The biophysical evolution of human influenza H3N2 neuraminidase

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.

Name thesis:degree_name

M.S.

Level thesis:degree_level

Thesis

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2022

Author dc:creator

• Teo, ChuYun

Contributors dc:contributor

• Wu, Nicholas C

• H3N2 Influenza A virus
• Neuraminidase
• Enzymatic activity
• Stability
• Surface expression.

Statement dc:rights

• Copyright 2022 ChuYun Teo

Language dc:language

en, eng

Handle dc:identifier

https://hdl.handle.net/2142/115681

OAI record oai:identifier

https://www.ideals.illinois.edu/oai-pmh?verb=GetRecord&metadataPrefix=etdms&identifier=oai%3Awww.ideals.illinois.edu%3A2142%2F115681