs) stand out for their large RNA genome and complex RNA-synthesizing machinery comprising 16 nonstructural proteins PROTEIN (nsps). The bifunctional nsp14 contains an N-terminal 3-to-5 exoribonuclease PROTEIN (ExoN) and a C-terminal N7-methyltransferase (N7-MTase) domain. While the latter presumably operates during viral mRNA capping, ExoN is thought to mediate proofreading during genome replication. In line with such a role, ExoN-knockout mutants of mouse hepatitis virus MESHD (MHV) and severe acute respiratory syndrome coronavirus (SARS-CoV MESHD) were previously found to have a crippled but viable hypermutation phenotype. Remarkably, using an identical reverse genetics approach, an extensive mutagenesis study revealed the corresponding ExoN-knockout mutants of another betacoronavirus, Middle East respiratory syndrome coronavirus (MERS-CoV) MESHD, to be non-viable. This is in agreement with observations previously made for alpha- and gammacoronaviruses. Only a single MERS-CoV ExoN active site mutant could be recovered, likely because the introduced D191E substitution is highly conservative in nature. For 11 other MERS-CoV ExoN active site mutants, not a trace of RNA synthesis could be detected, unless - in some cases - reversion had first occurred. Subsequently, we expressed and purified recombinant MERS-CoV nsp14 and established in vitro assays for both its ExoN and N7-MTase activities. All ExoN knockout mutations that were lethal when tested via reverse genetics were found to severely decrease ExoN activity, while not affecting N7-MTase activity. Our study thus reveals an additional function for MERS-CoV nsp14 ExoN PROTEIN, which apparently is critical for primary viral RNA synthesis, thus differentiating it from the proofreading activity thought to boost long-term replication fidelity in MHV and SARS-CoV MESHD. IO_SCPLOWMPORTANCEC_SCPLOWThe bifunctional nsp14 subunit of the coronavirus replicase contains 3-to-5 exoribonuclease PROTEIN (ExoN) and N7-methyltransferase (N7-MTase) domains. For the betacoronaviruses MHV and SARS-CoV, the ExoN domain was reported to promote the fidelity of genome replication, presumably by mediating some form of proofreading. For these viruses, ExoN knockout mutants are alive while displaying an increased mutation frequency. Strikingly, we now established that the equivalent knockout mutants of MERS-CoV ExoN are non-viable and completely deficient in RNA synthesis, thus revealing an additional and more critical function of ExoN in coronavirus replication. Both enzymatic activities of (recombinant) MERS-CoV nsp14 were evaluated using newly developed in vitro assays that can be used to characterize these key replicative enzymes in more detail and explore their potential as target for antiviral drug development.

    In-Silico Molecular Docking Show Mitocurcumin can Potentially Block Innate Immune Evasion Mechanism of SARS-CoV-2 and Enhance Viral Load Clearance

    Authors: Debojyoti Pal; Rahul Checker; Vijay Kutala; Santosh Sandur

    doi:10.26434/chemrxiv.12439967.v1 Date: 2020-06-09 Source: ChemRxiv

    In the present work, we have employed a molecular docking approach to study the ability of mitocurcumin (MC), a triphenyl phosphonium conjugated curcumin derivative, to inhibit SARS-CoV-2 infection MESHD. Computational analysis revealed that MC can bind strongly to SARS-CoV-2 ADP Ribose Phosphatase ( NSP3 HGNC NSP3 PROTEIN) with high binding energy of -10.3 kcal/mol and to SARS-CoV-2 methyltransferase ( NSP10 PROTEIN- NSP16 PROTEIN complex) with a high binding energy of -10.4 kcal/mol. We found that MC interacts with critical residues of viral NSP3 PROTEIN NSP3 HGNC macro-domain, known to suppress host immune response, through hydrophobic interactions and occupies its active site. Furthermore, MC interacts with the critical residues of NSP10 PROTEIN- NSP16 PROTEIN complex, known to prevent innate immune detection of viral mRNA, through hydrophobic and hydrogen bond interaction and occupies the methyl group donor site. MC is also found to bind to main protease PROTEIN of SARS-CoV-2 and may potentially act as an inhibitor of the viral protease. In conclusion, MC can potentially inhibit the activity of multiple SARS-CoV-2 proteins and may accentuate the innate immune system mediated clearance of viral load resulting in improved clinic outcome in COVID-19 MESHD patients.

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HGNC Genes
SARS-CoV-2 Proteins


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