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MeSH Disease

HGNC Genes

SARS-CoV-2 proteins

ProteinE (7)

ProteinS (5)

ProteinN (1)


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SARS-CoV-2 Proteins
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    Genome-wide CRISPR activation screen identifies novel receptors for SARS-CoV-2 entry MESHD

    Authors: Shiyou Zhu; Ying Liu; Zhuo Zhou; Zhiying Zhang; Xia Xiao; Zhiheng Liu; Ang Chen; Xiaojing Dong; Feng Tian; Shihua Chen; Yiyuan Xu; Chunhui Wang; Qiheng Li; Xuran Niu; Qian Pan; Shuo Du; Junyu Xiao; Jianwei Wang; Wensheng Wei

    doi:10.1101/2021.04.08.438924 Date: 2021-04-09 Source: bioRxiv

    The ongoing pandemic of coronavirus disease 2019 MESHD ( COVID-19 MESHD) caused by severe acute respiratory syndrome coronavirus 2 MESHD (SARS-CoV-2) has been endangering worldwide public health and economy. SARS-CoV-2 infects MESHD a variety of tissues where the known receptor ACE2 HGNC is low or almost absent, suggesting the existence of alternative pathways for virus entry. Here, we performed a genome-wide barcoded-CRISPRa screen to identify novel host factors that enable SARS-CoV-2 infection MESHD. In addition to known host proteins, i.e PROTEIN. ACE2 HGNC, TMPRSS2 HGNC, and NRP1 HGNC, we identified multiple host components, among which LDLRAD3 HGNC, TMEM30A HGNC, and CLEC4G HGNC were confirmed as functional receptors for SARS-CoV-2. All these membrane proteins bind directly to spike's N-terminal domain ( NTD HGNC). Their essential and physiological roles have all been confirmed in either neuron or liver cells. In particular, LDLRAD3 HGNC and CLEC4G HGNC mediate SARS-CoV-2 entry MESHD and infection in a fashion independent of ACE2 HGNC. The identification of the novel receptors and entry mechanisms could advance our understanding of the multiorgan tropism of SARS-CoV-2, and may shed light on the development of the therapeutic countermeasures against COVID-19 MESHD.

    Expression of human ACE2 HGNC N-terminal domain, part of the receptor for SARS-CoV-2, in fusion with maltose binding protein, E PROTEIN. coli ribonuclease I and human RNase A

    Authors: Shuang-yong Xu; Alexey Fomenkov; Tien-Hao Chen; Erbay Yigit; Yinhui Lu; Karl E Kadler

    doi:10.1101/2021.01.31.429007 Date: 2021-02-01 Source: bioRxiv

    The SARS-CoV-2 viral genome contains a positive-strand single-stranded RNA of ~30 kb. Human ACE2 HGNC protein is the receptor for SARS-CoV-2 virus attachment MESHD and initiation of infection MESHD. We propose to use ribonucleases (RNases) as antiviral agents to destroy the viral genome in vitro. In the virions the RNA is protected by viral capsid proteins, membrane proteins and nucleocapsid PROTEIN proteins. To overcome this protection we set out to construct RNase fusion with human ACE2 HGNC receptor N-terminal domain (ACE2NTD). We constructed six proteins expressed in E. coli cells: 1) MBP-ACE2NTD, 2) ACE2NTD-GFP, 3) RNase I (6xHis), 4) RNase III (6xHis), 5) RNase I-ACE2NTD (6xHis), and 6) human RNase A HGNC-ACE2NTD150 (6xHis). We evaluated fusion expression in different E. coli strains, partially purified MBP-ACE2NTD protein from the soluble fraction of bacterial cell lysate, and refolded MBP-ACE2NTD protein from inclusion body. The engineered RNase I-ACE2NTD (6xHis) and hRNase A-ACE2NTD (6xHis) fusions are active in cleaving COVID-19 MESHD RNA in vitro. The recombinant RNase I (6xHis) and RNase III (6xHis) are active in cleaving RNA and dsRNA in test tube. This study provides a proof-of-concept for construction of fusion protein between human cell receptor and nuclease that may be used to degrade viral nucleic acids in our environment.

    BRD2 HGNC inhibition blocks SARS-CoV-2 infection MESHD in vitro by reducing transcription of the host cell receptor ACE2

    Authors: Ruilin Tian; Avi J Samelson; Veronica V Rezelj; Merissa Chen; Gokul N Ramadoss; Xiaoyan Guo; Alice Mac Kain; Quang Dinh Tran; Shion A Lim; Irene Lui; James Nunez; Sarah J Rockwood; Na Liu; Jared Carlson-Stevermer; Jennifer Oki; Travis Maures; Kevin Holden; Jonathan S Weissman; James A Wells; Bruce Conklin; Marco Vignuzzi; Martin Kampmann; Roshni Patel; Juan P Dizon; Irina Shimeliovich; Anna Gazumyan; Marina Caskey; Pamela J Bjorkman; Rafael Casellas; Theodora Hatziioannou; Paul D Bieniasz; Michel C Nussenzweig

    doi:10.1101/2021.01.19.427194 Date: 2021-01-19 Source: bioRxiv

    SARS-CoV-2 infection MESHD of human cells is initiated by the binding of the viral Spike protein PROTEIN to its cell-surface receptor ACE2 HGNC. We conducted an unbiased CRISPRi screen to uncover druggable pathways controlling Spike protein PROTEIN binding to human cells. We found that the protein BRD2 HGNC is an essential node in the cellular response to SARS-CoV-2 infection MESHD. BRD2 HGNC is required for ACE2 HGNC transcription in human lung epithelial cells and cardiomyocytes, and BRD2 HGNC inhibitors currently evaluated in clinical trials potently block endogenous ACE2 HGNC expression and SARS-CoV-2 infection MESHD of human cells. BRD2 HGNC also controls transcription of several other genes induced upon SARS-CoV-2 infection MESHD, including the interferon response, which in turn regulates ACE2 HGNC levels. It is possible that the previously reported interaction between the viral E protein PROTEIN and BRD2 HGNC evolved to manipulate the transcriptional host response during SARS-CoV-2 infection MESHD. Together, our results pinpoint BRD2 HGNC as a potent and essential regulator of the host response to SARS-CoV-2 infection MESHD and highlight the potential of BRD2 HGNC as a novel therapeutic target for COVID-19 MESHD.

    Binding of SARS-CoV-2 spike PROTEIN protein to ACE2 HGNC is disabled by thiol-based drugs; evidence from in vitro SARS-CoV-2 infection MESHD studies.

    Authors: Kritika Khanna; Wilfred Raymond; Annabelle R Charbit; Jing Jin; Irina Gitlin; Monica Tang; Hannah S Sperber; Sergej Franz; Satish Pillai; Graham Simmons; John V Fahy; Suparerk Borwornpinyo; Arunee Thitithanyanont; Suradej Hongeng; Casey Barton Behravesh; Rebecca Fischer; Gabriel L Hamer; Marion Frankenberger; Lorenz Nowak; Katharina Heinig; Ina Koch; Mircea G Stoleriu; Anne Hilgendorff; Juergen Behr; Andreas Pichlmair; Benjamin Schubert; Fabian J Theis; Dirk H Busch; Herbert B Schiller; Kilian Schober; Evangelos J Giamarellos-Bourboulis; Timothy E Sweeney

    doi:10.1101/2020.12.08.415505 Date: 2020-12-08 Source: bioRxiv

    Coronavirus disease 2019 MESHD ( COVID-19 MESHD) is caused by the severe acute respiratory syndrome coronavirus 2 MESHD (SARS-CoV-2), and the SARS-CoV-2 spike PROTEIN protein is an envelope PROTEIN glycoprotein that binds angiotensin converting enzyme 2 as an entry receptor. The capacity of enveloped viruses to infect host MESHD cells depends on a precise thiol/disulfide balance in their surface glycoprotein complexes. To determine if cystines MESHD in the SARS-CoV-2 spike PROTEIN protein maintain a native binding interface that can be disrupted by drugs that cleave cystines, we tested if thiol-based drugs have efficacy in receptor binding and cell infection assays. We found that thiol-based drugs, cysteamine and WR-1065 (the active metabolite of amifostine) in particular, decrease binding of SARS-CoV-2 spike PROTEIN protein to its receptor, decrease the entry efficiency of SARS-CoV-2 spike PROTEIN pseudotyped virus, and inhibit SARS-CoV-2 live virus infection MESHD. Our findings uncover a vulnerability of SARS-CoV-2 to thiol-based drugs and provide rationale to test thiol-based drugs, especially cysteamine and amifostine, as novel treatments for COVID-19 MESHD. One Sentence SummaryThiol-based drugs decrease binding of SARS-CoV-2 spike PROTEIN protein to its receptor and inhibit SARS-CoV-2 cell entry.

    In vitro study of BromAc on SARS-CoV-2 spike PROTEIN and envelope proteins PROTEIN shows synergy and disintegration at modest concentrations

    Authors: Javed Akhter; Krishna Pillai; Samina Badar; Ahmed Mekkawy; Sarah Valle; David L Morris; Andrew McGuire; Renee Bazin; Andres Finzi; Alptekin Gueler; Jakob Loschko; Mohan Maddur; Kristin Tompkins; Journey Cole; Bonny Gaby Lui; Thomas Ziegenhals; Arianne Plaschke; David Eisel; Sarah Dany; Stephanie Fesser; Stephanie Erbar; ferdia Bates; Diana Schneider; Bernadette Jesionek; Bianca Saenger; Ann-Kathrin Wallisch; Yvonne Feuchter; Hanna Junginger; Stefanie Krumm; Andre Heinen; Petra Adams-Quack; Julia Schlereth; Christoph Kroener; Shannan Hall-Ursone; Kathleen Brasky; Matthew C Griffor; Seungil Han; Joshua Lees; Ellene Mashalidis; Parag Sahasrabudhe; Charles Tan; Danka Pavliakova; Guy Singh; Camila Fontes-Garfias; Michael Pride; Ingrid Scully; tara Ciolino; Jennifer Obregon; Michal Gazi; Ricardo Carrion; Kendra Alfson; Warren Kalina; Deepak Kaushal; Pei-Yong Shi; Thorsten Klamp; Corinna Rosenbaum; Andreas Kuhn; Oezlem Tuereci; Philip Dormitzer; Kathrin Jansen; Ugur Sahin; Akhilesh Kumar Maurya; K Hemanth; K Nagamani; K Sudha; T Ravi Chandra; K Tushara Rao; J Vyshnavi; Rashmi Upadhyay; Shalini Bahadur; Rambha Pathak; Shikha Seth; Rakesh Gupta; Rita Saxena; Preksha Dwivedi; Reeni Malik; Deepti Chourasia; Jaya Lalwani; UM Sharma; JL Marko; Amit Suri; Vijay Kumar; Rajnish Kaushik; Parul Kodan; Bhabani Prasad Acharya; Kuldeep Kumar Gaur; Anubhav Gupta; Prerna Sachdeva; Shruti Dogra; Aikaj Jindal; M Joseph John; Avtar Singh Dhanju; Ranjana Khetrepal; Neeraj Sharma; Neetu Kukar; Divya Kavita; Rajesh Kumar; Rajesh Mahajan; Gurpreet Singh; Jaspreet Kaur; Raminder Pal Singh; Rajni Bassi; Swapneil Parikh; Om Shrivastav; Jayanthi Shastri; Maherra Desai; Shreevatsa Udupa; Varun A Bafna; Vijay Barge; Rajendra Madane; Sheetal Yadav; Sanjeev Mishra; Archana Bajpayee; M K Garg; G K Bohra; Vijaylakshmi Nag; Puneeth Babu Anne; Mohd Nadeem; Pallavi Singh; Ram Niwas; Niranjan Shiwaji Khaire; Rattiram Sharma; Mini p Singh; Naresh Sachdeva; Suchet Sachdev; Rekha Hans; Vikas Suri; L N Yaddanapudi; PVM Lakshmi; Neha Singh; Divendu Bhushan; Neeraj Kumar; Muralidhar Tambe; Sonali Salvi; Nalini Kadgi; Shashikala Sangle; Leena Nakate; Samir Joshi; Rajesh Karyakarte; Suraj Goyanka; Nimisha Sharma; Nikhil Verma; Asim Das; Monika Bahl; Nitya Wadhwa; Shreepad Bhat; Shweta Deshmukh; Vrushali Wagh; Atul Kulkarni; Tanvi Yardi; Ram S Kalgud; Purushottam Reddy; Kavitha Yevoor; Prashanth Gajula; Vivek Maleyur; Medini S; Mohith HN; Anil Gurtoo; Ritika Sud; Sangeeta Pahuja; Anupam Prakash; Parijat Gogoi; Shailja Shukla; D Himanshu Reddy; Tulika Chandra; Saurabh Pandey; Pradeep Maurya; Ali Wahid; Vivek Kumar; Kamlesh Upadhyay; Nidhi Bhatnagar; Nilima Shah; Mamta Shah; Tarak Patel; Ram Mohan Jaiswal; Ashish Jain; Shweta Sharma; Puneet Rijhwani; Naveen Gupta; Tinkal C Patel; Mahesh G Solu; Jitendra Patel; Yash R Shah; Mayur Jarag; Varsha Godbole; Meenakshi Shah; Rikin Raj; Irfan Nagori; Pramod R Jha; Arti D Shah; Gowtham Yeeli; Archit Jain; Rooppreet Kaur Gill; KV Sreedhar Babu; B Suresh Babu; Alladi Mohan; B Vengamma; K Chandra Sekhar; Srinivasulu Damam; K Narsimhulu; C Aparna; G Baleswari; Ravindranath Reddy K; P Chandrasekhar; Sunil Jodharam Panjwani; Pankaj J Akholkar; Kairavi Parthesh Joshi; Pragnesh H Shah; Manish Barvaliya; Milind Baldi; Ashok Yadav; Manoj Gupta; Nitin Rawat; Dilip Chawda; M Natarajan; M Sintha; David Pradeep Kumar; Fathhur Rabbani; Vrushali Khirid Khadke; Dattatray Patki; Sonali Marathe; Clyde D Souza; Vipul Tadha; Satyam Arora; Devendra Kumar Gupta; Seema Dua; Nitu Chauhan; Ajeet Singh Chahar; Joy John Mammen; Snehil Kumar; Dolly Daniel; Ravindraa Singh; Venkatesh Dhat; Yogesh Agarwal; Sohini Arora; Ashish Pathak; Manju Purohit; Ashish Sharma; Jayashree Sharma; Manisha Madkaikar; Kavita Joshi; Reetika Malik Yadav; Swarupa Bhagwat; Niteen D Karnik; Yojana A Gokhale; Leena Naik; Sangita Margam; Santasabuj Das; Alka Turuk; V Saravana Kumar; K Kanagasabai; R Sabarinathan; Gururaj Deshpande; Sharda Sharma; Rashmi Gunjikar; Anita Shete; Darpan Phagiwala; Chetan Patil; Snehal Shingade; Kajal Jarande; Himanshu Kaushal; Pragya Yadav; Gajanan Sapkal; Priya Abraham

    doi:10.1101/2020.09.07.286906 Date: 2020-09-08 Source: bioRxiv

    Objectives: SARS-CoV-2 infection MESHD is the cause of a worldwide pandemic, currently with limited therapeutic options. It is characterised by being highly contagious and nasal mucosa appears to be the primary site with subsequent spread to the lungs and elsewhere. BromAc (Bromelain & Acetylcysteine) has been described to disrupt glycoproteins by the synchronous breakage of glycosidic linkages and disulphide bonds. The spike protein PROTEIN of SARS-CoV-2 is an attractive target as it is essential for binding to the ACE2 HGNC receptor in host cells and is formed of glycoprotein and disulphide bridges for stabilisation. Hence, we sought to determine whether BromAc has activity on the spike and envelope protein PROTEIN specific to SARS-CoV-2 virus. Design: Gel electrophoresis analysis was carried out on recombinant spike and envelope proteins PROTEIN that were treated with a range of concentrations of single agents and BromAc. For UV analysis of disulfide bonds reduction, both spike and envelope protein PROTEIN were treated with Acetylcysteine with the determination of loss of disulfide bonds. Results: Recombinant spike and envelope SARS-CoV-2 protein were fragmented by BromAc whilst single agents had minimal effect. Spike and envelope proteins PROTEIN disulphide bonds were reduced by Acetylcysteine. Conclusion: BromAc disintegrates the spike and envelope protein PROTEIN from SARS-CoV-2 and may render it non-infective. In vitro tests on live virus have been encouraging and clinical testing through nasal administration in patients with early SARS-CoV-2 infection MESHD is imminent.

    Unravelling the debate on heme effects in COVID-19 MESHD infections

    Authors: Marie-Therese Hopp; Daniel Domingo-Fernandez; Yojana Gadiya; Milena S Detzel; Benjamin F Schmalohr; Francel Steinbock; Diana Imhof; Martin Hofmann-Apitius

    doi:10.1101/2020.06.09.142125 Date: 2020-06-10 Source: bioRxiv

    The SARS-CoV-2 outbreak was recently declared a worldwide pandemic. Infection triggers the respiratory tract disease COVID-19 MESHD, which is accompanied by serious changes of clinical biomarkers such as hemoglobin and interleukins. The same parameters are altered during hemolysis MESHD, which is characterized by an increase in labile heme. We present two approaches that aim at analyzing a potential link between available heme and COVID-19 MESHD pathogenesis. Four COVID-19 MESHD related proteins, i.e PROTEIN. the host cell proteins ACE2 HGNC and TMPRSS2 HGNC as well as the viral protein 7a and S protein PROTEIN, were identified as potential heme binders. We also performed a detailed analysis of the common pathways induced by heme and SARS-CoV-2 by superimposition of knowledge graphs covering heme biology and COVID-19 MESHD pathophysiology. Herein, focus was laid on inflammatory pathways, and distinct biomarkers as the linking elements. Finally, the results substantially improve our understanding of COVID-19 MESHD infections and disease progression of patients with different clinical backgrounds and expand the diagnostic and treatment options.

    Functional pangenome analysis provides insights into the origin, function and pathways to therapy of SARS-CoV-2 coronavirus

    Authors: Intikhab Alam; Allan K Kamau; Maxat Kulmanov; Stefan T Arold; Arnab T Pain; Takashi Gojobori; Carlos M. Duarte

    doi:10.1101/2020.02.17.952895 Date: 2020-02-21 Source: bioRxiv

    The spread of the novel coronavirus (SARS-CoV-2) has triggered a global emergency, that demands urgent solutions for detection and therapy to prevent escalating health, social and economic impacts. The spike protein (S PROTEIN) of this virus enables binding to the human receptor ACE2 HGNC, and hence presents a prime target for vaccines preventing viral entry into host cells1. The S proteins PROTEIN from SARS-CoV-1 and SARS-CoV-2 MESHD are similar2, but structural differences in the receptor binding domain (RBD) preclude the use of SARS-CoV-1-specific neutralizing antibodies to inhibit SARS-CoV-23. Here we used comparative pangenomic analysis of all sequenced Betacoronaviruses to reveal that, among all core gene clusters present in these viruses, the envelope protein E PROTEIN shows a variant shared by SARS and SARS-Cov2 with two completely-conserved key functional features, an ion-channel and a PDZ-binding Motif (PBM). These features trigger a cytokine storm that activates the inflammasome, leading to increased edema MESHD in lungs causing the acute respiratory distress syndrome MESHD ( ARDS MESHD)4-6, the leading cause of death MESHD in SARS-CoV-1 and SARS-CoV-2 infection7 MESHD SARS-CoV-2 infection MESHD7,8. However, three drugs approved for human use may inhibit SARS-CoV-1 and SARS-CoV-2 Protein E PROTEIN, either acting upon the ion channel (Amantadine and Hexamethylene amiloride9,10) or the PBM (SB2035805), thereby potentially increasing the survival of the host, as already demonstrated for SARS-CoV-1in animal models. Hence, blocking the SARS protein E PROTEIN inhibits development of ARDS in vivo. Given that our results demonstrate that the protein E PROTEIN subcluster for the SARS clade is quasi-identical for the key functional regions of SARS-CoV-1 and SARS-CoV-2, we conclude that use of approved drugs shown to act as SARS E protein PROTEIN inhibitors can help prevent further casualties from COVID-2019 while vaccines and other preventive measures are being developed.

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MeSH Disease
HGNC Genes
SARS-CoV-2 Proteins


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