The biophysical evolution of human influenza H3N2 neuraminidase
Teo, ChuYun
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Permalink
https://hdl.handle.net/2142/115681
Description
Title
The biophysical evolution of human influenza H3N2 neuraminidase
Author(s)
Teo, ChuYun
Issue Date
2022-04-08
Director of Research (if dissertation) or Advisor (if thesis)
Wu, Nicholas C
Department of Study
Biochemistry
Discipline
Biochemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
M.S.
Degree Level
Thesis
Keyword(s)
H3N2 Influenza A virus, Neuraminidase, Enzymatic activity, Stability, Surface expression.
Abstract
The viral surface glycoprotein neuraminidase (NA) of influenza A virus (H3N2) has continue to evolve over the past 50 years. To date, NA has become one of the vaccine targets and the evolution of NA in escaping immune response is rarely explored. This study aimed towards understanding the biophysical properties of different human H3N2 NA strains that were isolated across 50 years. This study employed biochemical assay to detect NA expression, cell surface activity, protein activity, and stability. Our analysis showed that NA with higher surface expression has stronger cell surface enzyme activity. In addition, protein stability had no effect on the recombinant NA enzymatic activity. Overall, these results provide a mechanistic understanding of NA evolution of human H3N2 influenza A virus.
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