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Structural basis for a class of nanomolar influenza A neuraminidase inhibitors.

Kerry PS, Mohan S, Russell RJ, Bance N, Niikura M, Pinto BM
Sci Rep 3 2871 (2013)
Related entries: 4ks2, 4ks3, 4ks4, 4ks5

Cited: 21 times
EuropePMC logo PMID: 24129600

Abstract

The influenza virus neuraminidase (NA) is essential for the virus life cycle. The rise of resistance mutations against current antiviral therapies has increased the need for the development of novel inhibitors. Recent efforts have targeted a cavity adjacent to the catalytic site (the 150-cavity) in addition to the primary catalytic subsite in order to increase specificity and reduce the likelihood of resistance. This study details structural and in vitro analyses of a class of inhibitors that bind uniquely in both subsites. Crystal structures of three inhibitors show occupation of the 150-cavity in two distinct and novel binding modes. We believe these are the first nanomolar inhibitors of NA to be characterized in this way. Furthermore, we show that one inhibitor, binding within the catalytic site, offers reduced susceptibility to known resistance mutations via increased flexibility of a pendant pentyloxy group and the ability to pivot about a strong hydrogen-bonding network.

Articles - 4ks1 mentioned but not cited (4)

  1. Structural basis for a class of nanomolar influenza A neuraminidase inhibitors. Kerry PS, Mohan S, Russell RJ, Bance N, Niikura M, Pinto BM. Sci Rep 3 2871 (2013)
  2. The Mechanism by which 146-N-Glycan Affects the Active Site of Neuraminidase. Liu P, Wang Z, Zhang L, Li D, Lin J. PLoS One 10 e0135487 (2015)
  3. Optimisation of Neuraminidase Expression for Use in Drug Discovery by Using HEK293-6E Cells. Campbell AC, Tanner JJ, Krause KL. Viruses 13 1893 (2021)
  4. Prediction of the Inhibition of Influenza Virus Neuraminidase Various Strains by Means of a Generalized Model Constructed Using the Data on the Position of Known Ligands. Mikurova AV, Rybina AV, Skvortsov VS. Biochem Mosc Suppl B Biomed Chem 15 166-170 (2021)


Reviews citing this publication (6)

  1. WD40 repeat domain proteins: a novel target class? Schapira M, Tyers M, Torrent M, Arrowsmith CH. Nat Rev Drug Discov 16 773-786 (2017)
  2. Progress of small molecular inhibitors in the development of anti-influenza virus agents. Wu X, Wu X, Sun Q, Zhang C, Yang S, Li L, Jia Z. Theranostics 7 826-845 (2017)
  3. Learning from structure-based drug design and new antivirals targeting the ribonucleoprotein complex for the treatment of influenza. Monod A, Swale C, Tarus B, Tissot A, Delmas B, Ruigrok RW, Crépin T, Slama-Schwok A. Expert Opin Drug Discov 10 345-371 (2015)
  4. Inhibition of sialidase activity as a therapeutic approach. Glanz VY, Myasoedova VA, Grechko AV, Orekhov AN. Drug Des Devel Ther 12 3431-3437 (2018)
  5. Combating mutations in genetic disease and drug resistance: understanding molecular mechanisms to guide drug design. Albanaz ATS, Rodrigues CHM, Pires DEV, Ascher DB. Expert Opin Drug Discov 12 553-563 (2017)
  6. Thirty-Five-Year History of Desialylated Lipoproteins Discovered by Vladimir Tertov. Glanz V, Bezsonov EE, Soldatov V, Orekhov AN. Biomedicines 10 1174 (2022)

Articles citing this publication (11)

  1. Congress Meeting report: 4th ISIRV antiviral group conference: Novel antiviral therapies for influenza and other respiratory viruses. McKimm-Breschkin JL, Fry AM. Antiviral Res 129 21-38 (2016)
  2. Structure-Based Design of Human TLR8-Specific Agonists with Augmented Potency and Adjuvanticity. Beesu M, Caruso G, Salyer AC, Khetani KK, Sil D, Weerasinghe M, Tanji H, Ohto U, Shimizu T, David SA. J Med Chem 58 7833-7849 (2015)
  3. Inhibition of neuraminidase by Ganoderma triterpenoids and implications for neuraminidase inhibitor design. Zhu Q, Bang TH, Ohnuki K, Sawai T, Sawai K, Shimizu K. Sci Rep 5 13194 (2015)
  4. Modulating carnitine levels by targeting its biosynthesis pathway - selective inhibition of γ-butyrobetaine hydroxylase. Rydzik AM, Chowdhury R, Kochan GT, Williams ST, McDonough MA, Kawamura A, Schofield CJ. Chem Sci 5 1765-1771 (2014)
  5. Resistance to Mutant Group 2 Influenza Virus Neuraminidases of an Oseltamivir-Zanamivir Hybrid Inhibitor. Wu Y, Gao F, Qi J, Bi Y, Fu L, Mohan S, Chen Y, Li X, Pinto BM, Vavricka CJ, Tien P, Gao GF. J Virol 90 10693-10700 (2016)
  6. Serendipitous discovery of a potent influenza virus a neuraminidase inhibitor. Mohan S, Kerry PS, Bance N, Niikura M, Pinto BM. Angew Chem Int Ed Engl 53 1076-1080 (2014)
  7. Design and synthesis of 1,2,3-triazole-containing N-acyl zanamivir analogs as potent neuraminidase inhibitors. Das A, Adak AK, Ponnapalli K, Lin CH, Hsu KC, Yang JM, Hsu TA, Lin CC. Eur J Med Chem 123 397-406 (2016)
  8. Letter Atypical group 1 neuraminidase pH1N1-N1 bound to a group 1 inhibitor. Wu Y, Vavricka CJ, Wu Y, Li Q, Rudrawar S, Thomson RJ, von Itzstein M, Gao GF, Qi J. Protein Cell 6 771-773 (2015)
  9. Synthesis and evaluation of influenza A viral neuraminidase candidate inhibitors based on a bicyclo[3.1.0]hexane scaffold. Colombo C, Pinto BM, Bernardi A, Bennet AJ. Org Biomol Chem 14 6539-6553 (2016)
  10. Structure-based design of 5'-substituted 1,2,3-triazolylated oseltamivir derivatives as potent influenza neuraminidase inhibitors. Wang P, Oladejo BO, Li C, Fu L, Zhang S, Qi J, Lv X, Li X. RSC Adv 11 9528-9541 (2021)
  11. Influenza A Virus Neuraminidase Inhibitors. Sriwilaijaroen N, Vavricka CJ, Kiyota H, Suzuki Y. Methods Mol Biol 2556 321-353 (2022)


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