tetano
Editor, Senior Moderator
PLoS One. 2013 Jul 23;8(7):e70005. doi: 10.1371/journal.pone.0070005. Print 2013.
Analysis of Adaptation Mutants in the Hemagglutinin of the Influenza A(H1N1)pdm09 Virus.
Jim?nez-Alberto A, Alvarado-Facundo E, Ribas-Aparicio RM, Castel?n-Vega JA.
Source
Departamento de Microbiolog?a, Escuela Nacional de Ciencias Biol?gicas del Instituto Polit?cnico Nacional, Distrito Federal, Mexico City, Mexico.
Abstract
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.
PMID:
23894575
[PubMed - in process]
PMCID:
PMC3720954
Free PMC Article
http://www.ncbi.nlm.nih.gov/pubmed/23894575
Analysis of Adaptation Mutants in the Hemagglutinin of the Influenza A(H1N1)pdm09 Virus.
Jim?nez-Alberto A, Alvarado-Facundo E, Ribas-Aparicio RM, Castel?n-Vega JA.
Source
Departamento de Microbiolog?a, Escuela Nacional de Ciencias Biol?gicas del Instituto Polit?cnico Nacional, Distrito Federal, Mexico City, Mexico.
Abstract
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.
PMID:
23894575
[PubMed - in process]
PMCID:
PMC3720954
Free PMC Article
http://www.ncbi.nlm.nih.gov/pubmed/23894575