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Functional and structural analysis of influenza virus neuraminidase N3 offers further insight into the mechanisms of oseltamivir resistance.

Li Q, Qi J, Wu Y, Kiyota H, Tanaka K, Suhara Y, Ohrui H, Suzuki Y, Vavricka CJ, Gao GF
J Virol 87 10016-24 (2013)
Related entries: 4hzv, 4hzw, 4hzx, 4hzz, 4i00

Cited: 21 times
EuropePMC logo PMID: 23824808

Abstract

The influenza virus neuraminidase H274Y substitution is a highly prevalent amino acid substitution associated with resistance to the most heavily used influenza drug, oseltamivir. Previous structural studies suggest that the group specific 252 residue (Y252 in group 1 and T252 in group 2) might be a key factor underlying H274Y resistance. However, H274Y has only been reported in N1 subtypes, which indicates that there must be additional key residues that determine H274Y resistance. Furthermore, we found that members of NA serotype N3 also possess Y252, raising the key question as to whether or not H274Y resistance may also be possible for some group 2 NAs. Here, we demonstrate that the H274Y substitution results in mild oseltamivir resistance for N3. Comparative structural analysis of N3, N1, and their 274Y variants indicates that the interaction of residue 296 (H in N1 and nonaromatic for other serotypes) with conserved W295 is another important determinant of oseltamivir resistance.

Articles - 4hzy mentioned but not cited (1)

  1. Functional and structural analysis of influenza virus neuraminidase N3 offers further insight into the mechanisms of oseltamivir resistance. Li Q, Qi J, Wu Y, Kiyota H, Tanaka K, Suhara Y, Ohrui H, Suzuki Y, Vavricka CJ, Gao GF. J Virol 87 10016-10024 (2013)


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  2. Bat-derived influenza-like viruses H17N10 and H18N11. Wu Y, Wu Y, Tefsen B, Shi Y, Gao GF. Trends Microbiol 22 183-191 (2014)
  3. Influenza Neuraminidase Characteristics and Potential as a Vaccine Target. Creytens S, Pascha MN, Ballegeer M, Saelens X, de Haan CAM. Front Immunol 12 786617 (2021)
  4. Single enzyme nanoparticle, an effective tool for enzyme replacement therapy. Kim DH, Lee HS, Kwon TW, Han YM, Kang NW, Lee MY, Kim DD, Kim MG, Lee JY. Arch Pharm Res 43 1-21 (2020)

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  1. Molecular Characterizations of Surface Proteins Hemagglutinin and Neuraminidase from Recent H5Nx Avian Influenza Viruses. Yang H, Carney PJ, Mishin VP, Guo Z, Chang JC, Wentworth DE, Gubareva LV, Stevens J. J Virol 90 5770-5784 (2016)
  2. Structure-Based Modification of an Anti-neuraminidase Human Antibody Restores Protection Efficacy against the Drifted Influenza Virus. Jiang H, Peng W, Qi J, Chai Y, Song H, Bi Y, Rijal P, Wang H, Oladejo BO, Liu J, Shi Y, Gao GF, Townsend AR, Wu Y. mBio 11 e02315-20 (2020)
  3. Identification of Residues That Affect Oligomerization and/or Enzymatic Activity of Influenza Virus H5N1 Neuraminidase Proteins. Dai M, Guo H, Dortmans JC, Dekkers J, Nordholm J, Daniels R, van Kuppeveld FJ, de Vries E, de Haan CA. J Virol 90 9457-9470 (2016)
  4. Structure of influenza virus N7: the last piece of the neuraminidase "jigsaw" puzzle. Sun X, Li Q, Wu Y, Wang M, Liu Y, Qi J, Vavricka CJ, Gao GF. J Virol 88 9197-9207 (2014)
  5. 3D-quantitative structure-activity relationship and antiviral effects of curcumin derivatives as potent inhibitors of influenza H1N1 neuraminidase. Lai Y, Yan Y, Liao S, Li Y, Ye Y, Liu N, Zhao F, Xu P. Arch Pharm Res 43 489-502 (2020)
  6. Impact on antiviral resistance of E119V, I222L and R292K substitutions in influenza A viruses bearing a group 2 neuraminidase (N2, N3, N6, N7 and N9). Gaymard A, Charles-Dufant A, Sabatier M, Cortay JC, Frobert E, Picard C, Casalegno JS, Rosa-Calatrava M, Ferraris O, Valette M, Ottmann M, Lina B, Escuret V. J Antimicrob Chemother 71 3036-3045 (2016)
  7. Antiviral Activity of Isoimperatorin Against Influenza A Virus in vitro and its Inhibition of Neuraminidase. Lai Y, Han T, Zhan S, Jiang Y, Liu X, Li G. Front Pharmacol 12 657826 (2021)
  8. Predicting Displaceable Water Sites Using Mixed-Solvent Molecular Dynamics. Graham SE, Smith RD, Carlson HA. J Chem Inf Model 58 305-314 (2018)
  9. The significance of naturally occurring neuraminidase quasispecies of H5N1 avian influenza virus on resistance to oseltamivir: a point of concern. Schaduangrat N, Phanich J, Rungrotmongkol T, Lerdsamran H, Puthavathana P, Ubol S. J Gen Virol 97 1311-1323 (2016)
  10. Variability of tropism and replicative capacity of two naturally occurring influenza A H9N2 viruses in cell cultures from different tissues. Tombari W, ElBehi I, Amouna F, Ghram A. Avian Pathol 45 212-220 (2016)
  11. Accelerating reliable multiscale quantum refinement of protein-drug systems enabled by machine learning. Yan Z, Wei D, Li X, Chung LW. Nat Commun 15 4181 (2024)
  12. Emergence of a young case infected with avian influenza A (H5N6) in Anhui Province, East China during the COVID-19 pandemic. Yu JL, Hou S, Feng YT, Bu G, Chen QQ, Meng ZQ, Ding ZT, Guo LZ, Zhou X, Wang M, Huang XE, Li WW, He L, Gong L, Sun Y, Xu Z, Pan HF, He J, Wu JB. J Med Virol 93 5998-6007 (2021)
  13. Plasticity of the 340-Loop in Influenza Neuraminidase Offers New Insight for Antiviral Drug Development. Han N, Ng JTY, Li Y, Mu Y, Huang Z. Int J Mol Sci 21 E5655 (2020)
  14. Impact of the H274Y Substitution on N1, N4, N5, and N8 Neuraminidase Enzymatic Properties and Expression in Reverse Genetic Influenza A Viruses. Gaymard A, Picard C, Vazzoler G, Massin P, Frobert E, Sabatier M, Barthelemy M, Valette M, Ottmann M, Casalegno JS, Lina B, Escuret V. Viruses 16 388 (2024)
  15. Structural and inhibitor sensitivity analysis of influenza B-like viral neuraminidases derived from Asiatic toad and spiny eel. Li L, Chai Y, Peng W, Li D, Sun L, Gao GF, Qi J, Xiao H, Liu WJ, von Itzstein M, Gao F. Proc Natl Acad Sci U S A 119 e2210724119 (2022)
  16. Synthesis and Neuraminidase Inhibitory Activity of Sialic Acid Analogues with Fluoro, Phosphono, and Sulfo Functionalities. Vavricka CJ, Sriwilaijaroen N, Suzuki Y, Kiyota H. Methods Mol Biol 2556 303-320 (2022)


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