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Updated: Jun 28, 2025
11:20
Affinity Purification of Influenza Virus Ribonucleoprotein Complexes from the Chromatin of Infected Cells
Published on: June 3, 2012
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The immune-evasive proline-283 substitution in influenza nucleoprotein increases aggregation propensity without
Jimin Yoon1, Yu Meng Zhang1, Cheenou Her2
1Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.
Science Advances
|April 19, 2024
Summary
Influenza nucleoprotein
Area of Science:
- Virology
- Structural Biology
- Innate Immunity
Background:
- Nucleoprotein (NP) is crucial for influenza virus replication and packaging.
- NP influences viral sensitivity to host innate immunity factors like MxA.
- A specific NP mutation (Pro-283) confers resistance to MxA but impairs viral fitness.
Purpose of the Study:
- To investigate if the Pro-283 substitution in NP causes folding defects leading to impaired influenza growth.
- To biophysically characterize wild-type (Ser-283) and mutant (Pro-283) NP.
Main Methods:
- Biophysical characterization of NP variants.
- Analysis of protein folding pathways and aggregation propensity.
Main Results:
- The Pro-283 substitution alters NP's folding pathway.
- Pro-283 NP exhibits increased aggregation during folding.
- The native structure of NP remains unchanged by the Pro-283 substitution.
Conclusions:
- The Pro-283 substitution introduces a folding defect, not a structural defect, in influenza NP.
- Influenza viruses may utilize host chaperones to fold essential viral proteins for immune evasion.
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