2026-09-23T13:35:59Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/115681 2023-07-11 col_2142_5131 col_2142_14795 com_2142_5130 com_2142_14794 com_2142_14793 com_2142_8903

The student, ChuYun Teo, submitted this Thesis for approval on 2022-04-05 at 15:02. This Thesis was approved for publication on 2022-04-08 at 10:08. DSpace SAF Submission Ingestion Package generated from Vireo submission #17591 on 2022-11-11 at 12:18:53 Wu, Nicholas C 2022-05 application/pdf en text Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2024-05-01 The student, ChuYun Teo, accepted the attached license on 2022-04-05 at 14:55. The biophysical evolution of human influenza H3N2 neuraminidase Teo, ChuYun 2022-04-08 H3N2 Influenza A virus Neuraminidase Enzymatic activity Stability Surface expression. 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. Thesis eng https://hdl.handle.net/2142/115681 Copyright 2022 ChuYun Teo M.S. Thesis Biochemistry University of Illinois at Urbana-Champaign Biochemistry