Molecular changes associated with adaptation of human influenza A virus in embryonated chicken eggs are reported: 4 amino acid substitutions occurred in HA (G186V, S219F, V226I, V309I). These substitutions allowed binding to SAalpha2,3Gal- and SAalpha2,6Gal-containing receptors, conferred SAalpha2,3Gal specificity, and preserved antigenicity. Here, the author reports the result of protein secondary structure predictions of the adaption from its primary sequence using the NNPREDICT server. Comparing the classical HA of H3N2, the adaptation has additional helices and strands and these identified structural changes should be the explanation for the reported binding and antigenicity changes.

Molecular changes associated with adaptation of human influenza A virus in embryonated chicken eggs are reported: 4 amino acid substitutions occurred in HA (G186V, S219F, V226I, V309I). These substitutions allowed binding to SAalpha2,3Gal- and SAalpha2,6Gal-containing receptors, conferred SAalpha2,3Gal specificity, and preserved antigenicity. Here, the author reports the result of protein secondary structure predictions of the adaption from its primary sequence using the NNPREDICT server. Comparing the classical HA of H3N2, the adaptation has additional helices and strands and these identified structural changes should be the explanation for the reported binding and antigenicity changes.