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HGNC Genes

SARS-CoV-2 proteins

ProteinS (4)


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    SARS-CoV-2 Spike PROTEIN SARS-CoV-2 Spike MESHD Protein Impairs Endothelial Function via Downregulation of ACE2

    Authors: Cara R. Schiavon; Ming He; Hui Shen; Yichi Zhang; Yoshitake Cho; Leonardo Andrade; Gerry S. Shadel; Mark Hepokoski; Jin Zhang; Jason X.-J. Yuan; Atul Malhotra; Uri Manor; John Y-J. Shyy; Daniel Batlle; Thomas J Hope; Yang Shen; Yuan Luo; Young Chae; Hui Zhang; Suchitra Swaminathan; Glenn C. Randall; Alexis R Demonbreun; Michael G Ison; Deyu Fang; Huiping Liu; Nicholas C. Morano; Gregory J. Krause; Joseph M. Sweeney; Kelsie Cowman; Stephanie Allen; Jayabhargav Annam; Ariella Applebaum; Daniel Barboto; Ahmed Khokhar; Brianna J. Lally; Audrey Lee; Max Lee; Avinash Malaviya; Reise Sample; Xiuyi A. Yang; Yang Li; Rafael Ruiz; Raja Thota; Jason Barnhill; Doctor Y. Goldstein; Joan Uehlinger; Scott J. Garforth; Steven C. Almo; Jonathan R. Lai; Morayma Reyes Gil; Amy S. Fox; Kartik Chandran; Tao Wang; Johanna P. Daily; Liise-anne Pirofski

    doi:10.1101/2020.12.04.409144 Date: 2020-12-04 Source: bioRxiv

    Coronavirus disease 2019 MESHD ( COVID-19 MESHD) includes the cardiovascular complications in addition to respiratory disease MESHD. SARS-CoV-2 infection MESHD impairs endothelial function and induces vascular inflammation MESHD, leading to endotheliitis. SARS-CoV-2 infection MESHD relies on the binding of Spike glycoprotein PROTEIN ( S protein PROTEIN S protein HGNC) to angiotensin converting enzyme 2 HGNC ( ACE2 HGNC) in the host cells. We show here that S protein HGNC S protein PROTEIN alone can damage vascular endothelial cells (ECs) in vitro and in vivo, manifested by impaired mitochondrial function, decreased ACE2 HGNC expression and eNOS activity, and increased glycolysis. The underlying mechanism involves S protein PROTEIN S protein HGNC downregulation of AMPK HGNC and upregulation of MDM2 HGNC, causing ACE2 HGNC destabilization. Thus, the S protein PROTEIN S protein HGNC-exerted vascular endothelial damage via ACE2 HGNC downregulation overrides the decreased virus infectivity.

    The N-glycosylation sites and Glycan-binding ability of S-protein HGNC S-protein PROTEIN in SARS-CoV-2 Coronavirus

    Authors: Wentian Chen; Ziye Hui; Xiameng Ren; Yijie Luo; Jian Shu; Hanjie Yu; Zheng Li

    doi:10.1101/2020.12.01.406025 Date: 2020-12-01 Source: bioRxiv

    The emerging acute respiratory disease MESHD, COVID-19 MESHD, caused by SARS-CoV-2 Coronavirus (SARS2 CoV) has spread fastly all over the word. As a member of RNA viruses, the glycosylation of envelope glycoprotein plays the crucial role in protein folding, evasing host immune system, invading host cell membrane, even affecting host preference. Therefore, detail glyco-related researches have been adopted in the Spike protein (S PROTEIN S-protein HGNC) of SARS2 CoV from the bioinformatic perspective. Phylogenic analysis of S-protein HGNC S-protein PROTEIN sequences revealed the evolutionary relationship of N-glycosylation sites in different CoVs. Structural comparation of S-proteins PROTEIN indicated their similarity and distributions of N-glycosylation sites. Further potential sialic acid or galactose affinity domains have been described in the S-protein HGNC S-protein PROTEIN by docking analysis. Molecular dynamic simulation for the glycosylated complexus of S-protein HGNC S-protein PROTEIN- ACE2 HGNC implied that the complicate viral binding of receptor-binding domain may be influenced by peripheric N-glycans from own and adjacent monoers. These works will contribute to investigate the N-glycosylation in S-protein HGNC S-protein PROTEIN and explain the highly contagious of COVID-19 MESHD.

    Immunogenicity of novel mRNA COVID-19 MESHD vaccine MRT5500 in mice and non-human primates

    Authors: Kirill V Kalnin; Timothy Plitnik; Michael Kishko; Jinrong Zhang; Donghui Zhang; Andrien Beauvais; Natalie G Anosova; Timothy Tibbitts; Joshua M DiNapoli; Po-Wei D Huang; James Huleatt; Deanne Vincent; Katherine Fries; Shrirang Karve; Rebecca Goldman; Hardip Gopani; Anusha Dias; Khang Tran; Minnie Zacharia; Xiaobo Gu; Lianne Boeglin; Sudha Chivukula; Ron Swearingen; Victoria Landolfi; Tong-Ming Fu; Frank DeRosa; Danilo Casimiro

    doi:10.1101/2020.10.14.337535 Date: 2020-10-14 Source: bioRxiv

    An effective vaccine to address the global pandemic of coronavirus disease 2019 MESHD ( COVID-19 MESHD) is an urgent public health priority. Novel synthetic mRNA and vector-based vaccine technologies offer an expeditious development path alternative to traditional vaccine approaches. Here we describe the efforts to utilize an mRNA platform for rational design and evaluations of mRNA vaccine candidates based on Spike ( S) glycoprotein PROTEIN of Severe Acute Respiratory Syndrome Coronavirus 2 MESHD (SARS-CoV-2), the virus causing COVID-19 MESHD. Several mRNA constructs expressing various structural conformations of S-protein HGNC S-protein PROTEIN, including wild type (WT), a pre-fusion stabilized mutant (2P), a furin cleavage-site mutant (GSAS) and a double mutant form (2P/GSAS), were tested in a preclinical animal model for their capacity to elicit neutralizing antibodies (nAbs). The lead 2P/GSAS candidate was further assessed in dose-ranging studies in mice and Cynomolgus macaques. The selected 2P/GSAS vaccine formulation, now designated MRT5500, elicited potent nAbs as measured in two types of neutralization assays. In addition, MRT5500 elicited TH1-biased responses in both mouse and non-human primate species, a result that helps to address a hypothetical concern regarding potential vaccine-associated enhanced respiratory diseases MESHD associated with TH2-biased responses. These data position MRT5500 as a viable vaccine candidate for clinical development against COVID-19 MESHD.

    Identification of a Potent Inhibitor Targeting the Spike Protein PROTEIN of Pandemic Human Coronavirus, SARS-CoV-2 by Computational Methods

    Authors: SRUTHI UNNI; Snehal Aouti; Padmanabhan Balasundaram

    doi:10.26434/chemrxiv.12197934.v1 Date: 2020-04-27 Source: ChemRxiv

    Severe acute respiratory syndrome coronavirus (SARS-CoV-2 MESHD) is an emerging new viral pathogen that causes severe respiratory disease MESHD. SARS-CoV-2 is responsible for an outbreak of COVID-19 pandemic MESHD COVID-19 pandemic MESHD worldwide. As there are no confirmed antiviral drugs or vaccines currently available for the treatment of COVID-19 MESHD, discovering potent inhibitors or vaccines are urgently required for the benefit of humanity. The glycosylated Spike protein (S PROTEIN S-protein HGNC) directly interacts with human angiotensin-converting enzyme 2 HGNC ( ACE2 HGNC) receptor through the receptor-binding domain (RBD) of S-protein HGNC S-protein PROTEIN. As the S-protein HGNC S-protein PROTEIN is exposed to the surface and is essential for entry into the host, the S-protein HGNC S-protein PROTEIN can be considered as a first-line therapeutic target for antiviral therapy and vaccine development. In-silico screening, docking and molecular dynamics simulation studies were performed to identify repurposing drugs using DrugBank and PubChem library against the RBD of S-protein PROTEIN S-protein HGNC. The study identified a laxative drug, Bisoxatin (DB09219), which is used for the treatment of constipation MESHD and preparation of the colon for surgical procedures. It binds nicely at the S-protein PROTEIN S-protein HGNC ACE2 HGNC interface by making substantial pi-pi interactions with Tyr505 in the ‘Site 1’ hook region of RBD and hydrophilic interactions with Glu406, Ser494 and Thr500. Bisoxatin consistently binds to the protein throughout the 100 ns simulation. Taken together, we propose that the discovered molecule, Bisoxatin may be a potent repurpose drug to develop new chemical libraries for inhibiting SARS-CoV-2 entry into the host.

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MeSH Disease
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