Locating and Predicting Ligand-Binding Epitope Regions on the Enterovirus Genus with Icosahedral Point Array Asymmetric Units
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Authors
Blanzy, Preston T.
Issue Date
2024-06-01
Type
Thesis
Language
en_US
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Abstract
Virus capsids are comprised of many copies of one or several different types of capsid protein subunits. Its function is to protect the viral genetic material located within, as well as provide aid to host cell attachment. Typically, virus capsid structure can be separated by having helical or icosahedral symmetry. Icosahedral capsids describe roughly 50% of virus families, their structure is described by 20 equilateral triangular faces, 30 edges, and 12 vertices. Viruses that pertain to this form of symmetry can be classified via Triangulation Number; a method that focuses on the arrangement of protein subunits that form the capsid. T-Number Classification leads to the use of point arrays, which provide specific geometric constraints on a viruses capsid and genetic material. This modified fitting method uses gauge points to determine the overall radial scaling, which are located on the symmetrical axes of asymmetric units. This method indicates geometric locations where viruses can be modified with care, and locations where modifications are relatively easy to perform. Antivirals and vaccines can use the information given through these point arrays to find target sites to inhibit viruses from infecting the host and fully maturing. By using the best fitting point arrays for native virus capsids, radially increasing the scaling of these PAs was hypothesized to be able to describe ligand-binding epitope regions on the capsid. Native capsids for the enterovirus genus were analyzed, then compared to their virus with its receptor bound complexed to it. The algorithms used for this method were able to locate these regions on pre-complexed viruses, verifying that point arrays are a valuable method for future research in this field.
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14 p.
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