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 IV mutation literature information.


  Highly pathogenic avian influenza H7N9 viruses with reduced susceptibility to neuraminidase inhibitors showed comparable replication capacity to their sensitive counterparts.
 PMID: 31266524       2019       Virology journal
Abstract: CONCLUSIONS: All 4 amino acid substitutions (R292 K, E119V, A246T or H274Y) in NA reduced the susceptibility of HPAI H7N9 to NAIs.
Abstract: RESULTS: Four potential NAI resistance sites, R292 K, E119V, A246T or H274Y, were screened.
Method: A virus containing amino acid substitutions in sites related to potentially reduced susceptibility to NAIs in HPAI H7N9 viruses, including R292 K, E119V,


  Unique Determinants of Neuraminidase Inhibitor Resistance among N3, N7, and N9 Avian Influenza Viruses.
 PMID: 26292325       2015       Journal of virology
Abstract: In a fluorescence-based NA inhibition assay, we identified three categories of NA substitutions associated with reduced inhibition by NAIs (oseltamivir, zanamivir, and peramivir): (i) novel subtype-specific substitutions in or near the enzyme catalytic site (R152W, A246T, and D293N, N2 numbering), (ii) subtype-independent substitutions (E119G/V and/or D and R292K), and (iii) substitutions previously reported in other subtypes (Q136K, I222M, and E276D).



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