Analysis of adaptation mutants in the hemagglutinin of the influenza A(H1N1)pdm09 virus

Hemagglutinin is the major surface glycoprotein of influenza viruses. It participates in the initial steps of viral infection through receptor binding and membrane fusion events. The influenza pandemic of 2009 provided a unique scenario to study virus evolution. We performed molecular dynamics simul...

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Bibliographic Details
Published in:PloS one 2013-07, Vol.8 (7), p.e70005-e70005
Main Authors: Jiménez-Alberto, Alicia, Alvarado-Facundo, Esmeralda, Ribas-Aparicio, Rosa María, Castelán-Vega, Juan A
Format: Article
Language:English
Subjects:
Adaptation
Adaptation, Physiological - genetics
Antigenic drift
Antigens
Binding
Biology
Chemistry
Epidemiology
Genomes
Glycoproteins
Hemagglutinin Glycoproteins, Influenza Virus - chemistry
Hemagglutinin Glycoproteins, Influenza Virus - genetics
Hemagglutinin Glycoproteins, Influenza Virus - immunology
Hemagglutinin Glycoproteins, Influenza Virus - metabolism
Hemagglutinins
Humans
Influenza
Influenza A
Influenza A Virus, H1N1 Subtype - genetics
Influenza A Virus, H1N1 Subtype - immunology
Influenza A Virus, H1N1 Subtype - metabolism
Influenza A Virus, H1N1 Subtype - physiology
Influenza Pandemic, 1918-1919
Influenza, Human - epidemiology
Influenza, Human - virology
Ligands
Medicine
Membrane fusion
Molecular dynamics
Molecular Dynamics Simulation
Molecular Epidemiology
Mutants
Mutation
Pandemics
Proteins
RNA polymerase
Static Electricity
Surface Properties
Swine flu
Thermodynamics
Viruses
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Summary:Hemagglutinin is the major surface glycoprotein of influenza viruses. It participates in the initial steps of viral infection through receptor binding and membrane fusion events. The influenza pandemic of 2009 provided a unique scenario to study virus evolution. We performed molecular dynamics simulations with four hemagglutinin variants that appeared throughout the 2009 influenza A (H1N1) pandemic. We found that variant 1 (S143G, S185T) likely arose to avoid immune recognition. Variant 2 (A134T), and variant 3 (D222E, P297S) had an increased binding affinity for the receptor. Finally, variant 4 (E374K) altered hemagglutinin stability in the vicinity of the fusion peptide. Variants 1 and 4 have become increasingly predominant, while variants 2 and 3 declined as the pandemic progressed. Our results show some of the different strategies that the influenza virus uses to adapt to the human host and provide an example of how selective pressure drives antigenic drift in viral proteins.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0070005