Related Experiment Video
Updated: Mar 29, 2026

Affinity Purification of Influenza Virus Ribonucleoprotein Complexes from the Chromatin of Infected Cells
Published on: June 3, 2012
Proteasomes raise the microtubule dynamics in influenza A (H1N1) virus-infected LLC-MK2 cells
Abstract:
The dynamics of microtubule networks are known to have an impact on replication of influenza A virus in some cellular models. Here we present evidence suggesting that at late stages of LLC-MK2 cell infection by influenza A (H1N1) virus the ubiquitin-proteasome protein degradation system participates in destabilization of microtubules, and favours virus replication. Chemical inhibition of proteasome activity partially suppresses influenza A virus replication, while stimulation of proteasome activity favours influenza A virus replication. Conversely, in another cellular model, A549 cells, inhibitors and activators of proteasomes have a small effect on influenza A virus replication. These data suggest that influenza A virus might take selective advantage of proteasome functions in order to set up a favourable cytoskeletal "environment" for its replication and spread. Furthermore, the relationship between influenza virus and the host cell is likely to depend on both the cellular model and the virus strain.
Insights
Influenza A virus replication is influenced by microtubule dynamics and the ubiquitin-proteasome system. Proteasome activity destabilizes microtubules, favoring virus replication in LLC-MK2 cells but not A549 cells.
Area of Science:
- Virology
- Cell Biology
- Biochemistry
Background:
- Microtubule network dynamics are implicated in the replication of influenza A virus.
- The role of the ubiquitin-proteasome system in viral replication is not fully understood.
Purpose of the Study:
- To investigate the involvement of the ubiquitin-proteasome system in influenza A virus replication.
- To determine the impact of proteasome activity on microtubule destabilization during infection.
Main Methods:
- Infection of LLC-MK2 and A549 cells with influenza A (H1N1) virus.
- Chemical inhibition and stimulation of proteasome activity.
- Observation of virus replication rates and microtubule network stability.
Main Results:
- In LLC-MK2 cells, proteasome activity destabilized microtubules and enhanced influenza A virus replication.
- Inhibition of proteasomes partially suppressed virus replication, while stimulation favored it.
- A549 cells showed minimal impact of proteasome modulators on virus replication.
Conclusions:
- Influenza A virus may exploit proteasome functions to create a favorable cytoskeletal environment for replication.
- The host cell type and virus strain significantly influence the interplay between influenza virus and host proteasome activity.
Related Concept Videos
Microtubule Instability
Microtubule Instability
Leaky Scanning
The Proteasome
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Regulated Protein Degradation
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...

