Grant List
Represents Grant table in the DB
GET /v1/grants?page%5Bnumber%5D=1384&sort=program_reference_codes
{ "links": { "first": "https://cic-apps.datascience.columbia.edu/v1/grants?page%5Bnumber%5D=1&sort=program_reference_codes", "last": "https://cic-apps.datascience.columbia.edu/v1/grants?page%5Bnumber%5D=1442&sort=program_reference_codes", "next": "https://cic-apps.datascience.columbia.edu/v1/grants?page%5Bnumber%5D=1385&sort=program_reference_codes", "prev": "https://cic-apps.datascience.columbia.edu/v1/grants?page%5Bnumber%5D=1383&sort=program_reference_codes" }, "data": [ { "type": "Grant", "id": "1606", "attributes": { "award_id": "2033354", "title": "RAPID: Impact of SARS-CoV2 on function of the cellular tRNA methyltransferase 1 and redox homeostasis", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Biological Sciences (BIO)" ], "program_reference_codes": [ "096Z", "7465", "7914" ], "program_officials": [ { "id": 4213, "first_name": "Arcady", "last_name": "Mushegian", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2020-06-01", "end_date": "2021-11-30", "award_amount": 179077, "principal_investigator": { "id": 4214, "first_name": "Dragony", "last_name": "Fu", "orcid": "https://orcid.org/0000-0002-8725-8658", "emails": "[email protected]", "private_emails": "", "keywords": null, "approved": true, "websites": "['https://www.biorxiv.org/']", "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 464, "ror": "https://ror.org/022kthw22", "name": "University of Rochester", "address": "", "city": "", "state": "NY", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [], "awardee_organization": { "id": 464, "ror": "https://ror.org/022kthw22", "name": "University of Rochester", "address": "", "city": "", "state": "NY", "zip": "", "country": "United States", "approved": true }, "abstract": "Due to the global pandemic caused by SARS-CoV2, there is an urgent need to understand how coronavirus infection affects host cellular processes. This project will explore a recently discovered link between a SARS-CoV2 protein-cleaving enzyme and a human protein that may be its target. Combined biochemical, molecular, and cellular approaches will be used to study how interaction of the viral and human proteins can alter normal cellular functions. The outcomes are expected to uncover targets for therapeutic intervention to address the COVID-19 pandemic. The project will provide training opportunities for two graduate students who will carry out the research. Recently, a novel connection was discovered between the main protease of SARS-CoV2, called Nsp5, and the human tRNA methyltransferase enzyme known as TRMT1. TRMT1 methylates a specific position (m2.2G) in more than half of all cellular tRNAs and in many mitochondrial tRNAs, and TRMT1 is known to be essential for normal levels of protein synthesis and for redox homeostasis in human cells. TRMT1 contains an amino acid sequence that may be a target for cleavage by Nsp5, but the biological effects and downstream consequences of the Nsp5-TRMT1 interaction are unknown. This project will focus on three aims: determining the effects of Nsp5 binding on TMRT1's stability and ability to bind tRNAs; identifying TRMT1-dependent pathways that are modulated through Nsp5 interaction with TRMT1; and testing how TRMT1-dependent pathways impact the SARS-CoV2 life cycle. By understanding how SARS-CoV2 infection affects TRMT1 function, the project will yield insight into novel strategies that viruses employ to alter host gene expression and metabolism. The results could aid in development of new drug therapies or biomarkers for detecting coronavirus infection.This RAPID award is made by the Genetic Mechanisms Program in the Division of Molecular and Cellular Biosciences, using funds from the Coronavirus Aid, Relief, and Economic Security (CARES) Act.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.", "keywords": [], "approved": true } }, { "type": "Grant", "id": "1612", "attributes": { "award_id": "2032054", "title": "RAPID: Understanding the Effects of Glycosylation on Spike Vulnerabilities and the Host Range of SARS-CoV-2", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Biological Sciences (BIO)" ], "program_reference_codes": [ "096Z", "7465", "7914" ], "program_officials": [ { "id": 4229, "first_name": "Jaroslaw", "last_name": "Majewski", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2020-05-15", "end_date": "2022-04-30", "award_amount": 199910, "principal_investigator": { "id": 4230, "first_name": "Rommie E", "last_name": "Amaro", "orcid": null, "emails": "[email protected]", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 258, "ror": "", "name": "University of California-San Diego", "address": "", "city": "", "state": "CA", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [], "awardee_organization": { "id": 258, "ror": "", "name": "University of California-San Diego", "address": "", "city": "", "state": "CA", "zip": "", "country": "United States", "approved": true }, "abstract": "The COVID-19 pandemic is caused by the SARS-CoV-2 virus, a virus whose structure has not been fully characterized. The spike protein of the virus is believed to play a key role in infection. In this work computer simulations will be used to understand the role of sugar molecules that normally are present on the outside of host cells on the binding to host cells and the infectivity of the virus. Simulations will examine host cell membranes from species that include humans, cats, ferrets and other non-human primates in order to better understand the differences between virus transmission in different species. These simulations will provide information that is not currently accessible through experiment. The simulations and data sharing capabilities developed in this work will improve responsiveness against future pandemics. Additionally, the project will provide a training for two postdoctoral fellows. This research will use MD (molecular dynamics) computational methodology together with experimental data, to build and simulate biologically realistic conditions for the SARS-CoV-2 virus spike protein, alone, and also in complex with various forms of the ACE2 receptor and host cell membrane components. The aim is to determine areas of spike protein vulnerabilities as well as understand the effects of glycosylation on the structure and function of the SARS-CoV-2 infection machinery. The simulations will include ACE2 receptors in cats, ferrets, and other nonhuman primates to understand the molecular underpinnings of virus host range and transmissibility. The proposed research will provide a more complete understanding of the SARS-CoV-2 infection machinery and the molecular constituents with which it interacts at different host cells. This RAPID award is made by the Molecular Biophysics Program in the Division of Molecular and Cellular Biosciences, using funds from the Coronavirus Aid, Relief, and Economic Security (CARES) Act.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.", "keywords": [], "approved": true } }, { "type": "Grant", "id": "1614", "attributes": { "award_id": "2031094", "title": "RAPID: Host-pathogen interactions during genome replication of SARS-CoV2", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Biological Sciences (BIO)" ], "program_reference_codes": [ "096Z", "7465", "7914" ], "program_officials": [ { "id": 4233, "first_name": "Manju", "last_name": "Hingorani", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2020-06-01", "end_date": "2022-05-31", "award_amount": 162283, "principal_investigator": { "id": 4235, "first_name": "Taekjip", "last_name": "Ha", "orcid": "https://orcid.org/0000-0003-2195-6258", "emails": "[email protected]", "private_emails": "", "keywords": null, "approved": true, "websites": "['https://sites.google.com/site/taekjiphalab/covid-19-research']", "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 344, "ror": "https://ror.org/00za53h95", "name": "Johns Hopkins University", "address": "", "city": "", "state": "MD", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [ { "id": 4234, "first_name": "James M", "last_name": "Berger", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "awardee_organization": { "id": 344, "ror": "https://ror.org/00za53h95", "name": "Johns Hopkins University", "address": "", "city": "", "state": "MD", "zip": "", "country": "United States", "approved": true }, "abstract": "Replication of coronaviruses, including SARS-CoV-2 – the causative agent of COVID-19, is expected to involve protein factors from the infected host cell that provide activities not encoded in the viral genome. This project focuses on the need for the virus to co-opt a host 3’ to 5’ RNA helicase to synthesize the negative-strand RNA that serves as template for copying the positive-strand genome. A recent proteomic screen identified a candidate host helicase, DDX10, that interacts with SARS-CoV-2 proteins. The research will employ a suite of experimental approaches to characterize this enzyme and two other host RNA helicases also implicated in SARS-CoV-2 genome replication. Detailed knowledge of how host proteins contribute to viral replication will provide new targets for therapeutic intervention, importantly, in ways that help circumvent drug resistance through viral mutation. The project will also support training of a postdoctoral scholar and development of a new undergraduate biophysics course centered on coronavirus-related topics.Biochemical and biophysical techniques, such as X-ray crystallography, cryo-EM and single molecule spectroscopy, will be applied to determine structure-function properties that govern the helicase mechanism, including polarity, speed, processivity and associated energetics, and how its interactions with the viral NSP7/8 primase influence genome replication. The outcomes are expected to reveal the workings of host proteins during SARS-CoV-2 replication, and thereby open new avenues and novel drug targets to block its proliferation.This RAPID award is made by the Genetic Mechanisms Program in the Division of Molecular and Cellular Biosciences, using funds from the Coronavirus Aid, Relief, and Economic Security (CARES) Act.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.", "keywords": [], "approved": true } }, { "type": "Grant", "id": "1616", "attributes": { "award_id": "2028935", "title": "RAPID: Impact of inhibitors on SARS-CoV-2 polymerase and fidelity control of RNA synthesis", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Biological Sciences (BIO)" ], "program_reference_codes": [ "096Z", "7465", "7914" ], "program_officials": [ { "id": 4238, "first_name": "Manju", "last_name": "Hingorani", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2020-05-01", "end_date": "2022-04-30", "award_amount": 200000, "principal_investigator": { "id": 4239, "first_name": "Jin", "last_name": "Yu", "orcid": "https://orcid.org/0000-0001-8224-1374", "emails": "[email protected]", "private_emails": "", "keywords": null, "approved": true, "websites": "['https://sites.uci.edu/jinyulab/', 'https://sites.uci.edu/jinyulab/research/']", "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 177, "ror": "", "name": "University of California-Irvine", "address": "", "city": "", "state": "CA", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [], "awardee_organization": { "id": 177, "ror": "", "name": "University of California-Irvine", "address": "", "city": "", "state": "CA", "zip": "", "country": "United States", "approved": true }, "abstract": "RNA-dependent RNA polymerase (RdRp) is the core enzyme responsible for replication and transcription in RNA viruses such as SARS-CoV and MERS-CoV. Investigating the mechanism of action of RdRp offers promise for development of new antiviral therapeutics and for understanding the emergence of drug resistance, which is critical for an effective response to the COVID-19 crisis caused by SARS-CoV-2. This project will employ molecular modeling to investigate the structural dynamics underlying RdRp function. Notably, Remdesivir, a nucleotide analog, will be utilized to interrogate RdRp fidelity and better understand how it contributes to viral evolution, as well as the basis for the antiviral activity of this drug. The project also offers training opportunities for graduate and undergraduate students in computational biology.Molecular modeling and all-atom molecular dynamics simulations of conserved SARS-CoV RdRp enzymes are planned to investigate the structural dynamics and energetics governing the nucleotide addition cycle and replication fidelity. The project is guided by specific questions, including how nucleotide analogs impact selection of the correct nucleotide by RdRp, how non-nucleotide inhibitors affect the RdRp mechanism, and what mutations in RdRp might enable drug resistance. The outcomes are expected to yield novel mechanistic information about this important target enzyme for therapeutic intervention. This RAPID award is made by the Genetic Mechanisms Program in the Division of Molecular and Cellular Biosciences, using funds from the Coronavirus Aid, Relief, and Economic Security (CARES) Act.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.", "keywords": [], "approved": true } }, { "type": "Grant", "id": "1645", "attributes": { "award_id": "2027291", "title": "RAPID: Multiscale Modeling Of SARS-CoV-2 Viral Intracellular and Intercellular Dynamics", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Biological Sciences (BIO)" ], "program_reference_codes": [ "096Z", "7465", "7914" ], "program_officials": [ { "id": 4321, "first_name": "David", "last_name": "Rockcliffe", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2020-04-01", "end_date": "2021-03-31", "award_amount": 130197, "principal_investigator": { "id": 4322, "first_name": "Ranjan", "last_name": "Srivastava", "orcid": null, "emails": "[email protected]", "private_emails": "", "keywords": null, "approved": true, "websites": "['https://rslabs.org']", "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 257, "ror": "https://ror.org/02der9h97", "name": "University of Connecticut", "address": "", "city": "", "state": "CT", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [], "awardee_organization": { "id": 257, "ror": "https://ror.org/02der9h97", "name": "University of Connecticut", "address": "", "city": "", "state": "CT", "zip": "", "country": "United States", "approved": true }, "abstract": "________________________________________________________________________________________________________________The recent emergence of the SARS-CoV-2 virus, the etiological agent of COVID-19, has caused worldwide repercussions in just a few short weeks. The tremendous negative social, economic and health impact will be felt for a considerable time around the globe. Numerous complementary strategies must be taken to address this issue and to ameliorate the consequences. One such strategy that is clearly required is a better understanding of the fundamental biology of SARS-CoV-2. The objective of this project is to create a multiscale model of the intracellular and intercellular viral dynamics of the SARS-CoV-2 virus. A systems virology approach is used. This project would deliver an understanding of how the virus works and will provide the framework necessary for numerous fundamental studies and applied efforts for developing effective drugs and therapies. The developed model would be released under an open source license and made freely available from the GitHub website. The project would train one graduate student in the area of computational systems virology. This project creates intracellular and intercellular models of the SARS-2019-CoV-2 virus based on the current understanding of the virus reaction network. The reaction network topology is translated into a mathematical model with the use of the theory of reaction kinetics. A set of ordinary differential equations describing the dynamics of viral replication within an infected cell is formulated with the use of the mass action kinetics paradigm. With the use of Monte Carlo sampling of the model’s parameter space, as well as sensitivity analysis and stability analysis, mathematical and biological constraints are identified. Stochastic simulation is carried out to determine whether subpopulations of infected cells exist with potentially different phenotypes. Finally, with the use of principles grounded in basic calculus, the intracellular model is coupled to a standard intercellular model of viral replication dynamics. The multiscale models undergo the same analyses as the intracellular model and is also implemented stochastically to determine if incorporating higher scale information influences prediction of subpopulation distribution.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.", "keywords": [], "approved": true } }, { "type": "Grant", "id": "1280", "attributes": { "award_id": "2032016", "title": "RAPID: Interaction of the Coronavirus M protein with a Myosin V motor protein", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Biological Sciences (BIO)" ], "program_reference_codes": [ "096Z", "7465", "7914" ], "program_officials": [ { "id": 3294, "first_name": "Matt", "last_name": "Buechner", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2020-08-01", "end_date": "2021-07-31", "award_amount": 200000, "principal_investigator": { "id": 3295, "first_name": "James", "last_name": "Goldenring", "orcid": null, "emails": "[email protected]", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 456, "ror": "https://ror.org/05dq2gs74", "name": "Vanderbilt University Medical Center", "address": "", "city": "", "state": "TN", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [], "awardee_organization": { "id": 456, "ror": "https://ror.org/05dq2gs74", "name": "Vanderbilt University Medical Center", "address": "", "city": "", "state": "TN", "zip": "", "country": "United States", "approved": true }, "abstract": "The COVID-19 coronavirus represents one of the most acute and dangerous threat to global health in a century. The present COVID-19 outbreak is caused by the SARS-CoV-2 virus and is exacerbated by our present inability to inhibit the assembly of virus inside cells, which affects the spread of coronavirus within human patients. SARS-Cov-2 is a member of a family of related coronaviruses that includes SARS, MERS, and Mouse Hepatitis Virus (MHV). These are RNA viruses wrapped in a lipid membrane, which has a number of different proteins embedded in it. In general however, relatively little is known about how viral proteins are packaged together inside human cells to assemble coronavirus particles. This lack of knowledge impedes the development of strategies that could target the assembly of virus particles inside human cells. However, one membrane protein encoded by the virus, designated the M protein because of its membrane association, serves as the starting seed for the assembly of all the other coronavirus proteins. It has recently been discovered that the tail of the MHV version of the M protein can interact with a motor protein used for trafficking inside human cells. Because the sequence of the M-protein tails in this class of coronaviruses is very conserved, this project seeks to determine if this interaction is generalizable among SARS-CoV-2, and other related coronaviruses. If this interaction is present in SARS-CoV-2, then this project will identify the parts of the M protein that interact with the myosin motor. This would allow future research to evaluate drugs that can interrupt this interaction, which may alter the ability of the SARS-CoV-2 and other coronaviruses to assemble and spread. As a Broader Impact, the Project will provide critically needed information for fight the Covid-19 pandemic. Relatively little is known about the processes required for the assembly of coronavirus virions in human cells. The family of beta-coronaviruses, including SARS-CoV-2, SARS, MERS and MHV all utilize a similar compendium of proteins, including a membrane glycoprotein protein, termed the M protein. M protein serves as the nidus for assembly of other coronavirus proteins into the mature virus particle. This project seeks to expand on the recent finding that the M-protein of MHV interacts with a specific 26 amino acid alternatively spliced exon of Myosin Vb (MYO5B), termed exon D. This observation is the first to identify a key intracellular trafficking protein that interacts with the M protein. This project seeks to identify whether this interaction is preserved in the M proteins of other beta-coronavirus family members, including the SARS-CoV-2 virus. The Project will also determine the molecular basis of the interaction between M protein and Exon D of MYO5B. The Project will first utilize yeast 2-hybrid assays to evaluate the binding of the internal tails of SARS-CoV-2 (COVID-19), SARS and MERS and other related coronaviruses. Second, random mutagenesis of the coronavirus tails will be utilized to determine the common amino acid motifs used for interaction with MYO5B Exon D. Third, wild type and mutant coronavirus proteins will be expressed in HeLa cells, and mutations that block interactions with MYO5B on M protein will be evaluated for their effects on trafficking through the endoplasmic reticulum, the Golgi apparatus and to the plasma membrane. If verified with the SARS-CoV-2 M protein, the site of interaction with MYO5b Exon D could be utilized as a target for disruption of the assembly of coronavirus virions. This RAPID Project is expected to provide insights for the future development of molecular strategies to disrupt virion assembly in host cells, which could lead to new therapeutics for the treatment of Covid-19.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.", "keywords": [], "approved": true } }, { "type": "Grant", "id": "1316", "attributes": { "award_id": "2027096", "title": "RAPID: Biophysical characterization of the native SARS-CoV-2 virion by atomistic simulations", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Biological Sciences (BIO)" ], "program_reference_codes": [ "096Z", "7465", "7914", "9150" ], "program_officials": [ { "id": 3381, "first_name": "Jaroslaw", "last_name": "Majewski", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2020-04-01", "end_date": "2022-03-31", "award_amount": 200000, "principal_investigator": { "id": 3383, "first_name": "Juan", "last_name": "Perilla", "orcid": null, "emails": "[email protected]", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 442, "ror": "https://ror.org/01sbq1a82", "name": "University of Delaware", "address": "", "city": "", "state": "DE", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [ { "id": 3382, "first_name": "Jodi", "last_name": "Hadden-Perilla", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "awardee_organization": { "id": 442, "ror": "https://ror.org/01sbq1a82", "name": "University of Delaware", "address": "", "city": "", "state": "DE", "zip": "", "country": "United States", "approved": true }, "abstract": "Since December 2019, a novel coronavirus (SARS-CoV-2) that emerged in China has become a global pandemic. Research into the molecular basis of SARS-CoV-2 is now essential to provide understanding of viral entry and infection of human cells, a first step in developing novel drugs and vaccines to combat SARS-CoV-2. The research supported through this RAPID award will enable the development of an all-atom molecular dynamic simulation of the virus that includes realistic predictions of the envelope, membrane and spike proteins of the virus, as well as simulations of the complex surfaces of the human cells that the virus infects. This research could have immediate impact on steps taken to halt the spread of SARS-CoV-2. Simulation results will be broadly and quickly disseminated to ensure impact of the research. In addition, the investigators will use this as a training opportunity for students at all levels. This project will use to state of the art tools of computational virology to provide bio-physical characterization of the SARS-CoV-2 virion, revealing information relevant to the function and potential targeting and disruption of the virus. The PI proposes a study of the full-size viral envelope which can establish the effects of specific components of the virus, including its bilayer lipid composition, shedding light on the need for coronaviruses to remodel the host cell membrane for successful infection. Additionally the characterization of the native SARS-CoV-2 viral surface proteins, which represent key functional and antigenic sites, will form a good basis for development of an infectious SARS-CoV-2 virion and a platform to investigate a mechanism of host cell entry, in which coronaviruses bind to CD13 receptors in lipid rafts. Study of glycosylated S protein, proposed as one of the aspects of the work, will reveal details of epitope masking by the glycan shield, relevant to vaccine and antibody design, as well as the role of viral glycans in host cell adhesion in a second mechanism of cell entry mediated by S binding to ACE2 receptors. The work could have immediate impact of the current pandemic.This RAPID award is cofounded by the Molecular Biophysics Program in the Division of Molecular and Cellular Biosciences and the EPSCoR Program.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.", "keywords": [], "approved": true } }, { "type": "Grant", "id": "1988", "attributes": { "award_id": "2027066", "title": "RAPID:Antibody-Based Nanoplasmonic Barcode Biosensors for COVID-19 Detection", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Engineering (ENG)" ], "program_reference_codes": [ "096Z", "7465", "7914", "9150" ], "program_officials": [ { "id": 5307, "first_name": "Steven", "last_name": "Peretti", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2020-05-01", "end_date": "2021-04-30", "award_amount": 199651, "principal_investigator": { "id": 5310, "first_name": "Robert J", "last_name": "Pantazes", "orcid": "https://orcid.org/0000-0002-0994-007X", "emails": "[email protected]", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 273, "ror": "https://ror.org/02v80fc35", "name": "Auburn University", "address": "", "city": "", "state": "AL", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [ { "id": 5308, "first_name": "Jennifer", "last_name": "Maynard", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] }, { "id": 5309, "first_name": "Pengyu", "last_name": "Chen", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "awardee_organization": { "id": 273, "ror": "https://ror.org/02v80fc35", "name": "Auburn University", "address": "", "city": "", "state": "AL", "zip": "", "country": "United States", "approved": true }, "abstract": "Recent weeks and months have seen the emergence of COVID-19 as a major threat to health on a global scale. One major challenge associated with combating this disease is the lack of a rapid diagnostic device. Although current tests are sensitive, they require specially equipped laboratories and can take several days to provide results. This project aims to identify and validate antibodies for use in real-time, point-of-care, COVID-19 biosensor devices. Such devices could allow doctors and other healthcare professionals to immediately diagnose infected individuals and get them the treatment they need while more effectively containing the spread of this pandemic.SARS-CoV-2 is the viral cause of the COVID-19 illness. An antibody-based nanoplasmonic barcode biosensor could a provide real-time, point-of-care diagnostic device. This project will develop such a sensor. The first objective is the discovery of SARS-CoV-2 binding antibodies. To ensure a sufficient diversity of antibodies are identified, three parallel discovery pathways will be pursued: 1) the identification of antibodies that cross-react with SARS-CoV-2 and MERS-CoV spike proteins, 2) the rational engineering of anti- SARS-CoV-1 antibodies to bind SARS-CoV-2, and 3) the in silico, de novo design of novel SARS-CoV-2 antibodies. About four antibody pairs will be selected from the antibodies discovered through the three complementary approaches. The pairs will be used for SARS-CoV-2 detection on the basis of their affinity measured by ELISA and surface plasmon resonance and of the selectivity of their binding to unique epitopes, as monitored by competition ELISA. Finally, the antibody pairs will be used in the design and evaluation of SARS-CoV-2 nanoplasmonic biosensors. Nanoparticle signals will only be detected by the biosensors in the presence of virus. The proposed research will enable the more rapid detection of SARS-CoV-2 compared to current diagnostic tests, resulting in a better understanding of its spread and more effective containment.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.", "keywords": [], "approved": true } }, { "type": "Grant", "id": "2000", "attributes": { "award_id": "2030266", "title": "RAPID:CRISPR Whole genome screen to identify cellular machinery and pathways of SARS-CoV-2 entry into cells", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Biological Sciences (BIO)" ], "program_reference_codes": [ "096Z", "7465", "7914", "9150" ], "program_officials": [ { "id": 5344, "first_name": "Matt", "last_name": "Buechner", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2020-08-01", "end_date": "2022-01-31", "award_amount": 199475, "principal_investigator": { "id": 5345, "first_name": "Adam D", "last_name": "Hoppe", "orcid": "https://orcid.org/0000-0003-4180-0840", "emails": "[email protected]", "private_emails": "", "keywords": "['CRISPR']", "approved": true, "websites": "['https://orcs.thebiogrid.org/']", "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 591, "ror": "https://ror.org/015jmes13", "name": "South Dakota State University", "address": "", "city": "", "state": "SD", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [], "awardee_organization": { "id": 591, "ror": "https://ror.org/015jmes13", "name": "South Dakota State University", "address": "", "city": "", "state": "SD", "zip": "", "country": "United States", "approved": true }, "abstract": "This project will discover genes that help and/or inhibit the entry of the COVID-19 virus into cells using a new unbiased screening approach. This work will benefit society by creating a more comprehensive view of how COVID-19 infects cells. In addition, this work has the potential to identify host cell antiviral defense genes that can inhibit viral entry, as well as define genes that contribute to antibody protection in immune cells. Here, new CRISPR technology will be applied to screen the entire human genome to find these genes by correlating gene inactivation with increased or decreased viral entry into lung and immune cells. This information will provide the knowledge needed to develop new anti-viral strategies and to understand how environmental, genetic and cellular factors may influence the susceptibility of an individual to infection as well as the severity of the infection. The Broader Impacts of the project include training the next generation of virologists and cell biologists. Graduate students will participate in all phases of the project, including learning state-of-the-art CRISPR technologies. With the help of high school teachers, the work of this project will also be used to produce artistic descriptions that will allow broad dissemination of our findings to students, the scientific community, and the broader public.This work aims to elucidate host genes that promote and inhibit the entry of the SARS-CoV-2 virus, the causative agent of COVID-19, into epithelial cells and macrophages using new whole-genome CRISPR screening approaches. At present, the ACE2 viral receptor and the host cell protease, TMRPSS2, have been the focus of research on the machinery needed for viral entry. However, other receptors, including CD147 and other proteases can facilitate viral entry indicating that a broader perspective is needed. Conversely, little is known about the role of innate antiviral genes that may restrict viral entry. Rapid adaptation of current CRISPR whole genome screening strategies will enable identification and ranking of all genes contributing to and inhibiting SARS-CoV-2 entry into epithelial cells expressing the ACE2 receptor and macrophages via antibody/Fc receptor or CD147-mediated attachment. Screens conducted in epithelial cells are expected to provide a map of the genes that contribute to and inhibit infection as well as viral spread within the lung. While it is not yet clear the extent to which SARS-CoV-2 can replicate in macrophages, multiple lines of evidence indicate that the virus can infect macrophages in a process aided by the presence of antibodies that may modulate their inflammatory state contributing to COVID-19. The screening strategy of the Project using pseudotyped lentiviral vectors will enable detection of viral entry, absent viral replication, and will provide a description of the genes aiding and inhibiting antibody-dependent viral entry into macrophages. Comprehensive genetic analysis across both cell types will provide an unprecedented view of viral entry and will provide scientific knowledge urgently needed to combat COVID-19.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.", "keywords": [], "approved": true } }, { "type": "Grant", "id": "1359", "attributes": { "award_id": "2030473", "title": "RAPID: Structure of Membrane-Bound Fusion Peptide of SARS-CoV-2 Required for Infection", "funder": { "id": 3, "ror": "https://ror.org/021nxhr62", "name": "National Science Foundation", "approved": true }, "funder_divisions": [ "Biological Sciences (BIO)" ], "program_reference_codes": [ "096Z", "7465", "7914", "9150" ], "program_officials": [ { "id": 3503, "first_name": "Jaroslaw", "last_name": "Majewski", "orcid": null, "emails": "", "private_emails": "", "keywords": null, "approved": true, "websites": null, "desired_collaboration": null, "comments": null, "affiliations": [] } ], "start_date": "2020-06-01", "end_date": "2023-05-31", "award_amount": 200000, "principal_investigator": { "id": 3504, "first_name": "Steven R Van", "last_name": "Doren", "orcid": null, "emails": "[email protected]", "private_emails": "", "keywords": "['Biomolecular recognition']", "approved": true, "websites": "['https://cafnr.missouri.edu/person/steven-van-doren/', 'https://cafnrfaculty.missouri.edu/vandoren/']", "desired_collaboration": null, "comments": null, "affiliations": [ { "id": 292, "ror": "", "name": "University of Missouri-Columbia", "address": "", "city": "", "state": "MO", "zip": "", "country": "United States", "approved": true } ] }, "other_investigators": [], "awardee_organization": { "id": 292, "ror": "", "name": "University of Missouri-Columbia", "address": "", "city": "", "state": "MO", "zip": "", "country": "United States", "approved": true }, "abstract": "The 2019 novel coronavirus spread quickly and became a global pandemic. Infection by an enveloped virus, like SARS-CoV-2, requires fusion of the viral membrane with a host cell membrane. This NSF Rapid Response Research (RAPID) project will support studies to characterize a coronavirus fusion peptide before and after it binds to the cell membrane. The understanding of this process will inform the active development of vaccines and antibodies. The scientific activities will provide a special opportunity for the PI and his lab members to show local high school students how basic research can assist technology development to safeguard public health and safety.The nuclear magnetic resonance (NMR)-guided studies of SARS-CoV-2 docking into the human cells will provide the first structural models of lipid bilayer coordinates bound to a viral fusion peptide, thereby providing details of fusion peptide manipulation of the lipids. The results will prompt immune developers to consider the presence and format of the fusion peptide as antigen. The dynamic structure of the unbound state of the fusion peptide should represent its behavior as a solvent-exposed antigen and the structure of its bilayer-associated state will inform about sites accessible to antibodies outside the bilayer. This RAPID award is made by the Molecular Biophysics Program in the Division of Molecular and Cellular Biosciences, using funds from the Coronavirus Aid, Relief, and Economic Security (CARES) Act.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.", "keywords": [], "approved": true } } ], "meta": { "pagination": { "page": 1384, "pages": 1442, "count": 14420 } } }