Novel sialic acid derivatives lock open the 150-loop of an influenza A virus group-1 sialidase

Nature Communications

Volumn 1, Issue 8, 2010, Pages

  Rudrawar, Santosh ^a   Dyason, Jeffrey C ^a   Rameix Welti, Marie Anne ^b,c,d   Rose, Faith J ^a   Kerry, Philip S ^e   Russell, Rupert J M ^e   Van Der Werf, Sylvie ^b,c,d   Thomson, Robin J ^a   Naffakh, Nadia ^b,c,d   Von Itzstein, Mark ^a  

^a GRIFFITH UNIVERSITY   (Australia)

^b Sorbonne Paris Cité   (France)

^c CNRS   (France)

^d UNIVERSITÉ PARIS DESCARTES   (France)

^e UNIVERSITY OF ST ANDREWS   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

3 (P TOLYL)ALLYL NEU5AC2EN; 3 ALLYL NEU5AC2EN; 4 ACETAMIDO 5 AMINO 3 (1 ETHYLPROPOXY) 1 CYCLOHEXENE 1 CARBOXYLIC ACID; ANTIVIRUS AGENT; NEU5AC2EN; OSELTAMIVIR; SIALIC ACID DERIVATIVE; SIALIDASE; SIALIDASE INHIBITOR; UNCLASSIFIED DRUG; ZANAMIVIR;

ARTICLE; CHEMICAL STRUCTURE; DRUG RESISTANCE; ENZYME CONFORMATION; INFLUENZA VIRUS A; NONHUMAN; X RAY CRYSTALLOGRAPHY;

AVES; INFLUENZA A VIRUS; ORTHOMYXOVIRIDAE;

EID: 78650045655     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms1114     Document Type: Article

References (35)

1. Zambon, M. C. The pathogenesis of influenza in humans. Rev. Med. Virol. 11, 227-241 (2001).
2. World Health Organisation - Fact sheet No 211 (2009) Influenza. http://www.who.int/mediacentre/factsheets/fs211/en/.
3. Sullivan, S. J., Jacobson, R. M., Dowdle, W. R. & Poland, G. A. 2009 H1N1 influenza. Mayo Clin. Proc. 85, 64-76 (2010).
4. Wagner, R., Matrosovich, M. & Klenk, H.- D. Functional balance between haemagglutinin and neuraminidase in influenza virus infections. Rev. Med. Virol. 12, 159-166 (2002).
5. Russell, R. J. et al. The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design. Nature 443, 45-49 (2006).
6. von Itzstein, M. The war against influenza: Discovery and development of sialidase inhibitors. Nat. Rev. Drug Discov. 6, 967-974 (2007).
7. Li, Q. et al. The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site. Nat. Struct. Mol. Biol. 17, 1266-1268 (2010).
8. von Itzstein, M. & Thomson, R. J. Anti-influenza drugs: The development of sialidase inhibitors. Handb. Exp. Pharmacol. 189, 111-154 (2009).
9. De Clercq, E. Antiviral agents active against influenza A viruses. Nat. Rev. Drug Discov. 5, 1015-1025 (2006).
10. Wen, W. H. et al. Analogs of zanamivir with modified C4-substituents as the inhibitors against the group-1 neuraminidases of influenza viruses. Bioorg. Med. Chem. 18, 4074-4084 (2010).
11. Mohan, S., McAtamney, S., Haselhorst, T., von Itzstein, M. & Pinto, B. M. Carbocycles related to oseltamivir as influenza virus group-1-specific neuraminidase inhibitors. binding to N1 enzymes in the context of virus-like particles. J. Med. Chem. 53, 7377-7391 (2010).
12. Nolan, S. P. & Clavier, H. Chemoselective olefin metathesis transformations mediated by ruthenium complexes. Chem. Soc. Rev. 39, 3305-3316 (2010).
13. Rameix-Welti, M. A. et al. Natural variation can significantly alter the sensitivity of influenza A (H5N1) viruses to oseltamivir. Antimicrob. Agents Chemotherap. 50, 3809-3815 (2006).
14. Okamoto, K., Kondo, T. & Goto, T. Functionalization of 2-deoxy-2,3-dehydro-N-acetylneuraminic acid methyl ester. Bull. Chem. Soc. Jpn. 60, 631-636 (1987).
15. Paulsen, H. & Matschulat, P. Synthese von C-glycosiden der N-acetylneuraminsäure und weiteren derivaten. Liebigs Ann. Chem. 5, 487-495 (1991).
16. Scholl, M., Ding, S., Lee, C. W. & Grubbs, R. H. Synthesis and activity of a new generation of ruthenium-based olefin metathesis catalysts coordinated with 1,3-dimesityl-4,5-dihydroimidazol-2-ylidene ligands. Org. Lett. 1, 953-956 (1999).
17. Okomo-Adhiambo, M. et al. Host cell selection of influenza neuraminidase variants: Implications for drug resistance monitoring in A(H1N1) viruses. Antiviral Res. 85, 381-388 (2010).
18. Hurt, A. C., Holien, J. K., Parker, M., Kelso, A. & Barr, I. G. Zanamivir-resistant influenza viruses with a novel neuraminidase mutation. J. Virol. 83, 10366-10373 (2009).
19. Amaro, R. E. et al. Remarkable loop flexibility in avian influenza N1 and its implications for antiviral drug design. J. Am. Chem. Soc. 129, 7764-7765 (2007).
20. Taylor, N. R. & von Itzstein, M. Molecular modeling studies on ligand binding to sialidase from influenza virus and the mechanism of catalysis. J. Med. Chem. 37, 616-624 (1994).
21. Amaro, R. E., Cheng, X., Ivanov, I., Xu, D. & McCammon, J. A. Characterizing loop dynamics and ligand recognition in human- and avian-type influenza neuraminidases via generalized born molecular dynamics and end-point free energy calculations. J. Am. Chem. Soc. 131, 4702-4709 (2009).
22. Guex, N. & Peitsch, M. C. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 18, 2714-2723 (1997).
23. Hartshorn, M. J. AstexViewer: A visualisation aid for structure-based drug design. J. Comput. Aided Mol. Des. 16, 871-881 (2002).
24. Accelrys. InsightII (Accelrys, 2001).
25. Goodsell, D. S., Morris, G. M. & Olson, A. J. Automated docking of flexible ligands: Applications of AutoDock. J. Mol. Recognit. 9, 1-5 (1996).
26. Sanner, M. F. Python: A programming language for software integration and development. J. Mol. Graph. Model 17, 57-61 (1999).
27. Cheng, L. S. et al. Ensemble-based virtual screening reveals potential novel antiviral compounds for avian influenza neuraminidase. J. Med. Chem. 51, 3878-3894 (2008).
28. Potier, M. et al. Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-a-d-N-acetylneuraminate) substrate. Anal. Biochem. 94, 287-296 (1979).
29. Matrosovich, M. et al. Overexpression of the a-2,6-sialyltransferase in MDCK cells increases influenza virus sensitivity to neuraminidase inhibitors. J. Virol. 77, 8418-8425 (2003).
30. Matrosovich, M., Matrosovich, T., Garten, W. & Klenk, H. D. New low-viscosity overlay medium for viral plaque assays. Virol. J. 3, 63 (2006).
31. Pflugrath, J. W. The finer things in X-ray diffraction data collection. Acta Crystallogr. D Biol. Crystallogr. 55, 1718-1725 (1999).
32. Collaborative Computational Project, Number 4. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
33. Adams, P. D. et al. PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr. D Biol. Crystallogr. 58, 1948-1954 (2002).
34. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47, 110-119 (1991).
35. Emsley, P. & Cowtan, K. Coot: Model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132 (2004).