RAPID: Structure of Membrane-Bound Fusion Peptide of SARS-CoV-2 Required for Infection
- Funded by National Science Foundation (NSF)
- Total publications:2 publications
Grant number: 2030473
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Key facts
Disease
COVID-19Start & end year
20202021Known Financial Commitments (USD)
$200,000Funder
National Science Foundation (NSF)Principal Investigator
Steven Van DorenResearch Location
United States of AmericaLead Research Institution
University of Missouri-ColumbiaResearch Priority Alignment
N/A
Research Category
Pathogen: natural history, transmission and diagnostics
Research Subcategory
Pathogen morphology, shedding & natural history
Special Interest Tags
N/A
Study Type
Non-Clinical
Clinical Trial Details
N/A
Broad Policy Alignment
Pending
Age Group
Not Applicable
Vulnerable Population
Not applicable
Occupations of Interest
Not applicable
Abstract
Biological Sciences - 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.
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.
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