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Structure-based inhibitors of influenza virus sialidase. A benzoic acid lead with novel interaction.

Singh S, Jedrzejas MJ, Air GM, Luo M, Laver WG, Brouillette WJ
J Med Chem 38 3217-25 (1995)
Related entries: 1ing, 1inh, 1ivb, 1ivc, 1ivd, 1ive, 1ivf, 1ivg, 1nn2, 3nn9, 4nn9, 5nn9, 6nn9

Cited: 32 times
EuropePMC logo PMID: 7650674

Abstract

Influenza virus sialidase is a surface enzyme that is essential for infection of the virus. The catalytic site is highly conserved among all known influenza variants, suggesting that this protein is a suitable target for drug intervention. The most potent known inhibitors are analogs of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en), particularly the 4-guanidino derivative (4-guanidino-Neu5Ac2en). We utilized the benzene ring of 4-(N-acetylamino)benzoic acids as a cyclic template to substitute for the dihydropyran ring of Neu5Ac2en. In this study several 3-(N-acylamino) derivatives were prepared as potential replacements for the glycerol side chain of Neu5Ac2en, and some were found to interact with the same binding subsite of sialidase. Of greater significance was the observation that the 3-guanidinobenzoic acid derivative (equivalent to the 4-guanidino grouping of 4-guanidino-Neu5Ac2en), the most potent benzoic acid inhibitor of influenza sialidase thus far identified (IC50 = 10 microM), occupied the glycerol-binding subsite on sialidase as opposed to the guanidino-binding subsite. This benzoic acid derivative thus provides a new compound that interacts in a novel manner with the catalytic site of influenza sialidase.

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  2. AMMOS: Automated Molecular Mechanics Optimization tool for in silico Screening. Pencheva T, Lagorce D, Pajeva I, Villoutreix BO, Miteva MA. BMC Bioinformatics 9 438 (2008)
  3. 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)
  4. Ligand scaffold hopping combining 3D maximal substructure search and molecular similarity. Quintus F, Sperandio O, Grynberg J, Petitjean M, Tuffery P. BMC Bioinformatics 10 245 (2009)
  5. Development and validation of an improved algorithm for overlaying flexible molecules. Taylor R, Cole JC, Cosgrove DA, Gardiner EJ, Gillet VJ, Korb O. J. Comput. Aided Mol. Des. 26 451-472 (2012)
  6. A single N342D substitution in Influenza B Virus NA protein determines viral pathogenicity in mice. Zhou L, Feng Z, Liu J, Chen Y, Yang L, Liu S, Li X, Gao R, Zhu W, Wang D, Shu Y. Emerg Microbes Infect 9 1853-1863 (2020)
  7. 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)


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  2. New approaches to influenza chemotherapy. Neuraminidase inhibitors. Calfee DP, Hayden FG. Drugs 56 537-553 (1998)
  3. 'Flu' and structure-based drug design. Wade RC. Structure 5 1139-1145 (1997)
  4. Design and synthesis of carbohydrate-based inhibitors of protein-carbohydrate interactions. von Itzstein M, Colman P. Curr. Opin. Struct. Biol. 6 703-709 (1996)
  5. Recent progress and challenges in the discovery of new neuraminidase inhibitors. Chamni S, De-Eknamkul W. Expert Opin Ther Pat 23 409-423 (2013)
  6. Approaches and strategies for the treatment of influenza virus infections. Colacino JM, Staschke KA, Laver WG. Antivir. Chem. Chemother. 10 155-185 (1999)
  7. The Symmetry of Viral Sialic Acid Binding Sites-Implications for Antiviral Strategies. Rustmeier NH, Strebl M, Stehle T. Viruses 11 (2019)

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  1. Analysis of inhibitor binding in influenza virus neuraminidase. Smith BJ, Colman PM, Von Itzstein M, Danylec B, Varghese JN. Protein Sci. 10 689-696 (2001)
  2. Generation and characterization of a mutant of influenza A virus selected with the neuraminidase inhibitor BCX-140. Bantia S, Ghate AA, Ananth SL, Babu YS, Air GM, Walsh GM. Antimicrob. Agents Chemother. 42 801-807 (1998)
  3. Docking and 3D-QSAR studies of influenza neuraminidase inhibitors using three-dimensional holographic vector of atomic interaction field analysis. Sun J, Cai S, Yan N, Mei H. Eur J Med Chem 45 1008-1014 (2010)
  4. Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site. Finley JB, Atigadda VR, Duarte F, Zhao JJ, Brouillette WJ, Air GM, Luo M. J. Mol. Biol. 293 1107-1119 (1999)
  5. Benzoic acid and pyridine derivatives as inhibitors of Trypanosoma cruzi trans-sialidase. Neres J, Bonnet P, Edwards PN, Kotian PL, Buschiazzo A, Alzari PM, Bryce RA, Douglas KT. Bioorg. Med. Chem. 15 2106-2119 (2007)
  6. Hydrophobic benzoic acids as inhibitors of influenza neuraminidase. Atigadda VR, Brouillette WJ, Duarte F, Babu YS, Bantia S, Chand P, Chu N, Montgomery JA, Walsh DA, Sudbeck E, Finley J, Air GM, Luo M, Laver GW. Bioorg. Med. Chem. 7 2487-2497 (1999)
  7. Guanidinobenzoic acid inhibitors of influenza virus neuraminidase. Sudbeck EA, Jedrzejas MJ, Singh S, Brouillette WJ, Air GM, Laver WG, Babu YS, Bantia S, Chand P, Chu N, Montgomery JA, Walsh DA, Luo M. J. Mol. Biol. 267 584-594 (1997)
  8. Pyrrolidinobenzoic acid inhibitors of influenza virus neuraminidase: modifications of essential pyrrolidinone ring substituents. Brouillette WJ, Bajpai SN, Ali SM, Velu SE, Atigadda VR, Lommer BS, Finley JB, Luo M, Air GM. Bioorg. Med. Chem. 11 2739-2749 (2003)
  9. Design of benzoic acid inhibitors of influenza neuraminidase containing a cyclic substitution for the N-acetyl grouping. Brouillette WJ, Atigadda VR, Luo M, Air GM, Babu YS, Bantia S. Bioorg. Med. Chem. Lett. 9 1901-1906 (1999)
  10. Letter Molecular docking, 3D-QSAR studies, and in silico ADME prediction of p-aminosalicylic acid derivatives as neuraminidase inhibitors. Zhang J, Shan Y, Pan X, Wang C, Xu W, He L. Chem Biol Drug Des 78 709-717 (2011)
  11. Combining docking, scoring and molecular field analyses to probe influenza neuraminidase-ligand interactions. Abu Hammad AM, Afifi FU, Taha MO. J. Mol. Graph. Model. 26 443-456 (2007)
  12. Sialidase as a target for inhibitors of influenza virus replication. Bethell RC, Smith PW. Expert Opin Investig Drugs 6 1501-1509 (1997)
  13. Young adolescents who combine alcohol and energy drinks have a higher risk of reporting negative behavioural outcomes. Holubcikova J, Kolarcik P, Madarasova Geckova A, Joppova E, van Dijk JP, Reijneveld SA. Int J Public Health 62 379-386 (2017)
  14. Crystal structure of a new benzoic acid inhibitor of influenza neuraminidase bound with a new tilt induced by overpacking subsite C6. Venkatramani L, Johnson ES, Kolavi G, Air GM, Brouillette WJ, Mooers BH. BMC Struct. Biol. 12 7 (2012)
  15. Pyrrolidinobenzoic acid inhibitors of influenza virus neuraminidase: the hydrophobic side chain influences type A subtype selectivity. Li Y, Silamkoti A, Kolavi G, Mou L, Gulati S, Air GM, Brouillette WJ. Bioorg. Med. Chem. 20 4582-4589 (2012)
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  17. Molecular docking, synthesis, and biological evaluation of naphthoquinone as potential novel scaffold for H5N1 neuraminidase inhibition. Sharma G, Vasanth Kumar S, Wahab HA. J. Biomol. Struct. Dyn. 36 233-242 (2018)
  18. On three-dimensional holographic vector of atomic interaction field analysis for influenza neuraminidase inhibitors. Li ZS, Sun JY, Liang GZ, Lu FL, Zhu WP, Zhang MJ, Zhang Y, Yang SB, Shu M, Chen GH, Lu TT. Chem Biol Drug Des 73 236-243 (2009)


Related citations provided by authors (6)

  1. Benzoic acid inhibitors of influenza virus neuraminidase.. Luo M, Jedrzejas MJ, Singh S, White CL, Brouillette WJ, Air GM, Laver WG Acta Crystallogr D Biol Crystallogr 51 504-10 (1995)
  2. Structure-Based Inhibitors of Influenza Viral Neuraminidase. A Benzoic Acid Lead with Novel Interaction. Singh S, Jedrzejas MJ, Air GM, Luo M, Laver WG, Brouillette WJ J. Med. Chem. 38 3217- (1995)
  3. Structures of aromatic inhibitors of influenza virus neuraminidase.. Jedrzejas MJ, Singh S, Brouillette WJ, Laver WG, Air GM, Luo M Biochemistry 34 3144-51 (1995)
  4. Structure of influenza virus neuraminidase B/Lee/40 complexed with sialic acid and a dehydro analog at 1.8-A resolution: implications for the catalytic mechanism.. Janakiraman MN, White CL, Laver WG, Air GM, Luo M Biochemistry 33 8172-9 (1994)
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  6. Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants.. Tulip WR, Varghese JN, Baker AT, van Donkelaar A, Laver WG, Webster RG, Colman PM J Mol Biol 221 487-97 (1991)

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