The hemagglutinin of the influenza A(H1N1)pdm09 is mutating towards stability.

ABSTRACT: The last influenza A pandemic provided an excellent opportunity to study the adaptation of the influenza A(H1N1)pdm09 virus to the human host. Particularly, due to the availability of sequences taken from isolates since the beginning of the pandemic until date, we could monitor amino acid changes that occurred in the hemagglutinin (HA) as the virus spread worldwide and became the dominant H1N1 strain. HA is crucial to viral infection because it binds to sialidated cell-receptors and mediates fusion of cell and viral membranes; because antibodies that bind to HA may block virus entry to the cell, this protein is subjected to high selective pressure. Multiple alignment analysis of sequences of the HA from isolates taken since 2009 to date allowed us to find amino acid changes that were posit

SUBMITTER: Castelan-Vega JA 

PROVIDER: S-EPMC4198066 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature