How the influenza virus achieves efficient viral RNA replication

October 03, 2019

New insights on how subunits of the influenza virus polymerase co-evolve to ensure efficient viral RNA replication are provided by a study published October 3 in the open-access journal PLOS Pathogens by Nadia Naffakh of the Institut Pasteur, and colleagues. As the authors note, the findings could lead to novel strategies for antiviral drug development.

Because of their yearly recurrence and the occasional emergence of pandemics, influenza viruses represent a worldwide major public health threat. Enhancing fundamental knowledge about the influenza RNA-polymerase, which is an enzyme that consists of three subunits (i.e., a heterotrimer) and ensures transcription and replication of the viral genome, is essential to reach the goal of better prevention and treatment of disease.

In the new study, Naffakh and colleagues gained new insights into viral polymerase function. They showed that the polymerase subunits co-evolve to ensure not only optimal inter-subunit cooperation within the heterotrimer, but also proper levels dimerization - the process by which pairs of heterotrimers attach together -- which appears to be essential for efficient viral RNA replication. The findings point to influenza polymerase dimerization as a feature that can restrict genetic reassortment, a major evolutionary mechanism in which influenza viruses swap gene segments, and could become an attractive target for antiviral drug development.
Research Article

Funding: The author(s) received no specific funding for this work.

Competing Interests: The authors have declared that no competing interests exist.

Citation: Chen K-Y, Santos Afonso ED, Enouf V, Isel C, Naffakh N (2019) Influenza virus polymerase subunits co-evolve to ensure proper levels of dimerization of the heterotrimer. PLoS Pathog 15(10): e1008034.

Author Affiliations:

Unité de Génétique Moléculaire des Virus à ARN, Institut Pasteur, UMR 3569 CNRS, Paris, France

Unité de Génétique Moléculaire des Virus à ARN, Université Paris Diderot, Sorbonne Paris Cité, Paris, France

Unité de Génétique Moléculaire des Virus à ARN, Centre National de Référence des Virus des Infections Respiratoires, Institut Pasteur, Paris, France

Pasteur International Bioresources network (PIBnet), Plateforme de Microbiologie Mutualisée (P2M), Institut Pasteur, Paris, France

In your coverage please use this URL to provide access to the freely available paper:


Related Polymerase Articles from Brightsurf:

Researchers identify multiple molecules that shut down SARS-Cov-2 polymerase reaction
Researchers at Columbia Engineering and the University of Wisconsin-Madison have identified a library of molecules that shut down the SARS-CoV-2 polymerase reaction, a key step that establishes the potential of these molecules as lead compounds to be further modified for the development of COVID-19 therapeutics.

MU researcher identifies four possible treatments for COVID-19
While COVID-19 has infected millions of people worldwide and killed hundreds of thousands, there is currently no vaccine.

Structural visualizations illuminate remdesivir's mechanism of action
In a new study, researchers report the structure of remdesivir -- an antiviral drug that has shown promise against the SARS-CoV-2 virus in lab studies and early clinical trials -- bound to both a molecule of RNA and to the viral polymerase.

Study sheds light on how a drug being tested in COVID-19 patients works
As hospitalized COVID-19 patients undergo experimental therapy, research published in the Journal of Biological Chemistry explains how the drug, remdesivir, stops replication in coronaviruses.

Pioneering research gives fresh insight into 1 of the pivotal building blocks of life
The quest to better understand how genomic information is read has taken a new step forward, thanks to pioneering new research.

How the influenza virus achieves efficient viral RNA replication
New insights on how subunits of the influenza virus polymerase co-evolve to ensure efficient viral RNA replication are provided by a study published Oct.

New study discovers the three-dimensional structure of the genome replication machine
Mount Sinai researchers have discovered how the enzyme DNA polymerase delta works to duplicate the genome that cells hand down from one generation to the next.

Researchers identify key areas of measles virus polymerase to target for antiviral drug development
Targeting specific areas of the measles virus polymerase, a protein complex that copies the viral genome, can effectively fight the measles virus and be used as an approach to developing new antiviral drugs to treat the serious infectious disease, according to a study by the Institute for Biomedical Sciences at Georgia State University published in PLoS Pathogens.

Chemical modifiers tag-team to regulate essential mechanism of life
For decades, scientists thought that one modification, phosphorylation, ran the show.

New giant virus may help scientists better understand the emergence of complex life
A team of scientists led by virologist Masaharu Takemura at Tokyo University of Science and Hiroyuki Ogata at Kyoto University in Japan have discovered a giant virus that, much like the mythical monster Medusa, can turn almost amoeba to a stone-like cyst.

Read More: Polymerase News and Polymerase Current Events is a participant in the Amazon Services LLC Associates Program, an affiliate advertising program designed to provide a means for sites to earn advertising fees by advertising and linking to