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. Author manuscript; available in PMC: 2024 Sep 1.
Published in final edited form as: Antiviral Res. 2023 Aug 9;217:105701. doi: 10.1016/j.antiviral.2023.105701

Fig. 2. Binding modes of AV5080 (the carbon backbone is shown in purple) and oseltamivir (the carbon backbone is shown in orange) in the active site of NA of influenza A and B viruses with different NA substitutions (in green).

Fig. 2.

(A) The model of A/Vietnam/1203/2004 (H5N1) (PDB code: 2HU0) NA-E119G substitution leads to the loss of salt bridge contact between the NA amino acid residue and the guanidine moiety of zanamivir or AV5080. (B) The model of A/Tanzania/205/2010 (H3N2) (PDB code: 4GZP) NA-R292K substitution leads to the loss of hydrogen bonding stability and xH-π interactions with AV5080. (C) The model of Victoria Lineage B/Lyon/CHU/15.216/2011 (PDB code: 4CPZ) NA-I221L substitution can make the Ile221–Arg151–Asp197 cluster more labile within the NA active site. (D) The model of Yamagata lineage B/Brisbane/60/2008 (PDB code: 4CPN) NA-R150K substitution likely causes loss of contact with the carbonyl oxygen of AV5080.