Result: Control HAs, the A/H5N1 IN/05 wild-type (WT) HA (unstable), the A/H5N1 IN/05 HA carrying airborne-transmission substitutions (H103Y, T156A, Q222L, and G224S [H5 numbering used throughout]) (stable), and the human A/H3N2 NL/03 HA (stable), were included.
Potential Pandemic of H7N9 Avian Influenza A Virus in Human.
PMID: 30533399
2018
Frontiers in cellular and infection microbiology
Result: Amino acid changes S155N, T156A, G182V, S205Y, and Q222L (H5 numbering) in HA had very high proportions in both human- and avian-isolated H7N9 (Figure 1A).
Result: In waves 1-4, Q222L in HA and K526R in PB2 had high proportions in both human- and avian-isolated H7N9.
Discussion: Amino acid changes S155N, T156A, G182V, S205Y, and Q222L (H5 numbering) in HA increase virus-binding to human alpha-2,6 sialo-saccharide
Amino Acid Substitutions Associated with Avian H5N6 Influenza A Virus Adaptation to Mice.
Discussion: Among all six airborne-transmissible viruses, in addition to the three introduced mutations (Q222L and G224S in HA and E627K in PB2), two new amino acid substitutions were consistently detected: H103Y and T156A (both in HA).
Discussion: The Q222L and G224S amino acid mutations not only enhanced the binding of the H5N1 virus to alpha2,6 receptors, but also increased its affinity for alpha2,3 receptor, which probably conferred transmissibility to this H5N1 strain.
Novel Polymerase Gene Mutations for Human Adaptation in Clinical Isolates of Avian H5N1 Influenza Viruses.
Discussion: A ferret-transmission experiment showed that an H5N1 virus acquired both HA and polymerase mutations during adaptation to a new host, even though the virus used in that study was a recombinant virus intentionally carrying the well-known adaptation mutations PB2-E627K and HA-Q222L/G224S.
Prediction of avian influenza A binding preference to human receptor using conformational analysis of receptor bound to hemagglutinin.
Introduction: The H5 HA X-ray structure from A/Duck/Singapore/3/97 (abbreviated as Sing-97) shows preferential binding to Siaalpha(2,3)Gal receptor, owing to Q222L and G224S mutations.
Discussion: The order of selectivity toward Siaalpha(2,6)Gal binding was Puerto-34 > L129V/A134V Kan-1 Q222L/G224S Sing-97 >
Discussion: The two single mutations, Q222L and G224S cause a loss in human receptor affinity as shown by fluctuations to the trans-conformation, while the double mutation Q222L/G224S maintained its preference for human receptor as the bound alpha(2,6) glycosides were in the cis conformation.
IV mutation literature information.
PMID: 
2018
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