Advances in the structure-based design of the influenza a neuraminidase inhibitors

Current Drug Targets

Volumn 11, Issue 3, 2010, Pages 315-326

  Mitrasinovic, Petar M ^a  

^a Institute of Physics Belgrade   (Serbia)

Author keywords

Avian H5N1 influenza virus; Drug design; Neuraminidase; Oseltamivir; Zanamivir

Indexed keywords

AMANTADINE; ANTIVIRUS AGENT; OSELTAMIVIR; PERAMIVIR; RIMANTADINE; SIALIC ACID; SIALIDASE INHIBITOR; ZANAMIVIR;

BIOLOGY; CLINICAL TRIAL; DRUG DESIGN; DRUG STRUCTURE; HUMAN; INFLUENZA; INFLUENZA VIRUS A H5N1; NONHUMAN; POULTRY; REVIEW;

ANIMALS; ANTIVIRAL AGENTS; DRUG DELIVERY SYSTEMS; DRUG DESIGN; DRUG RESISTANCE, VIRAL; ENZYME INHIBITORS; HUMANS; INFLUENZA A VIRUS, H5N1 SUBTYPE; INFLUENZA IN BIRDS; INFLUENZA, HUMAN; NEURAMINIDASE; POULTRY;

EID: 77950832743     PISSN: 13894501     EISSN: None     Source Type: Journal    
DOI: 10.2174/138945010790711932     Document Type: Review

References (65)

1. Palese P, Shaw ML. Orthomyxoviridae: the viruses and their replication. In: Knipe DM, Howley PM Eds., Fields virology. Philadelphia, Lippincott Williams and Wilkins Publishers 2007; 47: 1647-1689
2. Claas EC, Osterhaus AD, van Beek R, et al. Human influenza A H5N1 virus related to a highly pathogenic avian influenza virus. Lancet 1998; 351: 472-477
3. Peiris M, Yuen KY, Leung CW, et al. Human infection with influenza H9N2. Lancet 1999; 354: 916-917
4. Fouchier RAM, Scneeburger PM, Rozendaal FW, et al. Avian influenza A virus (H7N7) associated with conjunctivitis and a fatal case of acute respiratory distress syndrome. Proc Natl Acad Sci USA 2004; 101: 1356-1361 (Pubitemid 38182693)
5. Roberts NA, Govorkova EA. The activity of neuraminidase inhibitor oseltamivir against all subtypes of influenza viruses. In: Mitrasinovic PM Ed, Global view of the fight against influenza. New York, Nova Science Publishers Inc 2009; 93-118.
6. Bender C, Hall H, Huang J, et al. Characterization of the surface proteins of influenza A (H5N1) viruses isolated from humans in 1997-1998. Virology 1999; 254: 115-123
7. World Health Organization. Global influenza program surveillance network.evolution of H5N1 avian influenza viruses in Asia. Emerg Infect Dis 2005; 11: 1515-1521
8. Kim C, Lew W, Williams M, et al. Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent antiinfluenza activity. J Am Chem Soc 1997; 119: 681-690 (Pubitemid 27101232)
9. von Itzstein M, Wu W, Pegg M, et al. Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature 1993; 363: 418-423 (Pubitemid 23179386)
10. von Itzstein M. The war against influenza: discovery and development of sialidase inhibitors. Nat Rev Drug Discov 2007; 6: 967-974 (Pubitemid 350201787)
11. Le QM, Kiso M, Someya K, et al. Avian flu: isolation of drug-resistant H5N1 virus. Nature 2005; 437: 1108. (Pubitemid 41509341)
12. Laver PG, Gibbs AJ. The origin and control of pandemic influenza. In: Mitrasinovic PM Ed, Global view of the fight against influenza. New York, Nova Science Publishers Inc 2009; 7-20.
13. Laver WG. Flu drugs: pathway to discovery. In: Mitrasinovic PM Ed. Global view of the fight against influenza. New York, Nova Science Publishers Inc 2009; 21-28.
14. Burmeister WP, Henrissat B, Bosso C, Cusack S, Ruigrok RW. Influenza B virus neuraminidase can synthesize its own inhibitor. Structure (Lond.) 1993; 1: 19-26.
15. Varghese JN, Laver WG, Colman PM. Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9Å resolution. Nature 1983; 303: 35-40. (Pubitemid 13125070)
16. Kerry PS, Russell RJ. The impact of structural biology on the understanding of the influenza virus and the rational design of antivirals. In: Mitrasinovic PM Ed. Global view of the fight against influenza. New York, Nova Science Publishers Inc 2009; 155-184
17. Russell R, Haire L, Stevens D, et al. The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design. Nature 2006; 443: 45-49 (Pubitemid 44344043)
18. Collins PJ, Haire LF, Lin YP, et al. Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants. Nature 2008; 453: 1258-1261
19. Brouillette WJ, Bajpai S, Ali S, et al. Pyrrolidinobenzoic acid inhibitors of influenza virus neuraminidase: modifications of essential pyrrolidinone ring substituents. Bioorg Med Chem 2003; 11: 2739-2749 (Pubitemid 36682998)
20. Berman H, Westbrook J, Feng Z, et al. The protein data bank. Nucleic Acids Res 2000; 28: 235-242
21. Liu Y, Zhang J, Xu W. Recent progress in rational drug design of neuraminidase inhibitors. Curr Med Chem 2007; 14: 2872-2891 (Pubitemid 350201654)
22. Sangma C, Hannongbua S. Computational methods used in design of neuraminidase inhibitors. Curr Computer-Aided Drug Des 2007; 3: 113-132
23. Nimmanpipug P, Jitonnom J, Ngaojampa C, Hannongbua S, Lee VS. A computational H5N1 neuraminidase model and its binding to commercial drugs. Mol Simul 2007; 33: 487-493 (Pubitemid 47301179)
24. Wei D-K, Du Q-S, Sun H, Chou K-C. Insights from modeling the 3D structure of H5N1 influenza virus neuraminidase and its binding interactions with ligands. Biochem Biophys Res Commun 2006; 344: 1048-1055
25. Mihajlovic ML, Mitrasinovic PM. Some novel insights into the binding of oseltamivir and zanamivir to H5N1 and N9 influenza virus neuraminidases: a homology modeling and flexible docking study. J Serb Chem Soc 2009; 74: 1-13.
26. Mihajlovic ML, Mitrasinovic PM. Computational investigations of the binding mechanism of current influenza virus neuraminidase inhibitors: correlation with experiment In: Mitrasinovic PM Ed. Global view of the fight against influenza. New York, Nova Science Publishers Inc 2009; 119-154
27. Meindl P, Tuppy H. 2-Deoxy-2,3-dehydrosialic acids. II. Competitive inhibition of Vibrio cholerae neuraminidase by 2-deoxy-2,3-dehydro-N- acylneuraminic acids. Hoppe Seylers Z Physiol Chem 1969; 350: 1088-1092
28. Meindl P, Bodo G, Palese P, Schulman J, Tuppy H. Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro-N-acetylneuraminic acid. Virology 1974; 58: 457-463
29. von Itzstein M, Dyason JC, Oliver SW, White HF, Wu WY, Kok GB. A study of the active site of influenza virus sialidase: an approach to the rational design of novel anti-influenza drugs. J Med Chem 1996; 39: 388-391
30. Taylor NR, Cleasby A, Singh O, Skarzynski T, Wonacott AJ, Smith PW. Dihydropyrancarboxamides related to zanamivir: a new series of inhibitors of influenza virus sialidases. 2. Crystallographic and molecular modeling study of complexes of 4-amino-4H-pyran-6-carboxamides and sialidase from influenza virus types A and B. J Med Chem 1998; 41: 798-807.
31. Varghese JN, Epa VC, Colman PM. Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase. Protein Sci 1995; 4(6): 1081-1087
32. Kim CU, Lew W, Williams MA, et al. Structure-activity relationship studies of novel carbocyclic influenza neuraminidase inhibitors. J Med Chem 1998; 41: 2451-2460 (Pubitemid 28321896)
33. Aruksakunwong O, Malaisree M, Decha P, et al. On the lower susceptibility of oseltamivir to influenza neuraminidase subtype N1 than those in N2 and N9. Biophys J 2007; 92: 798-807. (Pubitemid 46203210)
34. Wang T, Wade RC. Comparative binding energy (COMBINE) analysis of influenza neuraminidase-inhibitor complexes. J Med Chem 2001; 44: 961-971 (Pubitemid 32861621)
35. Ortiz AR, Pisabarro MT, Gago F, Wade RC. Prediction of drug binding affinities by comparative binding energy analysis. J Med Chem 1995; 38: 2681-2691
36. Laver WG. Foreword. In: Mitrasinovic PM Ed, Global view of the fight against influenza. New York, Nova Science Publishers Inc 2009; xi-xii.
37. Leach A, Shoichet B, Peishoff C. Prediction of protein-ligand interactions. Docking and scoring: successes and gaps. J Med Chem 2006; 49: 5851-5855 (Pubitemid 44484931)
38. Krovat E, Steindl T, Langer T. Recent advances in docking and scoring. Curr Computer-Aided Drug Des 2005; 1: 93-102.
39. Mohan V, Gibbs A, Cummings M, Jaeger E, DesJarlais R. Docking: successes and challenges. Curr Pharm Des 2005; 11: 323-333
40. Mihajlovic ML, Mitrasinovic PM. Applications of the ArgusLab4/ AScore protocol in the structure-based binding affinity prediction of various inhibitors of group-1 and group-2 influenza virus neuraminidases (NAs). Mol Simul 2009; 35: 311-324
41. Muegge I. The effects of small changes in protein structure on predicted binding modes of known inhibitors of influenza virus neuraminidase: PMF-scoring in DOCK4. Med Chem Res 1999; 9: 490-500. (Pubitemid 30084353)
42. Singh S, Jedrzejas M, Air G, Luo M, Laver W, Brouillette W. Structure-based inhibitors of influenza virus sialidase. A benzoic acid lead with novel interaction. J Med Chem 1995; 38: 3217-3225
43. Sudbeck E, Jedrzejas M, Singh S, et al. Guanidinobenzoic acid inhibitors of influenza virus neuraminidase. J Mol Biol 1997; 267: 584-594 (Pubitemid 27170684)
44. White C, Janakiraman M, Laver W, et al. A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies. J Mol Biol 1995; 245: 623-634
45. Thompson M. ArgusLab 4.0.1. Seattle, WA, Planaria Software LLC 2004; http://www.arguslab.com, December 10, 2009.
46. Muegge I, Martin Y. A general and fast scoring function for protein-ligand interactions: a simplified potential approach. J Med Chem 1999; 42: 791-804. (Pubitemid 29136170)
47. Muegge I, Martin Y, Hajduk P, Fesik S. Evaluation of PMF scoring in docking weak ligands to the FK506 binding protein. J Med Chem 1999; 42: 2498-2503 (Pubitemid 29344291)
48. QuantumLead 3.3.0. Moscow, Russia, Quantum Pharmaceuticals 2004; http://www.q-lead.com/, December 10, 2009.
49. Mihajlovic ML, Mitrasinovic PM. Another look at the molecular mechanism of the resistance of H5N1 influenza A virus neuraminidase (NA) to oseltamivir (OTV). Biophys Chem 2008; 136: 152-158
50. Mitrasinovic PM. On the structure-based design of novel inhibitors of H5N1 influenza A virus neuraminidase (NA). Biophys Chem 2009; 140: 35-38
51. Moscona A. Medical management of influenza infection. Annu Rev Med 2008; 59: 397-413.
52. Moscona A. Neuraminidase inhibitors for influenza. N Engl J Med 2005; 353: 1363-1373
53. Wang MZ, Tai CY, Mendel DB. Mechanism by which mutations at His274 alter sensitivity of influenza A virus N1 neuraminidase to oseltamivir carboxylate and zanamivir. Antimicrob Agents Chemother 2002; 46: 3809-3816
54. Moscona A. Global transmission of oseltamivir-resistant influenza. N Engl J Med 2009; 360: 953-956
55. Magano J. Synthetic approaches to the neuraminidase inhibitors zanamivir (Relenza) and oseltamivir phosphate (Tamiflu) for the treatment of influenza. Chem Rev 2009; 109: 4398-4438.
56. Govorkova EA, Leneva IA, Goloubeva OG, Bush K, Webster RG. Comparison of efficacies of RWJ-270201, zanamivir, and oseltamivir against H5N1, H9N2, and other avian influenza viruses. Antimicrob Agents Chemother 2001; 45: 2723-2732 (Pubitemid 32906663)
57. Rungrotmongkol T, Malaisree M, Udommaneethanakit T, Hannongbua S. Comment on "Another look at the molecular mechanism of the resistance of H5N1 influenza A virus neuraminidase (NA) to oseltamivir (OTV)". Biophys Chem 2009; 141: 131-132
58. Mitrasinovic PM. Reply to Comment on "Another look at the molecular mechanism of the resistance of H5N1 influenza A virus neuraminidase (NA) to oseltamivir (OTV)". Biophys Chem 2009; 141: 133.
59. Rameix-Welti MA, Agou F, Buchy P, et al. Natural variation can significantly alter the sensitivity of influenza A (H5N1) viruses to oseltamivir. Antimicrob Agents Chemother 2006; 50: 3809-3815 (Pubitemid 44684897)
60. Rungrotmongkol T, Udommaneethanakit T, Malaisree M, et al. How does each substituent functional group of oseltamivir lose its activity against virulent H5N1 influenza mutants? Biophys Chem 2009; 145: 29-36.
61. Gastreich M, Lilienthal M, Briem H, Claussen H. Ultrafast de novo docking combining pharmacophores and combinatorics. J Comput - Aided Mol Des 2006; 20: 717-734
62. Böhm H - J. The development of a simple empirical scoring function to estimate the binding constant for a protein-ligand complex of known three-dimensional structure. J Comput -Aided Mol Des 1994; 8: 243-256
63. Rarey M, Kramer B, Lengauer T, Klebe G. A fast flexible docking method using an incremental construction algorithm. J Mol Biol 1996; 261: 470-489 (Pubitemid 26335901)
64. Krieger E. YASARA. Graz, Austria, Biosciences 1993; http://www.yasara. org/.
65. Du Q-S, Wang S-Q, Chou K-C. Analogue inhibitors by modifying oseltamivir based on the crystal neuraminidase structure for treating drug-resistant H5N1 virus. Biochem Biophys Res Commun 2007; 362: 525-531