Substitutions in position 222 of haemagglutinin of pandemic influenza A (H1N1) 2009 viruses in Spain

Emergent 2009 influenza A(H1N1) viruses containing HA D222N mutation associated with severe clinical outcomes in the Americas

“…7,11,15,16 Further, nine D222 variants carrying changes to glycine (G), asparagine (N) or mixed D222G/N were isolated and identified from 17 autopsy samples from the Russian Federation. 17 Fewer than 30 viruses with the D222N mutation were identified and published in public databases since the beginning of the 2009 pandemic, and these are genetically distinct from those clustering within the novel sub-clade (Fig.…”

Sialic acid receptors: focus on their role in influenza infection

“…The first marker of pathogenicity and severe clinical outcome has been associated to a single point mutation D225G at the RBS of the HA, which has been detected in viruses from several countries around the world. [30][31][32][33][34] Studies using experimental in vivo models analyzing the pathogenic effect of the mutation D225G are controversial; [34][35][36][37] foremost, the amino acid residue 225 has shown polymorphism for 225D/G/N in the HA of the H1N1pdm09 virus. 38,39 Overall, viruses with 225G phenotype showed changes in the virus receptor-binding profile and the cell/tissue tropism and dual binding for SAα2,6 and SAα2,3.…”

Theoretical Investigation on the Binding Specificity of Sialyldisaccharides with Hemagglutinins of Influenza A Virus by Molecular Dynamics Simulations

“…A single amino acid change in the receptor-binding site of hemagglutinin of influenza A virus alters the binding specificity from N23G to N26G (38,39). It has been reported by Taubenberger and co-workers (40) that mutation at positions 190 and 225 (E190D and G225D) and 226 and 228 (Q226K and G228S) will affect the binding specificity to sialic acid.…”