Acquisition of Human-Type Receptor Binding Specificity by New H5N1 Influenza Virus Sublineages during Their Emergence in Birds in Egypt
Analysis of receptor docking modes of EG/D1 HA and HA mutants.
Structural models of H5 HA. (A) Ribbon model of EG/D1 HA. The trimeric globular-head region is shown. Key residues in our analysis are shown in a colored space-filling model. Receptor binding domains are colored blue (130 loop), green (190 helix) and purple (220 loop). (B) Molecular surface of EG/D1 HA. The red circle indicates the receptor binding pocket. (C) Docking models for EG/D1, EG/D1Q192H and EG/D1129Δ,I151T HA with a human-type receptor analog (PDBID code 1MQN). Residues 127E, 128A, 130S and 131G are colored green, as is 129S, and the other residues and domains are displayed in the same colors as above. An additional hydrogen bond between E127 and T151 is indicated in the red circle. The Udock scores of the corresponding complexes are shown at the bottom.