Corpus overview


MeSH Disease

HGNC Genes

SARS-CoV-2 proteins

ProteinS (16)

ProteinS1 (1)


SARS-CoV-2 Proteins
    displaying 1 - 10 records in total 32
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    An Innovative antibody-based Plug-and-Play strategy for SARS-CoV-2


    doi:10.1101/2021.03.11.434589 Date: 2021-03-12 Source: bioRxiv

    The novel and highly pathogenic coronavirus (SARS-CoV-2) remains a public health threat worldwide. SARS-CoV-2 enters human host lung cells via its spike protein PROTEIN binding to angiotensin-converting enzyme 2 HGNC ( ACE2 HGNC) in a process critical dependent on host protease-mediated fusion event. Thus, effective targeted therapies blocking the first step of viral fusion and cellular entry remains a critical unmet medical need to overcome disease pathology. Here we engineered and describe an antibody-based novel and targeted plug-and-play strategy, which directly competes with the proteolytic activation function of SAR-CoV-2 spike protein PROTEIN. The described strategy involves the engineering of furin HGNC substrate residues in IgG1 Fc-extended flexible region of spike targeting antibody. Our results with spike receptor-binding domain (RBD) targeting CR3022 antibody support blockade of the viral function using proof of concept ACE2 HGNC overexpressing cells. Our study reveals analytical, safe, and selective mechanistic insights for SARS-CoV-2 therapeutic design and is broadly applicable to the future coronaviridae family members (including newly identified mutant variants) exploiting the host protease system for their deadly pathology.

    SARS-CoV-2 Viremia MESHD is Associated with Distinct Proteomic Pathways and Predicts COVID-19 MESHD Outcomes

    Authors: Yijia Li; Alexis M Schneider; Arnav Mehta; Moshe Sade-Feldman; Kyle R Kays; Matteo Gentili; Nicole C Charland; Anna LK Gonye; Irena Gushterova; Hargun K Khanna; Thomas J LaSalle; Kendall M Lavin-Parsons; Brendan M Lilley; Carl L Lodenstein; Kasidet Manakongtreecheep; Justin D Margolin; Brenna N McKaig; Blair A Parry; Maricarmen Rojas-Lopez; Brian C Russo; Nihaarika Sharma; Jessica Tantivit; Molly F Thomas; James Regan; James P Flynn; Alexandra-Chloe Villani; Nir Hacohen; Marcia B Goldberg; Michael R Filbin; Jonathan Z Li

    doi:10.1101/2021.02.24.21252357 Date: 2021-02-26 Source: medRxiv

    Background: Severe Acute Respiratory Syndrome Coronavirus 2 MESHD (SARS-CoV-2) plasma viremia MESHD has been associated with severe disease and death in coronavirus disease MESHD coronavirus disease 2019 MESHD ( COVID-19 MESHD) in small-scale cohort studies. The mechanisms behind this association remain elusive. Methods: We evaluated the relationship between SARS-CoV-2 viremia MESHD, disease outcome, inflammatory and proteomic profiles in a cohort of COVID-19 MESHD emergency department participants. SARS-CoV-2 viral load was measured using qRT-PCR based platform. Proteomic data were generated with Proximity Extension Assay (PEA) using the Olink platform. Results: Three hundred participants with nucleic acid test-confirmed COVID-19 MESHD were included in this study. Levels of plasma SARS-CoV-2 viremia MESHD at the time of presentation predicted adverse disease outcomes, with an adjusted odds ratio (aOR) of 10.6 (95% confidence interval [CI] 4.4, 25.5, P<0.001) for severe disease (mechanical ventilation and/or 28-day mortality) and aOR of 3.9 (95%CI 1.5, 10.1, P=0.006) for 28-day mortality. Proteomic analyses revealed prominent proteomic pathways associated with SARS-CoV-2 viremia MESHD, including upregulation of SARS-CoV-2 entry factors ( ACE2 HGNC, CTSL HGNC, FURIN HGNC), heightened markers of tissue damage to the lungs, gastrointestinal tract, endothelium/vasculature and alterations in coagulation pathways. Conclusions: These results highlight the cascade of vascular and tissue damage associated with SARS-CoV-2 plasma viremia MESHD that underlies its ability to predict COVID-19 MESHD disease outcomes.

    A novel antibody against the furin HGNC cleavage site of SARS-CoV-2 spike PROTEIN protein: effects on proteolytic cleavage and ACE2 HGNC binding

    Authors: Michael G Spelios; Jeanne M Capanelli; Adam W Li

    doi:10.1101/2021.02.09.430451 Date: 2021-02-09 Source: bioRxiv

    SARS-CoV-2 harbors a unique S1/S2 furin HGNC cleavage site within its spike protein PROTEIN, which can be cleaved by furin HGNC and other proprotein convertases. Proteolytic activation of SARS-CoV-2 spike PROTEIN protein at the S1 PROTEIN/S2 boundary facilitates interaction with host ACE2 HGNC receptor for cell entry. To address this, high titer antibody was generated against the SARS-CoV-2-specific furin HGNC motif. Using a series of innovative ELISA-based assays, this furin HGNC site blocking antibody displayed high sensitivity and specificity for the S1/S2 furin HGNC cleavage site, and demonstrated effective blockage of both enzyme-mediated cleavage and spike- ACE2 HGNC interaction. The results suggest that immunological blocking of the furin HGNC cleavage site may afford a suitable approach to stem proteolytic activation of SARS-CoV-2 spike PROTEIN protein and curtail viral infectivity.

    Persistently increased systemic ACE2 HGNC activity and Furin HGNC levels are associated with increased inflammatory response in smokers with SARS-CoV-2 COVID-19 MESHD

    Authors: Gagandeep Kaur; Shaiesh Yogeswaran; Thivanka Muthumalage; Irfan Rahman

    doi:10.1101/2021.01.14.21249836 Date: 2021-01-15 Source: medRxiv

    BackgroundTobacco smoking is known to be involved in the pathogenesis of several cardiopulmonary diseases MESHD, and smokers are susceptible to infectious agents. However, the progression of lung injury MESHD based on COVID-19 MESHD susceptibility and severity amongst smokers and those with pre-existing pulmonary diseases MESHD is not known. We determined the systemic expression and activity of COVID-19 MESHD related proteins, cytokine/chemokines, and lipid mediators (lipidomics) amongst COVID-19 MESHD patients with and without a history of smoking with a view to define biomarkers. MethodsWe obtained serum from COVID-19 MESHD positive and COVID-19 MESHD recovered patients with and without a history of smoking. We conducted a Luminex multiplex assay (cytokine levels), LC/MS (eicosanoids or oxylipin panel) and enzymatic activity assays on the serum samples to study the systemic changes in COVID-19 MESHD patients. ResultsOn comparing the cytokine profiles among COVID-19 MESHD positive and COVID-19 MESHD negative patients, we found a significant upregulation in the production of pro-inflammatory cytokines like IL-1 HGNC, IL-8 HGNC, IL-2 HGNC, VEGF HGNC and IL-10 HGNC in COVID-19 MESHD positive patients as compared to the respective controls. Interestingly, smoking history resulted in further augmentation of the release of some hyper-inflammatory cytokines MESHD, like IFN-{gamma HGNC}, Eotaxin HGNC, MCP-1 HGNC and IL-9 HGNC amongst COVID-19 MESHD positive patients. The enzymatic activity for ACE2 HGNC, the binding partner for SARS-CoV2 virus in the host cell, was found to be significantly increased in the serum of patients with a smoking history compared to the serum collected from the non-smoking controls. Similarly to our cytokine analysis, our measurement of serum Furin HGNC levels was also affected by the patients smoking history, in which we reported a substantial rise in serum Furin HGNC levels of COVID-19 MESHD patients. The analysis of lipid mediators revealed a distinct signature amongst the COVID-19 MESHD positive versus recovered subjects in PGF2, HETEs, LXA4 and LTB4 levels. However, we did not find any changes in the levels of any lipid mediators based on the smoking history of the patients. Overall, our results point towards distinct systemic signatures amongst COVID-19 MESHD positive patients. We also show that smoking adversely affects the systemic levels of inflammatory markers and COVID-19 MESHD related proteins, thus suggesting that COVID-19 MESHD infection may have severe outcomes amongst smokers which is reflected systemically.

    Fibrinolysis influences SARS-CoV-2 infection MESHD in ciliated cells

    Authors: Myoung Ryoul Park; Chunmei Cai; Min-Jung Seo; Hong-Tae Yun; Soo-Kwon Park; Man-Soo Choi; Chang-Hwan Park; Jung Kyung Moon

    doi:10.1101/2021.01.07.425801 Date: 2021-01-08 Source: bioRxiv

    Rapid spread of COVID-19 MESHD has caused an unprecedented pandemic worldwide, and an inserted furin HGNC site in SARS-CoV-2 spike PROTEIN protein (S PROTEIN) may account for increased transmissibility. Plasmin HGNC, and other host proteases, may cleave the furin HGNC site of SARS-CoV-2 S protein PROTEIN and {gamma} subunits of epithelial sodium channels ({gamma} ENaC), resulting in an increment in virus infectivity and channel activity. As for the importance of ENaC in the regulation of airway surface and alveolar fluid homeostasis MESHD, whether SARS-CoV-2 will share and strengthen the cleavage network with ENaC proteins at the single-cell level is urgently worthy of consideration. To address this issue, we analyzed single-cell RNA sequence (scRNA-seq) datasets, and found the PLAU HGNC (encoding urokinase plasminogen activator), SCNN1G HGNC ({gamma}ENaC), and ACE2 HGNC (SARS-CoV-2 receptor) were co-expressed in alveolar epithelial MESHD, basal, club, and ciliated epithelial cells. The relative expression level of PLAU HGNC, TMPRSS2 HGNC, and ACE2 HGNC were significantly upregulated in severe COVID-19 MESHD patients and SARS-CoV-2 infected MESHD cell lines using Seurat and DESeq2 R packages. Moreover, the increments in PLAU HGNC, FURIN HGNC, TMPRSS2 HGNC, and ACE2 HGNC were predominately observed in different epithelial cells and leukocytes. Accordingly, SARS-CoV-2 may share and strengthen the ENaC fibrinolytic proteases network in ACE2 HGNC positive airway and alveolar MESHD epithelial cells, which may expedite virus infusion into the susceptible cells and bring about ENaC associated edematous respiratory condition MESHD.

    Furin HGNC cleaves SARS-CoV-2 spike PROTEIN-glycoprotein at S1/S2 and S2'for viral fusion/entry: indirect role for TMPRSS2

    Authors: Rachid Essalmani; Jaspreet Jain; Delia Susan-Resiga; Ursula Andreo; Alexandra Evagelidis; Rabeb Mouna Derbali; David Huynh; Frederic Dallaire; Melanie Laporte; Adrien Delpal; Priscila Sutto-Ortiz; Bruno Coutard; Claudine Mapa; Keith Wilcoxen; Etienne Decroly; Tram Pham; Eric A. Cohen; Nabil G. G Seidah; Massimo Zollo; Achille Iolascon; Mario Capasso; Nour Albes; Hani M. Al-Afghani; Bader Alghamdi; Mansour Almutair; Ebrahim Sabri Mahmoud; Leen Abu Safie; Hadeel El Bardisy; Fawz S. Al Harthi; Abdulraheem Alshareef; Bandar Ali Suliman; Saleh Alqahtani; Abdulaziz AlMalik; May M. Alrashed; Salam Massadeh; Vincent Mooser; Mark Lathrop; Yaseen Arabi; Hamdi Mbarek; Chadi Saad; Wadha Al-Muftah; Radja Badji; Asma Al Thani; Said I. Ismail; Ali G. Gharavi; Malak S. Abedalthagafi; J Brent Richards; David B. Goldstein; Krzysztof Kiryluk

    doi:10.1101/2020.12.18.423106 Date: 2020-12-20 Source: bioRxiv

    The Spike (S)-protein PROTEIN of SARS-CoV-2 binds host-cell receptor ACE2 HGNC and requires proteolytic 'priming' (S1/S2) and 'fusion-activation' (S2') for viral entry. The S-protein PROTEIN furin HGNC-like motifs PRRAR685{downarrow} and KPSKR815{downarrow} indicated that proprotein convertases promote virus entry. We demonstrate that furin HGNC and PC5A induce cleavage at both sites, ACE2 HGNC enhances S2' processing, and their pharmacological inhibition (BOS-inhibitors) block endogenous cleavages. S1/S2-mutations (S1/S2) limit S-protein PROTEIN-mediated cell-to-cell fusion, similarly to BOS-inhibitors. Unexpectedly, TMPRSS2 HGNC does not cleave at S1/S2 or S2', but it can: (i) cleave/inactivate S-protein PROTEIN into S2a/S2b; (ii) shed ACE2 HGNC; (iii) cleave S1-subunit into secreted S1', activities inhibited by Camostat. In lung-derived Calu-3 cells, BOS-inhibitors and S1/S2 severely curtail 'pH-independent' viral entry, and BOS-inhibitors alone/with Camostat potently reduce infectious viral titer and cytopathic effects. Overall, our results show that: furin HGNC plays a critical role in generating fusion-competent S-protein PROTEIN, and indirectly, TMPRSS2 HGNC promotes viral entry, supporting furin HGNC and TMPRSS2 HGNC inhibitors as potential antivirals against SARS-CoV-2

    Genetic variability in COVID-19 MESHD-related genes in the Brazilian population

    Authors: Rodrigo Secolin; Tania K de Araujo; Marina C. Gonsales; Cristiane S. Rocha; Michel Satya Naslavsky; Luiz De Marco; Maria Bicalho; Vinicius L Vazquez; Mayana Zatz; Wilson A Silva Jr.; Iscia Lopes-Cendes; Sebla B Kutluay; Mei-Ling Li; Gary Brewer; Blanton S Tolbert; Amanda E Hargrove; Alexandra W. Dretler; Ria Gripaldo; Andrea N. Lane; Hao Wu; Saeyun Lee; Mindy Hernandez; Vanessa Engineer; John Varghese; Sang Le; Iñaki Sanz; John L. Daiss; Frances Eun-Hyung Lee

    doi:10.1101/2020.12.04.411736 Date: 2020-12-06 Source: bioRxiv

    SARS-CoV-2 employs the angiotensin-converting enzyme 2 HGNC ( ACE2 HGNC) receptor and the transmembrane serine protease ( TMPRSS2 HGNC) to infect human lung cells. Previous studies have suggested that different host genetic backgrounds in ACE2 HGNC and TMPRSS2 HGNC could contribute to differences in the rate of infection or severity of COVID-19 MESHD. Recent studies also showed that variants in 15 genes related to type I interferon immunity to influenza virus could predispose to life-threatening COVID-19 MESHD pneumonia MESHD. Additional genes ( SLC6A20 HGNC, LZTFL1 HGNC, CCR9 HGNC, FYCO1 HGNC, CXCR6 HGNC, XCR1 HGNC, IL6 HGNC, CTSL HGNC, ABO, and FURIN HGNC) and HLA alleles have also been implicated in response to infection with SARS-CoV-2. Currently, Brazil has recorded the third-highest number of COVID-19 MESHD patients worldwide. We aim to investigate the genetic variation present in COVID-19 MESHD-related genes in the Brazilian population. We analysed 27 candidate genes and HLA alleles in 954 admixed Brazilian exomes. We used the information available in two public databases ( and, and additional exomes from individuals born in southeast Brazil, the region with the highest number of COVID-19 MESHD patients in the country. Variant allele frequencies were compared with the 1000 Genomes Project phase 3 (1KGP) and the gnomAD databases. We found 395 non-synonymous variants; of these, 325 were also found in the 1000 Genome Project phase 3 (1KGP) and/or gnomAD. Six of these variants were previously reported as putatively influencing the rate of infection or clinical prognosis for COVID-19 MESHD. The remaining 70 variants were identified exclusively in the Brazilian sample, with a mean allele frequency of 0.0025. In silico prediction of the impact in protein function revealed that three of these rare variants were pathogenic. Furthermore, we identified HLA alleles that were previously associated with COVID-19 MESHD response at loci DQB1 HGNC and DRB1 HGNC. Our results showed genetic variability common to other populations, but also rare and ultra-rare variants exclusively found in the Brazilian population. These findings could potentially lead to differences in the rate of infection or response to infection by SARS-CoV-2 and should be further investigated in patients with the disease.

    Multimodal Single-Cell Omics Analysis of COVID-19 MESHD Sex Differences in Human Immune Systems

    Authors: Yuan Hou; Yadi Zhou; Michaela Gack; Justin Lathia; Asha Kallianpur; Reena Mehra; Timothy Chan; Jae U. Jung; Lara Jehi; Charis Eng; Feixiong Cheng; Emily R Ko; Ephraim L Tsalik; gregory sempowski; Thomas N Denny; Thomas W Burke; Micah T McClain; Christopher W. Woods; Xiling Shen; Daniel R Saban; Brea Tinsley; Alan Trudeau; Jitendra Singh; Lindsey Whitmore; Helen Zheng; Matthew Benedek; Jenna Currier; Mark Dresel; Ashish Duvvuru; Britney Dyszel; Emily Fingar; Elizabeth M. Hennen; Michael Kirsch; Ali A. Khan; Charlotte Labrie-Cleary; Stephanie Laporte; Evan Lenkeit; Kailey Martin; Marilyn Orellana; Melanie Ortiz-Alvarez de la Campa; Isaac Paredes; Baleigh Wheeler; Allison Rupert; Andrew Sam; Katherine See; Santiago Soto Zapata; Paul A. Craig; Bonnie L. Hall; Jennifer Jiang; Julia R. Koeppe; Stephen A. Mills; Michael J. Pikaart; Rebecca Roberts; Yana Bromberg; J. Steen Hoyer; Siobain Duffy; Jay Tischfield; Francesc X. Ruiz; Eddy Arnold; Jean Baum; Jesse Sandberg; Grace Brannigan; Sagar D. Khare; Stephen K. Burley

    doi:10.1101/2020.12.01.407007 Date: 2020-12-01 Source: bioRxiv

    Sex differences in the risk of SARS-CoV-2 infection MESHD have been controversial and the underlying mechanisms of COVID-19 MESHD sexual dimorphism remain understudied. Here we inspected sex differences in SARS-CoV-2 positivity, hospitalization, admission to the intensive care unit (ICU), sera immune profiling, and two single-cell RNA-sequencing (snRNA-seq) profiles from nasal tissues and peripheral blood mononuclear cells (PBMCs) of COVID-19 MESHD patients with varying degrees of disease severity. Our propensity score-matching observations revealed that male individuals have a 29% increased likelihood of SARS-CoV-2 positivity, with a hazard ration (HR) 1.32 (95% confidence interval [CI] 1.18-1.48) for hospitalization and HR 1.51 (95% CI 1.24-1.84) for admission to ICU. Sera from male patients at hospital admission had decreased lymphocyte count and elevated inflammatory markers ( C-reactive protein HGNC, procalcitonin, and neutrophils). We found that SARS-CoV-2 entry factors, including ACE2 HGNC, TMPRSS2 HGNC, FURIN HGNC and NRP1 HGNC, have elevated expression in nasal squamous MESHD cells from males with moderate and severe COVID-19 MESHD. Cell-cell network proximity analysis suggests possible epithelium-immune cell interactions and immune vulnerability underlying a higher mortality in males with COVID-19 MESHD. Monocyte-elevated expression of Toll like receptor 7 HGNC ( TLR7 HGNC) and Bruton tyrosine kinase ( BTK HGNC) is associated with severe outcomes in males with COVID-19 MESHD. These findings provide basis for understanding immune responses underlying sex differences, and designing sex-specific targeted treatments and patient care for COVID-19 MESHD.

    A Meta-analysis of Comorbidities in COVID-19 MESHD: Which Diseases increase the Susceptibility of SARS-CoV-2 Infection MESHD?

    Authors: Srinivasan Ramachandran; Manoj Kumar Singh; Ahmed Mobeen; Amit Chandra; Sweta Joshi

    id:10.20944/preprints202009.0486.v1 Date: 2020-09-21 Source:

    Background: Comorbidities have been frequently reported in COVID-19 MESHD patients, which often lead to more severe outcomes. The underlying molecular mechanisms behind these clinical observations have not yet been explained. Herein, we investigated the disease-specific gene expression signatures that may induce susceptibility to SARS-CoV-2 infection MESHD. Methods: We studied 30 frequently occurring acute, chronic, or infectious diseases of recent times that have shown comorbidity in one or another respiratory disease MESHD(s) caused by pathogenic human infecting coronaviruses, especially SARS-CoV-2. We retrieved array-based gene expression data for each disease and control from relevant datasets. Subsequently, all the datasets were quantile normalized, and log-2 transformed data was used for analysis. Results The expression of ACE2 HGNC receptor and host proteases, namely FURIN HGNC and TMPRSS2 HGNC that are essential for cellular entry of SARS-CoV-2, was upregulated in all six studied subtypes of leukemia MESHD (hereafter, referred as leukemia MESHD). The expression of ACE2 HGNC was also increased in psoriasis MESHD, lung cancer MESHD, Non-alcoholic fatty liver disease MESHD ( NAFLD MESHD), breast cancer MESHD, and pulmonary arterial hypertension MESHD patients. The expression of FURIN HGNC was higher in psoriasis MESHD, NAFLD MESHD, lung cancer MESHD, and in type II diabetic liver MESHD, whereas it was lowered in breast cancer MESHD. Similarly, the expression of TMPRSS2 HGNC was increased during lung cancer MESHD and type II diabetes MESHD; it was decreased during psoriasis MESHD, NAFLD MESHD, lung cancer MESHD, breast cancer MESHD, and cervical cancer MESHD.Furthermore, a heightened expression of genes that are involved in immune response was observed in leukemia MESHD patients, as shown by the higher expression of IFNA2 HGNC, IFNA8 HGNC, IFNA10 HGNC, IFNA14 HGNC, IFNA16 HGNC, IFNA21 HGNC, IFNB1 HGNC, CXCL10 HGNC, and IL6 HGNC. The expression of JAK1 HGNC, STAT1 HGNC, IL6 HGNC, and CXCL10 HGNC was higher in NAFLD MESHD. Besides, JAK1 HGNC and STAT1 HGNC were upregulated in type II diabetic muscles MESHD. In addition, most of the upregulated genes in COVID-19 MESHD patients showed a similar trend in leukemia MESHD, NAFLD MESHD, and psoriasis MESHD. Furthermore, SARS-CoV-2, SARS-CoV MESHD and MERS CoV, were found to commonly alter two genes, namely, CARBONIC ANHYDRASE 11 and CLUSTERIN.Conclusions: The genes that may confer susceptibility to SARS-CoV-2 infection MESHD are mostly upregulated in leukemia MESHD patients; hence, leukemia MESHD patients are relatively more susceptible to develop COVID-19 MESHD, followed by other chronic disorders MESHD, such as, NAFLD MESHD, type II diabetes MESHD, psoriasis MESHD, and hypertension MESHD. This study identifies key genes that are altered in the studied diseases types, which may aid in the infection of SARS-CoV-2 MESHD and underlie COVID-19 MESHD associated comorbidities.

    Furin HGNC cleavage of SARS-CoV-2 Spike PROTEIN promotes but is not essential for infection and cell-cell fusion

    Authors: Guido Papa; Donna Mallery; Anna Albecka; Lawrence Welch; Jerome Cattin-Ortola; Jakub Luptak; David Paul; Harvey McMahon; Ian G. Goodfellow; Andrew P Carter; Sean P Munro; Leo C James

    doi:10.1101/2020.08.13.243303 Date: 2020-08-14 Source: bioRxiv

    Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infects MESHD cells by binding to the host cell receptor Ace2 HGNC and undergoing virus-host membrane fusion. Fusion is triggered by the protease TMPRSS2 HGNC, which processes the viral Spike (S) protein PROTEIN to reveal the fusion peptide. SARS-CoV-2 has evolved a multibasic site at the S1-S2 boundary, which is thought to be cleaved by furin HGNC in order to prime S protein PROTEIN for TMPRSS2 HGNC processing. Here we show that CRISPR-Cas9 knockout of furin HGNC reduces, but does not prevent, the production of infectious SARS-CoV-2 MESHD virus. Comparing S processing in furin HGNC knockout cells to multibasic site mutants reveals that while loss of furin HGNC substantially reduces S1-S2 cleavage it does not prevent it. SARS-CoV-2 S MESHD S protein PROTEIN also mediates cell-cell fusion, potentially allowing virus to spread virion-independently. We show that loss of furin HGNC in either donor or acceptor cells reduces, but does not prevent, TMPRSS2 HGNC-dependent cell-cell fusion, unlike mutation of the multibasic site that completely prevents syncytia formation. Our results show that while furin HGNC promotes both SARS-CoV-2 infectivity MESHD and cell-cell spread it is not essential, suggesting furin HGNC inhibitors will not prevent viral spread.

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MeSH Disease
HGNC Genes
SARS-CoV-2 Proteins

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