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Updated: Dec 11, 2025
Co-immunoprecipitation of the Mouse Mx1 Protein with the Influenza A Virus Nucleoprotein
Published on: April 21, 2015
Experimental validation of influenza A virus matrix protein (M1) interaction with host cellular alpha enolase and
Shruti Mishra1, Priya Goyal1, Deepshikha Kumar1
1Molecular Virology Laboratory, School of Biotechnology, Jawaharlal Nehru University, New Delhi, India.
Abstract:
Influenza A virus, a respiratory pathogen manipulates various host cellular processes to establish a successful infection in a host. We had reported earlier the interaction of influenza A virus nucleoprotein with host glycolytic enzymes; alpha enolase and pyruvate kinase in A549 cells. Matrix protein (M1), another multifunctional protein encoded by genome segment 7 forms the inner layer of the virion and interacts with the ribonucleoprotein complex. Nucleoprotein and matrix protein, major structural components of the virion together contribute to the stability of the capsid. Thus, we have investigated the interaction of viral matrix protein with host glycolytic enzymes; alpha enolase and pyruvate kinase. Results had demonstrated differential expression of these two glycolytic enzymes in response to matrix protein and their interaction with matrix protein by in vitro binding, co-immunoprecipitation and co-localization studies. Our results confirmed that viral matrix protein interacts with host glycolytic enzymes in association with viral nucleoprotein.
Insights
Influenza A virus matrix protein (M1) interacts with host glycolytic enzymes, alpha enolase and pyruvate kinase. This interaction occurs alongside the viral nucleoprotein, impacting host cell processes during infection.
Area of Science:
- Virology
- Molecular Biology
- Biochemistry
Background:
- Influenza A virus is a respiratory pathogen that hijacks host cellular processes.
- Previous studies reported interactions between influenza A virus nucleoprotein and host glycolytic enzymes alpha enolase and pyruvate kinase.
- The viral matrix protein (M1) is crucial for virion structure and ribonucleoprotein complex interaction.
Purpose of the Study:
- To investigate the interaction between the influenza A virus matrix protein (M1) and host glycolytic enzymes, specifically alpha enolase and pyruvate kinase.
- To elucidate the role of M1 protein in modulating host cell metabolism during viral infection.
Main Methods:
- In vitro binding assays to assess direct protein-protein interactions.
- Co-immunoprecipitation studies to confirm interactions in a cellular context.
- Co-localization experiments to determine the spatial relationship between viral proteins and host enzymes within infected cells.
- Analysis of differential gene expression of glycolytic enzymes in response to M1 protein.
Main Results:
- Differential expression of alpha enolase and pyruvate kinase was observed in response to the influenza A virus M1 protein.
- Direct binding, co-immunoprecipitation, and co-localization studies confirmed the interaction between M1 protein and host glycolytic enzymes.
- The interaction of M1 protein with these enzymes was found to be associated with the viral nucleoprotein.
Conclusions:
- Influenza A virus matrix protein (M1) interacts with host glycolytic enzymes alpha enolase and pyruvate kinase.
- These interactions are dependent on the presence of the viral nucleoprotein.
- The findings suggest a role for M1 protein in manipulating host metabolic pathways through interaction with glycolytic enzymes, potentially aiding viral replication and pathogenesis.
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