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Updated: May 16, 2026

Affinity Purification of Influenza Virus Ribonucleoprotein Complexes from the Chromatin of Infected Cells
Published on: June 3, 2012
[PB1-F2 protein of influenza A virus interacts with human MOAP-1 protein]
Yuming Cui1, Peili Hou, Maolin Zhang
1Key Laboratory of Zoonosis Ministry of Education, institute of zoonosis, Jilin University, Changchun 130062, China. cuiyuming25@163.com
Objective:
To identify the interaction between influenza A virus PB1-F2 and human modulator of apoptosis 1 (MOAP-1).
Methods:
The recombinant plasmid pACT2-MOAP-1 was constructed and co-transformed into yeast AH109 with pGBKT7-PB1-F2. The growth of the co-transformants on quadruple dropout medium and beta-galactosidase activity of the reporter gene were tested. We further confirmed the interaction of cellular protein MOAP-1 and PB1-F2 by glutathione S-transferase (GST) pull-down and co-immunoprecipitation (Co-IP) assays. In addition, we investigated the effect of PB1-F2 on MOAP-1 protein level by Western blot.
Results:
The results of yeast two-hybrid assay showed that MOAP-1 specifically interacted with PB1-F2 in yeast cells. Furthermore, the binding of MOAP-1 with PB1-F2 was demonstrated by glutathione S-transferase pull-down and Co-IP assays. PB1-F2 could upregulate exogenous MOAP-1 protein level.
Conclusion:
These results suggested that influenza virus PB1-F2 interacted with MOAP-1 and it might be involved in the regulation of cell growth and apoptosis via association with MOAP-1.
Insights
Influenza A virus PB1-F2 protein interacts with human modulator of apoptosis 1 (MOAP-1). This interaction may regulate cell growth and apoptosis.
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Context:
- Influenza A virus is a significant human pathogen.
- The viral protein PB1-F2 is known to modulate host cell functions.
- Modulator of apoptosis 1 (MOAP-1) is a key regulator of apoptosis.
Purpose:
- To investigate the potential interaction between influenza A virus PB1-F2 and human MOAP-1.
- To elucidate the functional consequences of this interaction.
Summary:
- Yeast two-hybrid assays, GST pull-down, and co-immunoprecipitation confirmed specific binding between PB1-F2 and MOAP-1.
- PB1-F2 was found to upregulate exogenous MOAP-1 protein levels.
- These findings indicate a direct interaction between the viral protein and a host apoptosis regulator.
Impact:
- The interaction suggests a novel mechanism by which influenza A virus may manipulate host cell processes.
- PB1-F2's association with MOAP-1 could play a role in viral pathogenesis by influencing cell growth and apoptosis.
- This research provides a foundation for further studies into viral control of host cell death pathways.
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