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HGNC Genes

SARS-CoV-2 proteins

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    Membrane lectins enhance SARS-CoV-2 infection MESHD and influence the neutralizing activity of different classes of antibodies

    Authors: Florian A. Lempp; Leah Soriaga; Martin Montiel-Ruiz; Fabio Benigni; Julia Noack; Young-Jun Park; Siro Bianchi; Alexandra C. Walls; John E. Bowen; Jiayi Zhou; Hanna Kaiser; Maria Agostini; Marcel Meury; Exequiel Dellota Jr.; Stefano Jaconi; Elisabetta Cameroni; Herbert W. Virgin; Antonio Lanzavecchia; David Veesler; Lisa Purcell; Amalio Telenti; Davide Corti

    doi:10.1101/2021.04.03.438258 Date: 2021-04-04 Source: bioRxiv

    Investigating the mechanisms of SARS-CoV-2 cellular infection MESHD is key to better understand COVID-19 MESHD immunity and pathogenesis. Infection, which involves both cell attachment and membrane fusion, relies on the ACE2 HGNC receptor that is paradoxically found at low levels in the respiratory tract, suggesting that additional mechanisms facilitating infection may exist. Here we show that C-type lectin receptors, DC-SIGN, L-SIGN HGNC and the sialic acid-binding Ig-like lectin 1 HGNC ( SIGLEC1 HGNC) function as auxiliary receptors by enhancing ACE2 HGNC-mediated infection and modulating the neutralizing activity of different classes of spike-specific antibodies. Antibodies to the N-terminal domain ( NTD HGNC) or to the conserved proteoglycan site at the base of the Receptor Binding Domain (RBD), while poorly neutralizing infection of ACE2 HGNC over-expressing cells, effectively block lectin-facilitated infection. Conversely, antibodies to the Receptor Binding Motif ( RBM HGNC), while potently neutralizing infection of ACE2 HGNC over-expressing cells, poorly neutralize infection of cells expressing DC-SIGN or L-SIGN HGNC and trigger fusogenic rearrangement of the spike promoting cell-to-cell fusion. Collectively, these findings identify a lectin-dependent pathway that enhances ACE2 HGNC-dependent infection by SARS-CoV-2 and reveal distinct mechanisms of neutralization by different classes of spike-specific antibodies.

    SARS-CoV-2 comprehensive receptor profiling: mechanistic insight to drive new therapeutic strategies

    Authors: Sarah MV Brockbank; Raquel Faba-Rodriguez; Lyn Rosenbrier Ribeiro; Catherine Geh; Helen Thomas; Jenni Delight; Lucy Coverley; W Mark Abbott; Jo Soden; Jim Freeth

    doi:10.1101/2021.03.11.434937 Date: 2021-03-11 Source: bioRxiv

    Here we describe a hypothesis free approach to screen for interactions of SARS-CoV-2 spike MESHD SARS-CoV-2 spike PROTEIN ( S) protein PROTEIN with human cell surface receptors. We used a library screening approach to detect binding interactions across one of the largest known panels of membrane-bound and soluble receptors, comprising 5845 targets, expressed recombinantly in human cells. We were able confirm and replicate SARS-CoV-2 binding to ACE2 HGNC and other putative coreceptors such as CD209 HGNC and CLEC4M HGNC. More significantly, we identified interactions with a number of novel SARS-CoV-2 S binding proteins. Three of these novel receptors, NID1 HGNC, CNTN1 HGNC and APOA4 HGNC were specific to SARS-CoV-2, and not SARS-COV MESHD, with APOA4 HGNC binding the S-protein HGNC S-protein PROTEIN with equal affinity as ACE2 HGNC. With this knowledge we may further understand the disease pathogenesis of COVID-19 MESHD patients and how infection by SARS-CoV-2 may lead to differences in pathology in specific organs or indeed the virulence observed in different ethnicities. Importantly we illustrate a methodology which can be used for rapid, unbiassed identification of cell surface receptors, to support drug screening and drug repurposing approaches for this and future pandemics.

    The N-terminal domain of spike glycoprotein PROTEIN mediates SARS-CoV-2 infection MESHD by associating with L-SIGN HGNC and DC-SIGN

    Authors: Wai Tuck Soh; Yafei Liu; Emi E Nakayama; Chikako Ono; Shiho Torii; Hironori Nakagami; Yoshiharu Matsuura; Tatsuo Shioda; Hisashi Arase; Reid Simon; Ivan Grishagin; Laura Brovold; Ewy A Mathé; Matthew D Hall; Samuel G Michael; Alexander G Godfrey; Jordi Mestres; Lars J Jensen; Tudor I Oprea; Isabel Crooker; Sara Y Del Valle; Guido Espana; Geoffrey Fairchild; Richard C Gerkin; Timothy C Germann; Quanquan Gu; Xiangyang Guan; Lihong Guo; Gregory R Hart; Thomas J Hladish; Nathaniel Hupert; Daniel Janies; Cliff C Kerr; Daniel J Klein; Eili Klein; Gary Lin; Carrie Manore; Lauren Ancel Meyers; John Mittler; Kunpeng Mu; Rafael C NUNez; Rachel Oidtman; Remy Pasco; Ana Pastore y Piontti Pastore y Piontti; Rajib Paul; Carl AB Pearson; Dianela Perdomo; T Alex Perkins; Kelly Pierce; Alexander N Pillai; Rosalyn Cherie Rael; Katherine Rosenfeld; Chrysm Watson Ross; Julie A Spencer; Arlin B Stoltzfus; Kok Ben Toh; Shashaank Vattikuti; Alessandro Vespignani; Lingxiao Wang; Lisa White; Pan Xu; Yupeng Yang; Osman N Yogurtcu; Weitong Zhang; Yanting Zhao; Difan Zou; Matthew Ferrari; David Pannell; Michael Tildesley; Jack Seifarth; Elyse Johnson; Matthew Biggerstaff; Michael Johansson; Rachel B Slayton; John Levander; Jeff Stazer; Jessica Salermo; Michael C Runge

    doi:10.1101/2020.11.05.369264 Date: 2020-11-05 Source: bioRxiv

    The widespread occurrence of SARS-CoV-2 has had a profound effect on society and a vaccine is currently being developed. Angiotensin-converting enzyme 2 HGNC ( ACE2 HGNC) is the primary host cell receptor that interacts with the receptor-binding domain (RBD) of the SARS-CoV-2 spike PROTEIN protein. Although pneumonia MESHD is the main symptom in severe cases of SARS-CoV-2 infection MESHD, the expression levels of ACE2 HGNC in the lung is low, suggesting the presence of another receptor for the spike protein PROTEIN. In order to identify the additional receptors for the spike protein PROTEIN, we screened a receptor for the SARS-CoV-2 spike PROTEIN protein from the lung cDNA library. We cloned L-SIGN HGNC as a specific receptor for the N-terminal domain ( NTD HGNC) of the SARS-CoV-2 spike PROTEIN protein. The RBD of the spike protein PROTEIN did not bind to L-SIGN HGNC. In addition, not only L-SIGN HGNC but also DC-SIGN, a closely related C-type lectin receptor HGNC to L-SIGN HGNC, bound to the NTD HGNC of the SARS-CoV-2 spike PROTEIN protein. Importantly, cells expressing L-SIGN HGNC and DC-SIGN were both infected by SARS-CoV-2. Furthermore, L-SIGN HGNC and DC-SIGN induced membrane fusion by associating with the SARS-CoV-2 spike PROTEIN protein. Serum antibodies from infected patients and a patient-derived monoclonal antibody against NTD HGNC inhibited SARS-CoV-2 infection of L-SIGN MESHD L-SIGN HGNC or DC-SIGN expressing cells. Our results highlight the important role of NTD HGNC in SARS-CoV-2 dissemination through L-SIGN HGNC and DC-SIGN and the significance of having anti- NTD HGNC neutralizing antibodies in antibody-based therapeutics.

    ACE2 HGNC interaction networks in COVID-19 MESHD: a physiological framework for prediction of outcome in patients with cardiovascular risk factors

    Authors: Zofia Wicik; Ceren Eyileten; Daniel Jakubik; Rodrigo Pavao; Jolanta M Siller-Matula; Marek Postula

    doi:10.1101/2020.05.13.094714 Date: 2020-05-14 Source: bioRxiv

    BackgroundSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection MESHD ( coronavirus disease 2019 MESHD; COVID-19 MESHD) is associated with adverse outcome in patients with cardiovascular disease MESHD ( CVD MESHD). AimTo characterize the interaction between SARS-CoV-2 and Angiotensin Converting Enzyme 2 HGNC ( ACE2 HGNC) functional networks with focus on CVD. MethodsUsing bioinformatic tools, network medicine approaches and publicly available datasets, we investigated ACE2 HGNC tissue expression and described ACE2 HGNC interaction network which could be affected by SARS-CoV-2 infection MESHD. We identified top ACE2 HGNC interactors, including miRNAs which are shared regulators between the ACE2 HGNC, virus-infection related proteins and heart interaction networks, using lung and nervous system networks as a reference. We also identified main SARS-CoV-2 risk groups and performed drug predictions for them. ResultsWe found the same range of ACE2 HGNC expression confidence in respiratory and cardiovascular systems (averaging 4.48 and 4.64, respectively). Analysing the complete ACE2 HGNC interaction network, we identified 11 genes ( ACE2 HGNC, DPP4 HGNC, ANPEP HGNC, CCL2 HGNC, TFRC HGNC, MEP1A HGNC, ADAM17 HGNC, FABP2 HGNC, NPC1 HGNC, CLEC4M HGNC, TMPRSS2 HGNC) associated with virus-infection related processes. Previously described genes associated with cardiovascular risk factors DPP4 HGNC, CCL2 HGNC and ANPEP HGNC were extensively connected with top regulators of ACE2 HGNC network, including ACE HGNC, INS and KNG1 HGNC. Enrichment analysis revealed several disease phenotypes associated with interaction networks of ACE2 HGNC, heart tissue, and virus-infection related protein, with the strongest associations with the following diseases (in decreasing rank order): obesity, hypertensive disease, non-insulin dependent diabetes mellitus, congestive heart failure, and coronary artery disease. We described for the first time microRNAs- miR HGNC (miR-302c-5p, miR-1305 HGNC, miR-587 HGNC, miR-26b HGNC-5p, and mir-27a-3p), which were common regulators of the three networks: ACE2 HGNC, heart tissue and virus-infection related proteins. ConclusionOur study provides novel information regarding the complexity of signaling pathways affected by SARS-CoV-2 and proposes predictive tools as miR HGNC towards personalized diagnosis and therapy in COVID-19 MESHD. Additionally, our study provides a list of miRNAs with biomarker potential in prediction of adverse outcome in patients with COVID-19 MESHD and CVD. O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=106 SRC="FIGDIR/small/094714v2_ufig1.gif" ALT="Figure 1"> View larger version (29K): org.highwire.dtl.DTLVardef@11e52b0org.highwire.dtl.DTLVardef@1c6d9ceorg.highwire.dtl.DTLVardef@57be3org.highwire.dtl.DTLVardef@8889c_HPS_FORMAT_FIGEXP M_FIG C_FIG

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MeSH Disease
HGNC Genes
SARS-CoV-2 Proteins


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