Heat shock protein 90 inhibitors as broad spectrum anti-infectives

Current Pharmaceutical Design

Volumn 19, Issue 3, 2013, Pages 377-386

  Rochani, Ankit K ^a   Singh, Meetali ^a   Tatu, Utpal ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

17 AAG; Anti infective; Hsp90 inhibitors; Malaria; Plasmodium falciparum Hsp90; Surra

Indexed keywords

3 (5 CHLORO 2,4 DIHYDROXYPHENYL) N ETHYL 4 (4 METHOXYPHENYL) 5 PYRAZOLECARBOXAMIDE; 4 [4 (1,4 BENZODIOXAN 6 YL) 5 METHYL 1H PYRAZOL 3 YL] 6 ETHYLRESORCINOL; 5 (2,4 DIHYDROXY 5 ISOPROPYLPHENYL) 4 (4 MORPHOLINOMETHYLPHENYL) 3 ISOXAZOLECARBOXYLIC ACID ETHYLAMIDE; ADENOSINE TRIPHOSPHATASE; ALVESPIMYCIN; ANSAMYCIN DERIVATIVE; ANTIINFECTIVE AGENT; AT 13387; CASPOFUNGIN; CELASTROL; CNF 2024; FLUCONAZOLE; GANETESPIB; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; HSP 990; KW 2478; MEPACRINE; NOVOBIOCIN; RADICICOL; RETASPIMYCIN; SNX 5422; TANESPIMYCIN; TRICHOSTATIN A; UNCLASSIFIED DRUG;

AFRICAN TRYPANOSOMIASIS; ANTIFUNGAL RESISTANCE; ANTIMALARIAL DRUG SUSCEPTIBILITY; ANTINEOPLASTIC ACTIVITY; ANTIPROTOZOAL ACTIVITY; ANTIVIRAL ACTIVITY; ANTIVIRAL SUSCEPTIBILITY; ASPERGILLOSIS; ASPERGILLUS FUMIGATUS; BINDING AFFINITY; CANDIDA; CANDIDA ALBICANS; CANDIDA KRUSEI; CANDIDA PARAPSILOSIS; CANDIDIASIS; CARBOXY TERMINAL SEQUENCE; CELL CYCLE ARREST; CELL CYCLE G1 PHASE; CONCENTRATION RESPONSE; DRUG ABSORPTION; DRUG DISTRIBUTION; DRUG EFFICACY; DRUG EXCRETION; DRUG FORMULATION; DRUG METABOLISM; DRUG POTENTIATION; DRUG SAFETY; DRUG STRUCTURE; DRUG TARGETING; ENZYME ACTIVITY; EPSTEIN BARR VIRUS; FATIGUE; FUNGICIDAL ACTIVITY; GENOTOXICITY; GROWTH INHIBITION; HEPATITIS B VIRUS; HERPES SIMPLEX VIRUS 1; HERPES SIMPLEX VIRUS 2; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS 1; IC 50; INFLUENZA VIRUS; LEISHMANIA DONOVANI; LIFE CYCLE; MALARIA FALCIPARUM; NAUSEA; NONHUMAN; PAIN; PLASMODIUM BERGHEI INFECTION; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; PROTEIN FUNCTION; REVIEW; SIDE EFFECT; SURVIVAL RATE; TOXOPLASMA GONDII; TOXOPLASMOSIS; TROPHOZOITE; TRYPANOSOMA EVANSI; UNSPECIFIED SIDE EFFECT; VIRUS INHIBITION; VOMITING;

EID: 84876725385     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/138161213804143608     Document Type: Review

References (88)

1. Johnson JL, Brown C. Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms. Cell Stress Chaperones 2009; 14[1]: 83-94.
2. Taipale M, Jarosz DF, Lindquist S. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat Rev Mol Cell Biol 2010; 11[7]: 515-28.
3. Wiesgigl M, Clos J. Heat shock protein 90 homeostasis controls stage differentiation in Leishmania donovani. Mol Biol Cell 2001; 12[11]: 3307-16.
4. Graefe SE, Wiesgigl M, Gaworski I, Macdonald A, Clos J. Inhibition of HSP90 in Trypanosoma cruzi induces a stress response but no stage differentiation. Eukaryot Cell 2002; 1[6]: 936-43.
5. Banumathy G, Singh V, Pavithra SR, Tatu U. Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes. J Biol Chem 2003; 278[20]: 18336-45.
6. Nageshan RK, Roy N, Hehl AB, Tatu U. Post-transcriptional repair of a split heat shock protein 90 gene by mRNA trans-splicing. J Biol Chem.; 286[9]: 7116-22.
7. Wider D, Peli-Gulli MP, Briand PA, Tatu U, Picard D. The complementation of yeast with human or Plasmodium falciparum Hsp90 confers differential inhibitor sensitivities. Mol Biochem Parasitol 2009; 164[2]: 147-52.
8. Finkelstein DB, Strausberg S. Identification and expression of a cloned yeast heat shock gene. J Biol Chem 1983; 258[3]: 1908-13.
9. Ritossa. A new puffing pattern induced by temperature shock and DNP in Drosophila. Experientia 1962; 18: 571-3.
10. DeBoer C, Meulman PA, Wnuk RJ, Peterson DH. Geldanamycin, a new antibiotic. J Antibiot [Tokyo] 1970; 23[9]: 442-7.
11. Lakomek HJ, Will H, Zech M, Kruskemper HL. A new serologic marker in ankylosing spondylitis. Arthritis Rheum 1984; 27[9]: 961-7.
12. Kubo T, Towle CA, Mankin HJ, Treadwell BV. Stress-induced proteins in chondrocytes from patients with osteoarthritis. Arthritis Rheum 1985; 28[10]: 1140-5.
13. Schuh S, Yonemoto W, Brugge J et al. A 90,000-dalton binding protein common to both steroid receptors and the Rous sarcoma virus transforming protein, pp60v-src. J Biol Chem 1985; 260[26]: 14292-6.
14. Whitesell L, Mimnaugh EG, De Costa B, Myers CE, Neckers LM. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA 1994; 91[18]: 8324-8.
15. Cowen LE, Singh SD, Kohler JR, et al. Harnessing Hsp90 function as a powerful, broadly effective therapeutic strategy for fungal infectious disease. Proc Natl Acad Sci USA 2009; 106[8]: 2818-23.
16. Pallavi R, Roy N, Nageshan RK, et al. Heat shock protein 90 as a drug target against protozoan infections: biochemical characterization of HSP90 from Plasmodium falciparum and Trypanosoma evansi and evaluation of its inhibitor as a candidate drug. J Biol Chem 2010; 285[49]: 37964-75.
17. Mollapour M, Neckers L. Quinacrine: New anti-tumor application for an old anti-malaria drug. Cell Cycle 2010; 9[2]: 228.
18. Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 1997; 89[2]: 239-50.
19. Dolgin E, Motluk A. Heat shock and awe. Nat Med 2011; 17[6]: 646-9.
20. Dutta R, Inouye M. GHKL, an emergent ATPase/kinase superfamily. Trends Biochem Sci 2000; 25[1]: 24-8.
21. Stetler RA, Gan Y, Zhang W, et al. Heat shock proteins: cellular and molecular mechanisms in the central nervous system. Prog Neurobiol 2010; 92[2]: 184-211.
22. Pearl LH, Prodromou C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem 2006; 75: 271-94.
23. McClellan AJ. et al. Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches, 131. [2007].
24. Solit DB, Chiosis G. Development and application of Hsp90 inhibitors. Drug Discov Today 2008; 13 [1-2]: 38-43.
25. Acharya P, Kumar R, Tatu U. Chaperoning a cellular upheaval in malaria: heat shock proteins in Plasmodium falciparum. Mol Biochem Parasitol 2007; 153[2]: 85-94.
26. World Health Organization [home page on internet]. Avenue Appia 20, 1211 Geneva 27, Switzerland: World Health Organization; c 2011 [updated 2011]. Available from; http: //www.who.int/mediacentre/factsheets/fs094/en/. [cited]; Available from.
27. http: //www.cdc.gov [home page internet]. Centers for Disease Control and Prevention 1600 Clifton Rd. Atlanta, GA 30333, USA; Updated 2012 March 27. Available http: //www.cdc.gov/malaria/about/disease.html.
28. Pavithra SR, Banumathy G, Joy O, Singh V, Tatu U. Recurrent fever promotes Plasmodium falciparum development in human erythrocytes. J Biol Chem 2004; 279[45]: 46692-9.
29. Rubul Mout Z-dX, Angela KH Wolf, Vincent JO Davisson, Gautam K Jarori. Antimalarial activity of geldanamycin derivatives in mice infected with Plasmodium yoelii. Malaria J 2012; 11[54].
30. Kumar R, Pavithra SR, Tatu U. Three-dimensional structure of heat shock protein 90 from Plasmodium falciparum: molecular modelling approach to rational drug design against malaria. J Biosci 2007; 32[3]: 531-6.
31. Corbett KD, Berger JM. Structure of the ATP-binding domain of Plasmodium falciparum Hsp90. Proteins 2010; 78[13]: 2738-44.
32. World Organisation for Animal Health [home page on internet]. 12, rue de Prony 75017 Paris, France: OIE Organisation Mondiale de la Santé Animale World Organisation for Animal Health Organization Mudial de Sanidad Animal; c 2011 [updated 2011]. Available from http: //www.oie.int/animal-heatlh-in-the-world/oie-listeddiseases-2011/.
33. Jones C, Anderson S, Singha UK, Chaudhuri M. Protein phosphatase 5 is required for Hsp90 function during proteotoxic stresses in Trypanosoma brucei. Parasitol Res 2008; 102[5]: 835-44.
34. Neckers L, Tatu U. Molecular chaperones in pathogen virulence: emerging new targets for therapy. Cell Host Microbe 2008; 4[6]: 519-27.
35. Echeverria PC, Matrajt M, Harb OS, et al. Toxoplasma gondii Hsp90 is a potential drug target whose expression and subcellular localization are developmentally regulated. J Mol Biol 2005; 350[4]: 723-34.
36. Hu J, Seeger C. Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase. Proc Natl Acad Sci USA 1996; 93[3]: 1060-4.
37. Jeon YK, Park CH, Kim KY, et al. The heat-shock protein 90 inhibitor, geldanamycin, induces apoptotic cell death in Epstein-Barr virus-positive NK/T-cell lymphoma by Akt down-regulation. J Pathol 2007; 213[2]: 170-9.
38. Li YH, Tao PZ, Liu YZ, Jiang JD. Geldanamycin, a ligand of heat shock protein 90, inhibits the replication of herpes simplex virus type 1 in vitro. Antimicrob Agents Chemother 2004; 48[3]: 867-72.
39. Chase G, Deng T, Fodor E, et al. Hsp90 inhibitors reduce influenza virus replication in cell culture. Virology 2008; 377[2]: 431-9.
40. Vozzolo L, Loh B, Gane PJ, et al. Gyrase B inhibitor impairs HIV-1 replication by targeting Hsp90 and the capsid protein. J Biol Chem 2010; 285[50]: 39314-28.
41. Ju HQ, Xiang YF, Xin BJ, et al. Synthesis and in vitro anti-HSV-1 activity of a novel Hsp90 inhibitor BJ-B11. Bioorg Med Chem Lett 2011; 21[6]: 1675-7.
42. Klepser ME. Antifungal resistance among Candida species. Pharmacotherapy 2001; 21[8 Pt 2]: 124S-32S.
43. Rutherford SL, Lindquist S. Hsp90 as a capacitor for morphological evolution. Nature 1998; 396[6709]: 336-42.
44. Jarosz DF, Lindquist S. Hsp90 and environmental stress transform the adaptive value of natural genetic variation. Science.; 330[6012]: 1820-4.
45. Queitsch C, Sangster TA, Lindquist S. Hsp90 as a capacitor of phenotypic variation. Nature 2002; 417[6889]: 618-24.
46. Casey JT WP, Shea DGO. Characterization of adsorbent resins for the recovery of geldanamycin from fermentation broth. Separation purification technology 2007; 53: 281-8.
47. TOXNET Toxicology Data Network [home page on internet]. Two Democracy Plaza, Suite 510 6707 Democracy Blvd, MSC 5467 Bethesda, MD 20892-5467: National Library of Medicine National Institutes of Health; c 2005-2010 [updated 2010 June 17]. Available from http: //toxnet.nim.nih.gov/cgibin/ sis/search/r?dbs+genetox: @term+@rn+@rel+%2230562-34-6%22.
48. Lin Zhang iCTC, assignee. Process for preparing 17-allyl amino geldanamycin [17-AAG] and other ansamycins. United States patent US 20050176695A1 2005
49. Schulte TW, Neckers LM. The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother Pharmacol 1998; 42[4]: 273-9.
50. Hosokawa N, Hirayoshi K, Nakai A, et al. Flavonoids inhibit the expression of heat shock proteins. Cell Struct Funct 1990; 15[6]: 393-401.
51. Hadden MK, Galam L, Gestwicki JE, Matts RL, Blagg BS. Derrubone, an inhibitor of the Hsp90 protein folding machinery. J Nat Prod 2007; 70[12]: 2014-8.
52. Donnelly A, Blagg BS. Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket. Curr Med Chem 2008; 15[26]: 2702-17.
53. Marcu MG, Schulte TW, Neckers L. Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins. J Natl Cancer Inst 2000; 92[3]: 242-8.
54. Marcu MG, Chadli A, Bouhouche I, Catelli M, Neckers LM. The heat shock protein 90 antagonist novobiocin interacts with a previously unrecognized ATP-binding domain in the carboxyl terminus of the chaperone. J Biol Chem 2000; 275[47]: 37181-6.
55. ClinicalTrials. gov [home page internet]. National Library of Medicine 8600 Rockville Pike Bethesda, MD 20894: NLM National Institute of Health; c 1993-2008 [updated 2010 September 15]. Available http: //clinicaltrials.gov/ct2/show/NCT00514371? term=tanespimycin&rank=2.
56. Lancet JE, Gojo I, Burton M, et al. Phase I study of the heat shock protein 90 inhibitor alvespimycin [KOS-1022, 17-DMAG] administered intravenously twice weekly to patients with acute myeloid leukemia. Leukemia 2010; 24[4]: 699-705.
57. Ramanathan RK, Egorin MJ, Erlichman C, et al. Phase I pharmacokinetic and pharmacodynamic study of 17-dimethylaminoethylamino-17-demethoxygeldanamycin, an inhibitor of heat-shock protein 90, in patients with advanced solid tumors. J Clin Oncol 2010; 28[9]: 1520-6.
58. Pacey S, Wilson RH, Walton M, et al. A phase I study of the heat shock protein 90 inhibitor alvespimycin [17-DMAG] given intravenously to patients with advanced solid tumors. Clin Cancer Res 2011; 17[6]: 1561-70.
59. Ge J, Normant E, Porter JR, et al. Design, synthesis, and biological evaluation of hydroquinone derivatives of 17-amino-17-demethoxygeldanamycin as potent, water-soluble inhibitors of Hsp90. J Med Chem 2006; 49[15]: 4606-15.
60. ClinicalTrials. gov [home page internet]. National Library of Medicine 8600 Rockville Pike Bethesda, MD 20894: NLM National Institute of Health; c 1993-2008 [updated 2011 June 6]. Available http: //www.clinicaltrials.gov/ct2/show/ct2/results?term=STA-9090.
61. Modi S, Stopeck AT, Gordon MS, et al. Combination of trastuzumab and tanespimycin [17-AAG, KOS-953] is safe and active in trastuzumab-refractory HER-2 overexpressing breast cancer: a phase I dose-escalation study. J Clin Oncol 2007; 25[34]: 5410-7.
62. Bagatell R, Gore L, Egorin MJ, et al. Phase I pharmacokinetic and pharmacodynamic study of 17-N-allylamino-17-demethoxygeldanamycin in pediatric patients with recurrent or refractory solid tumors: a pediatric oncology experimental therapeutics investigators consortium study. Clin Cancer Res 2007; 13[6]: 1783-8.
63. Modi S, Stopeck A, Linden H, et al. HSP90 inhibition is effective in breast cancer: a phase II trial of tanespimycin [17-AAG] plus trastuzumab in patients with HER2-positive metastatic breast cancer progressing on trastuzumab. Clin Cancer Res 2011; 17[15]: 5132-9.
64. Shin HC, Alani AW, Cho H, Bae Y, Kolesar JM, Kwon GS. A 3-in-1 polymeric micelle nanocontainer for poorly water-soluble drugs. Mol Pharm 2011; 8[4]: 1257-65.
65. Solit DB, Ivy SP, Kopil C, et al. Phase I trial of 17-allylamino-17-demethoxygeldanamycin in patients with advanced cancer. Clin Cancer Res 2007; 13[6]: 1775-82.
66. Ramanathan RK, Trump DL, Eiseman JL, et al. Phase I pharmacokinetic-pharmacodynamic study of 17-[allylamino]-17-demethoxygeldanamycin [17AAG, NSC 330507], a novel inhibitor of heat shock protein 90, in patients with refractory advanced cancers. Clin Cancer Res 2005; 11[9]: 3385-91.
67. Weigel BJ, Blaney SM, Reid JM, et al. A phase I study of 17-allylaminogeldanamycin in relapsed/refractory pediatric patients with solid tumors: a Children's Oncology Group study. Clin Cancer Res 2007; 13[6]: 1789-93.
68. Banerji U, O'Donnell A, Scurr M, et al. Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies. J Clin Oncol 2005; 23[18]: 4152-61.
69. Grem JL, Morrison G, Guo XD, et al. Phase I and pharmacologic study of 17-[allylamino]-17-demethoxygeldanamycin in adult patients with solid tumors. J Clin Oncol 2005; 23[9]: 1885-93.
70. Ramanathan RK, Egorin MJ, Eiseman JL, et al. Phase I and pharmacodynamic study of 17-[allylamino]-17-demethoxygeldanamycin in adult patients with refractory advanced cancers. Clin Cancer Res 2007; 13[6]: 1769-74.
71. Solit DB, Osman I, Polsky D, et al. Phase II trial of 17-allylamino-17-demethoxygeldanamycin in patients with metastatic melanoma. Clin Cancer Res 2008; 14[24]: 8302-7.
72. Heath EI, Gaskins M, Pitot HC, et al. A phase II trial of 17-allylamino-17-demethoxygeldanamycin in patients with hormonerefractory metastatic prostate cancer. Clin Prostate Cancer 2005; 4[2]: 138-41.
73. Pacey S, Gore M, Chao D, et al. A Phase II trial of 17-allylamino, 17-demethoxygeldanamycin [17-AAG, tanespimycin] in patients with metastatic melanoma. Invest New Drugs 2010; 30[1]: 341-9.
74. Ronnen EA, Kondagunta GV, Ishill N, et al. A phase II trial of 17-[Allylamino]-17-demethoxygeldanamycin in patients with papillary and clear cell renal cell carcinoma. Invest New Drugs 2006; 24[6]: 543-6.
75. Franco CMM RG, Mukhopadhyay T, Ganguli N, Fehlhaber HW, inventor; Hoechst Aktiengesellschaft, assignee. Ansamycin antibiotics and its use as a medicament. United States patent US 4738958 1988 Apr.
76. Wrona AV, Panek JS. Design and synthesis of ansamycin antibiotics. C R Chimie 2008; 11: 1483-522.
77. Lee K, Ryu JS, Jin Y, et al. Synthesis and anticancer activity of geldanamycin derivatives derived from biosynthetically generated metabolites. Org Biomol Chem 2008; 6[2]: 340-8.
78. Eichner S, Floss HG, Sasse F, Kirschning A. New, highly active nonbenzoquinone geldanamycin derivatives by using mutasynthesis. Chembiochem 2009; 10[11]: 1801-5.
79. Zapf CW, Bloom JD, McBean JL, et al. Design and SAR of macrocyclic Hsp90 inhibitors with increased metabolic stability and potent cell-proliferation activity. Bioorg Med Chem Lett 2011; 21[8]: 2278-82.
80. Day JE, Sharp SY, Rowlands MG, et al. Inhibition of Hsp90 with resorcylic acid macrolactones: synthesis and binding studies. Chemistry 2010; 16[34]: 10366-72.
81. Brandt GE, Schmidt MD, Prisinzano TE, Blagg BS. Gedunin, a novel hsp90 inhibitor: semisynthesis of derivatives and preliminary structure-activity relationships. J Med Chem 2008; 51[20]: 6495-502.
82. Zhang T, Hamza A, Cao X, et al. A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells. Mol Cancer Ther 2008; 7[1]: 162-70.
83. Wang Y, Xiao J, Suzek TO, et al. PubChem's BioAssay Database. Nucleic Acids Res. Jan; 40[Database issue]: D400-12.
84. Adayev T, Wegiel J, Hwang YW. Harmine is an ATP-competitive inhibitor for dual-specificity tyrosine phosphorylation-regulated kinase 1A [Dyrk1A]. Arch Biochem Biophys 2010; 507[2]: 212-8.
85. Maggon K. Global pharmaceutical market intelligence monograph: Global pharma markets, cancer, diabetes, infections, cardiac, CNS, hypertension, respiratory [book on internet]. Knol Publishing [cited 2011 Apr 25]. Available from http: //knol.google.com/k/globalpharmaceutical-market-intellegence-monograph#.
86. http: //www.biomedtrends.com/GetDetails.asp?CatName= Pharmaceuticals.
87. Anti-infective and anti-microbial review and outlook 2011: http: //www.pharmalive.com/special_reports/sample.cfm?reportID=354.
88. Spiderbiotech bite a better health[home page internet]. Ribes 5-10010 Colleretto Giacosa [TO] c/o Bioindustry Park Canavese, Italy: Spider Biotech S.r. l; c 2005-2009 [updated 2009]. Available http: //www.spiderbiotech.com/SpiderBiotech_Science.htm.