Skip to main content
Erschienen in: Archives of Virology 11/2017

05.08.2017 | Review

HSP90: a promising broad-spectrum antiviral drug target

verfasst von: Yiliang Wang, Fujun Jin, Rongze Wang, Feng Li, Yanting Wu, Kaio Kitazato, Yifei Wang

Erschienen in: Archives of Virology | Ausgabe 11/2017

Einloggen, um Zugang zu erhalten

Abstract

The emergence of antiviral drug-resistant mutants is the most important issue in current antiviral therapy. As obligate parasites, viruses require host factors for efficient replication. An ideal therapeutic target to prevent drug-resistance development is represented by host factors that are crucial for the viral life cycle. Recent studies have indicated that heat shock protein 90 (HSP90) is a crucial host factor that is required by many viruses for multiple phases of their life cycle including viral entry, nuclear import, transcription, and replication. In this review, we summarize the most recent advances regarding HSP90 function, mechanisms of action, and molecular pathways that are associated with viral infection, and provide a comprehensive understanding of the role of HSP90 in the immune response and exosome-mediated viral transmission. In addition, several HSP90 inhibitors have entered clinical trials for specific cancers that are associated with viral infection, which further implies a crucial role for HSP90 in the malignant transformation of virus-infected cells; as such, HSP90 inhibitors exhibit excellent therapeutic potential. Finally, we describe the challenge of developing HSP90 inhibitors as anti-viral drugs.
Literatur
1.
Zurück zum Zitat Navarromarí JM, Mayoralcortés JM, Pérezruiz M, Rodríguezbaño J, Carratalá J, Gallardogarcía V (2010) Influenza a (H1N1) virus infection in humans: review to 30th October 2009. Enfermedades Infecciosas Y Microbiología Clínica 28(7):446–452CrossRef Navarromarí JM, Mayoralcortés JM, Pérezruiz M, Rodríguezbaño J, Carratalá J, Gallardogarcía V (2010) Influenza a (H1N1) virus infection in humans: review to 30th October 2009. Enfermedades Infecciosas Y Microbiología Clínica 28(7):446–452CrossRef
2.
Zurück zum Zitat Stadler K, Masignani V, Eickmann M, Becker S, Abrignani S, Klenk HD, Rappuoli R (2003) SARS—beginning to understand a new virus. Nat Rev Microbiol 1(3):209–218PubMedCrossRef Stadler K, Masignani V, Eickmann M, Becker S, Abrignani S, Klenk HD, Rappuoli R (2003) SARS—beginning to understand a new virus. Nat Rev Microbiol 1(3):209–218PubMedCrossRef
3.
Zurück zum Zitat Chun TW, Moir S, Fauci AS (2015) HIV reservoirs as obstacles and opportunities for an HIV cure. Nat Immunol 16(6):584–589PubMedCrossRef Chun TW, Moir S, Fauci AS (2015) HIV reservoirs as obstacles and opportunities for an HIV cure. Nat Immunol 16(6):584–589PubMedCrossRef
4.
Zurück zum Zitat Krammer F, Palese P (2015) Advances in the development of influenza virus vaccines. Nat Rev Drug Discov 14(3):167–182PubMedCrossRef Krammer F, Palese P (2015) Advances in the development of influenza virus vaccines. Nat Rev Drug Discov 14(3):167–182PubMedCrossRef
5.
Zurück zum Zitat Clercq ED, Herdewijn P (2002) Strategies in the design of antiviral drugs. Nat Rev Drug Discov 1(1):13–25PubMedCrossRef Clercq ED, Herdewijn P (2002) Strategies in the design of antiviral drugs. Nat Rev Drug Discov 1(1):13–25PubMedCrossRef
6.
Zurück zum Zitat Organization WH (2016) Global report on early warning indicators of HIV drug resistance: technical report Organization WH (2016) Global report on early warning indicators of HIV drug resistance: technical report
7.
Zurück zum Zitat Piret J, Boivin G (2010) Resistance of herpes simplex viruses to nucleoside analogues: mechanisms, prevalence, and management. Antimicrob Agents Chemother 55(2):459–472PubMedPubMedCentralCrossRef Piret J, Boivin G (2010) Resistance of herpes simplex viruses to nucleoside analogues: mechanisms, prevalence, and management. Antimicrob Agents Chemother 55(2):459–472PubMedPubMedCentralCrossRef
8.
Zurück zum Zitat Richardson PG, Mitsiades CS, Laubach JP, Lonial S, Chanan-Khan AA, Anderson KC (2011) Inhibition of heat shock protein 90 (HSP90) as a therapeutic strategy for the treatment of myeloma and other cancers. Br J Haematol 152(4):367–379PubMedCrossRef Richardson PG, Mitsiades CS, Laubach JP, Lonial S, Chanan-Khan AA, Anderson KC (2011) Inhibition of heat shock protein 90 (HSP90) as a therapeutic strategy for the treatment of myeloma and other cancers. Br J Haematol 152(4):367–379PubMedCrossRef
9.
Zurück zum Zitat Fedson DS (2006) Pandemic influenza: a potential role for statins in treatment and prophylaxis. Clin Infect Dis Off Publ Infectious Dis Soc Am 43(2):199–205. doi:10.1086/505116 CrossRef Fedson DS (2006) Pandemic influenza: a potential role for statins in treatment and prophylaxis. Clin Infect Dis Off Publ Infectious Dis Soc Am 43(2):199–205. doi:10.​1086/​505116 CrossRef
10.
Zurück zum Zitat Marjuki H, Alam MI, Ehrhardt C, Wagner R, Planz O, Klenk HD, Ludwig S, Pleschka S (2006) Membrane accumulation of influenza A virus hemagglutinin triggers nuclear export of the viral genome via protein kinase Calpha-mediated activation of ERK signaling. J Biol Chem 281(24):16707–16715. doi:10.1074/jbc.M510233200 PubMedCrossRef Marjuki H, Alam MI, Ehrhardt C, Wagner R, Planz O, Klenk HD, Ludwig S, Pleschka S (2006) Membrane accumulation of influenza A virus hemagglutinin triggers nuclear export of the viral genome via protein kinase Calpha-mediated activation of ERK signaling. J Biol Chem 281(24):16707–16715. doi:10.​1074/​jbc.​M510233200 PubMedCrossRef
11.
Zurück zum Zitat Sgarbanti R, Nencioni L, Amatore D, Coluccio P, Fraternale A, Sale P, Mammola CL, Carpino G, Gaudio E, Magnani M, Ciriolo MR, Garaci E, Palamara AT (2011) Redox regulation of the influenza hemagglutinin maturation process: a new cell-mediated strategy for anti-influenza therapy. Antioxid Redox Signal 15(3):593–606. doi:10.1089/ars.2010.3512 PubMedCrossRef Sgarbanti R, Nencioni L, Amatore D, Coluccio P, Fraternale A, Sale P, Mammola CL, Carpino G, Gaudio E, Magnani M, Ciriolo MR, Garaci E, Palamara AT (2011) Redox regulation of the influenza hemagglutinin maturation process: a new cell-mediated strategy for anti-influenza therapy. Antioxid Redox Signal 15(3):593–606. doi:10.​1089/​ars.​2010.​3512 PubMedCrossRef
12.
Zurück zum Zitat Shim HY, Quan X, Yi YS, Jung G (2011) Heat shock protein 90 facilitates formation of the HBV capsid via interacting with the HBV core protein dimers. Virology 410(1):161–169PubMedCrossRef Shim HY, Quan X, Yi YS, Jung G (2011) Heat shock protein 90 facilitates formation of the HBV capsid via interacting with the HBV core protein dimers. Virology 410(1):161–169PubMedCrossRef
13.
Zurück zum Zitat Ju HQ, Xiang YF, Xin BJ, Pei Y, Lu JX, Wang QL, Xia M, Qian CW, Ren Z, Wang SY (2011) Synthesis and in vitro anti-HSV-1 activity of a novel Hsp90 inhibitor BJ-B11. Bioorg Med Chem Lett 21(6):1675–1677PubMedCrossRef Ju HQ, Xiang YF, Xin BJ, Pei Y, Lu JX, Wang QL, Xia M, Qian CW, Ren Z, Wang SY (2011) Synthesis and in vitro anti-HSV-1 activity of a novel Hsp90 inhibitor BJ-B11. Bioorg Med Chem Lett 21(6):1675–1677PubMedCrossRef
14.
15.
Zurück zum Zitat Deepti J, Munira Q, Neha G, Rajnish J, Nitin G (2009) Association of Epstein Barr virus infection (EBV) with breast cancer in rural indian women. Plos One 4(12):e8180CrossRef Deepti J, Munira Q, Neha G, Rajnish J, Nitin G (2009) Association of Epstein Barr virus infection (EBV) with breast cancer in rural indian women. Plos One 4(12):e8180CrossRef
16.
Zurück zum Zitat Mazouni C, Fina F, Romain S, Ouafik L, Bonnier P, Brandone J-M, Martin P-M (2011) Epstein-Barr virus as a marker of biological aggressiveness in breast cancer. Br J Cancer 104(2):332PubMedCrossRef Mazouni C, Fina F, Romain S, Ouafik L, Bonnier P, Brandone J-M, Martin P-M (2011) Epstein-Barr virus as a marker of biological aggressiveness in breast cancer. Br J Cancer 104(2):332PubMedCrossRef
17.
Zurück zum Zitat Zhoulei L, Nicolas G, Ken H, Alexandra J, Michaela A, Annette F, Anja B, Axel W, Christian P, Markus S, Andreas B, Ulrich K, Tobias D (2012) FLT-PET is superior to FDG-PET for very early response prediction in NPM-ALK-positive lymphoma treated with targeted therapy. Cancer Res 72(19):5014–5024 Zhoulei L, Nicolas G, Ken H, Alexandra J, Michaela A, Annette F, Anja B, Axel W, Christian P, Markus S, Andreas B, Ulrich K, Tobias D (2012) FLT-PET is superior to FDG-PET for very early response prediction in NPM-ALK-positive lymphoma treated with targeted therapy. Cancer Res 72(19):5014–5024
18.
Zurück zum Zitat Oki Y, Younes A, Knickerbocker J, Samaniego F, Nastoupil L, Hagemeister F, Romaguera J, Fowler N, Kwak L, Westin J (2015) Experience with HSP90 inhibitor AUY922 in patients with relapsed or refractory non-Hodgkin lymphoma. Haematologica 100(7):e272PubMedPubMedCentralCrossRef Oki Y, Younes A, Knickerbocker J, Samaniego F, Nastoupil L, Hagemeister F, Romaguera J, Fowler N, Kwak L, Westin J (2015) Experience with HSP90 inhibitor AUY922 in patients with relapsed or refractory non-Hodgkin lymphoma. Haematologica 100(7):e272PubMedPubMedCentralCrossRef
19.
Zurück zum Zitat Jhaveri K, Chandarlapaty S, Lake D, Gilewski T, Robson M, Goldfarb S, Drullinsky P, Sugarman S, Wasserheit-Leiblich C, Fasano J, Moynahan ME, D’Andrea G, Lim K, Reddington L, Haque S, Patil S, Bauman L, Vukovic V, El-Hariry I, Hudis C, Modi S (2014) A phase II open-label study of ganetespib, a novel heat shock protein 90 inhibitor for patients with metastatic breast cancer. Clin Breast Cancer 14(3):154–160. doi:10.1016/j.clbc.2013.12.012 PubMedCrossRef Jhaveri K, Chandarlapaty S, Lake D, Gilewski T, Robson M, Goldfarb S, Drullinsky P, Sugarman S, Wasserheit-Leiblich C, Fasano J, Moynahan ME, D’Andrea G, Lim K, Reddington L, Haque S, Patil S, Bauman L, Vukovic V, El-Hariry I, Hudis C, Modi S (2014) A phase II open-label study of ganetespib, a novel heat shock protein 90 inhibitor for patients with metastatic breast cancer. Clin Breast Cancer 14(3):154–160. doi:10.​1016/​j.​clbc.​2013.​12.​012 PubMedCrossRef
20.
Zurück zum Zitat Agyeman AS, Jun WJ, Proia DA, Kim CR, Skor MN, Kocherginsky M, Conzen SD (2016) Hsp90 inhibition results in glucocorticoid receptor degradation in association with increased sensitivity to paclitaxel in triple-negative breast cancer. Hormones Cancer 7(2):114–126. doi:10.1007/s12672-016-0251-8 PubMedPubMedCentralCrossRef Agyeman AS, Jun WJ, Proia DA, Kim CR, Skor MN, Kocherginsky M, Conzen SD (2016) Hsp90 inhibition results in glucocorticoid receptor degradation in association with increased sensitivity to paclitaxel in triple-negative breast cancer. Hormones Cancer 7(2):114–126. doi:10.​1007/​s12672-016-0251-8 PubMedPubMedCentralCrossRef
21.
Zurück zum Zitat Geller R, Taguwa S (1823) Frydman J (2011) Broad action of Hsp90 as a host chaperone required for viral replication☆. Biochimica Et Biophysica Acta 3:698–706 Geller R, Taguwa S (1823) Frydman J (2011) Broad action of Hsp90 as a host chaperone required for viral replication☆. Biochimica Et Biophysica Acta 3:698–706
22.
Zurück zum Zitat Nakagawa SI, Umehara T, Matsuda C, Kuge S, Sudoh M, Kohara M (2007) Hsp90 inhibitors suppress HCV replication in replicon cells and humanized liver mice. Biochem Biophys Res Commun 353(4):882–888PubMedCrossRef Nakagawa SI, Umehara T, Matsuda C, Kuge S, Sudoh M, Kohara M (2007) Hsp90 inhibitors suppress HCV replication in replicon cells and humanized liver mice. Biochem Biophys Res Commun 353(4):882–888PubMedCrossRef
25.
Zurück zum Zitat Taipale M, Krykbaeva I, Koeva M, Kayatekin C, Westover K, Karras G, Lindquist S (2012) quantitative analysis of Hsp90-client interactions reveals principles of substrate recognition. Cell 150(5):987–1001PubMedPubMedCentralCrossRef Taipale M, Krykbaeva I, Koeva M, Kayatekin C, Westover K, Karras G, Lindquist S (2012) quantitative analysis of Hsp90-client interactions reveals principles of substrate recognition. Cell 150(5):987–1001PubMedPubMedCentralCrossRef
26.
Zurück zum Zitat Sellers RP, Alexander LD, Johnson VA, Lin CC, Savage J, Corral R, Moss J, Slugocki TS, Singh EK, Davis MR (2010) Design and synthesis of Hsp90 inhibitors: exploring the SAR of sansalvamide A derivatives. Bioorg Med Chem 18(18):6822–6856PubMedPubMedCentralCrossRef Sellers RP, Alexander LD, Johnson VA, Lin CC, Savage J, Corral R, Moss J, Slugocki TS, Singh EK, Davis MR (2010) Design and synthesis of Hsp90 inhibitors: exploring the SAR of sansalvamide A derivatives. Bioorg Med Chem 18(18):6822–6856PubMedPubMedCentralCrossRef
27.
Zurück zum Zitat Hoyle C, Smyllie H, Leak D (2015) Measles virus infection inactivates cellular protein phosphatase 5 with consequent suppression of Sp1 and c-Myc activities. J Virol 89(19):9709–9718CrossRef Hoyle C, Smyllie H, Leak D (2015) Measles virus infection inactivates cellular protein phosphatase 5 with consequent suppression of Sp1 and c-Myc activities. J Virol 89(19):9709–9718CrossRef
28.
Zurück zum Zitat Filone CM, Caballero IS, Dower K, Mendillo ML, Cowley GS, Santagata S, Rozelle DK, Yen J, Rubins KH, Hacohen N (2014) The master regulator of the cellular stress response (HSF1) is critical for orthopoxvirus infection. PLoS Pathog 10(2):e1003904PubMedPubMedCentralCrossRef Filone CM, Caballero IS, Dower K, Mendillo ML, Cowley GS, Santagata S, Rozelle DK, Yen J, Rubins KH, Hacohen N (2014) The master regulator of the cellular stress response (HSF1) is critical for orthopoxvirus infection. PLoS Pathog 10(2):e1003904PubMedPubMedCentralCrossRef
29.
Zurück zum Zitat Anderson I, Low JS, Weston S, Weinberger M, Zhyvoloup A, Labokha AA, Corazza G, Kitson RA, Moody CJ, Marcello A (2014) Heat shock protein 90 controls HIV-1 reactivation from latency. Proc Natl Acad Sci 111(15):1528–1537CrossRef Anderson I, Low JS, Weston S, Weinberger M, Zhyvoloup A, Labokha AA, Corazza G, Kitson RA, Moody CJ, Marcello A (2014) Heat shock protein 90 controls HIV-1 reactivation from latency. Proc Natl Acad Sci 111(15):1528–1537CrossRef
30.
Zurück zum Zitat Liu D, Wu AD, Cui L, Hao R, Wang Y, He J, Guo D (2014) Hepatitis B virus polymerase suppresses NF-κB signaling by inhibiting the activity of IKKs via interaction with Hsp90β. Plos One 9(3):e91658–e91658PubMedPubMedCentralCrossRef Liu D, Wu AD, Cui L, Hao R, Wang Y, He J, Guo D (2014) Hepatitis B virus polymerase suppresses NF-κB signaling by inhibiting the activity of IKKs via interaction with Hsp90β. Plos One 9(3):e91658–e91658PubMedPubMedCentralCrossRef
31.
Zurück zum Zitat Song HL, Ran S, Mi NL, Kim CS, Lee H, Kong YY, Kim H, Jang SK (2008) A molecular chaperone glucose-regulated protein 94 blocks apoptosis induced by virus infection†. Hepatology 47(3):854–866PubMedCrossRef Song HL, Ran S, Mi NL, Kim CS, Lee H, Kong YY, Kim H, Jang SK (2008) A molecular chaperone glucose-regulated protein 94 blocks apoptosis induced by virus infection†. Hepatology 47(3):854–866PubMedCrossRef
32.
Zurück zum Zitat Rathore APS, Haystead T, Das PK, Merits A, Ng ML, Vasudevan SG (2014) Chikungunya virus nsP3 & nsP4 interacts with HSP-90 to promote virus replication: HSP-90 inhibitors reduce CHIKV infection and inflammation in vivo ☆. Antivir Res 103(1):7–16PubMedCrossRef Rathore APS, Haystead T, Das PK, Merits A, Ng ML, Vasudevan SG (2014) Chikungunya virus nsP3 & nsP4 interacts with HSP-90 to promote virus replication: HSP-90 inhibitors reduce CHIKV infection and inflammation in vivo ☆. Antivir Res 103(1):7–16PubMedCrossRef
33.
Zurück zum Zitat Jeon YK, Park CH, Kim KY, Li YC, Kim J, Kim YA, Paik JH, Park BK, Kim CW, Kim YN (2007) 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 213(2):170–179PubMedCrossRef Jeon YK, Park CH, Kim KY, Li YC, Kim J, Kim YA, Paik JH, Park BK, Kim CW, Kim YN (2007) 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 213(2):170–179PubMedCrossRef
34.
Zurück zum Zitat Kotsiopriftis M, Tanner JE, Alfieri C (2005) Heat shock protein 90 expression in Epstein-Barr virus-infected B cells promotes gammadelta T-cell proliferation in vitro. J Virol 79(11):7255–7261PubMedPubMedCentralCrossRef Kotsiopriftis M, Tanner JE, Alfieri C (2005) Heat shock protein 90 expression in Epstein-Barr virus-infected B cells promotes gammadelta T-cell proliferation in vitro. J Virol 79(11):7255–7261PubMedPubMedCentralCrossRef
36.
Zurück zum Zitat Nayar U, Lu P, Goldstein RL, Vider J, Ballon G, Rodina A, Taldone T, Erdjument-Bromage H, Chomet M, Blasberg R (2013) Targeting the Hsp90-associated viral oncoproteome in gammaherpesvirus-associated malignancies. Blood 122(16):2837–2847PubMedPubMedCentralCrossRef Nayar U, Lu P, Goldstein RL, Vider J, Ballon G, Rodina A, Taldone T, Erdjument-Bromage H, Chomet M, Blasberg R (2013) Targeting the Hsp90-associated viral oncoproteome in gammaherpesvirus-associated malignancies. Blood 122(16):2837–2847PubMedPubMedCentralCrossRef
37.
Zurück zum Zitat Field N, Low W, Daniels M, Howell S, Daviet L, Boshoff C, Collins M (2003) KSHV vFLIP binds to IKK-γ to activate IKK. J Cell Sci 116(Pt18):3721–3728PubMedCrossRef Field N, Low W, Daniels M, Howell S, Daviet L, Boshoff C, Collins M (2003) KSHV vFLIP binds to IKK-γ to activate IKK. J Cell Sci 116(Pt18):3721–3728PubMedCrossRef
38.
Zurück zum Zitat Wei B, Cui Y, Huang Y, Liu H, Li L, Li M, Ruan KC, Zhou Q, Wang C (2015) Tom70 mediates Sendai virus-induced apoptosis on mitochondria. J Virol 89(7):3804–3818PubMedPubMedCentralCrossRef Wei B, Cui Y, Huang Y, Liu H, Li L, Li M, Ruan KC, Zhou Q, Wang C (2015) Tom70 mediates Sendai virus-induced apoptosis on mitochondria. J Virol 89(7):3804–3818PubMedPubMedCentralCrossRef
39.
Zurück zum Zitat Yang K, Shi H, Qi R, Sun S, Tang Y, Zhang B, Wang C (2006) Hsp90 regulates activation of interferon regulatory factor 3 and TBK-1 stabilization in Sendai virus-infected cells. Mol Biol Cell 17(3):1461–1471PubMedPubMedCentralCrossRef Yang K, Shi H, Qi R, Sun S, Tang Y, Zhang B, Wang C (2006) Hsp90 regulates activation of interferon regulatory factor 3 and TBK-1 stabilization in Sendai virus-infected cells. Mol Biol Cell 17(3):1461–1471PubMedPubMedCentralCrossRef
40.
Zurück zum Zitat Basta S, Stoessel R, Basler M, van den Broek M, Groettrup M (2005) Cross-presentation of the long-lived lymphocytic choriomeningitis virus nucleoprotein does not require neosynthesis and is enhanced via heat shock proteins. J Immunol 175(2):796–805. doi:10.4049/jimmunol.175.2.796 PubMedCrossRef Basta S, Stoessel R, Basler M, van den Broek M, Groettrup M (2005) Cross-presentation of the long-lived lymphocytic choriomeningitis virus nucleoprotein does not require neosynthesis and is enhanced via heat shock proteins. J Immunol 175(2):796–805. doi:10.​4049/​jimmunol.​175.​2.​796 PubMedCrossRef
42.
Zurück zum Zitat Kouwaki T, Fukushima Y, Daito T, Sanada T, Yamamoto N, Mifsud EJ, Leong CR, Tsukiyama-Kohara K, Kohara M, Matsumoto M, Seya T, Oshiumi H (2016) Extracellular vesicles including exosomes regulate innate immune responses to hepatitis B virus infection. Front Immunol. doi:10.3389/fimmu.2016.00335 Kouwaki T, Fukushima Y, Daito T, Sanada T, Yamamoto N, Mifsud EJ, Leong CR, Tsukiyama-Kohara K, Kohara M, Matsumoto M, Seya T, Oshiumi H (2016) Extracellular vesicles including exosomes regulate innate immune responses to hepatitis B virus infection. Front Immunol. doi:10.​3389/​fimmu.​2016.​00335
43.
45.
Zurück zum Zitat Bukong TN, Hou W, Kodys K, Szabo G (2013) Ethanol facilitates hepatitis C virus replication via up-regulation of GW182 and heat shock protein 90 in human hepatoma cells. Hepatology 57(1):70–80PubMedPubMedCentralCrossRef Bukong TN, Hou W, Kodys K, Szabo G (2013) Ethanol facilitates hepatitis C virus replication via up-regulation of GW182 and heat shock protein 90 in human hepatoma cells. Hepatology 57(1):70–80PubMedPubMedCentralCrossRef
46.
Zurück zum Zitat Keryerbibens C, Piochedurieu C, Villemant C, Souquère S, Nishi N, Hirashima M, Middeldorp J, Busson P (2006) Exosomes released by EBV-infected nasopharyngeal carcinoma cells convey the viral latent membrane protein 1 and the immunomodulatory protein galectin 9. BMC Cancer 6(1):1–8CrossRef Keryerbibens C, Piochedurieu C, Villemant C, Souquère S, Nishi N, Hirashima M, Middeldorp J, Busson P (2006) Exosomes released by EBV-infected nasopharyngeal carcinoma cells convey the viral latent membrane protein 1 and the immunomodulatory protein galectin 9. BMC Cancer 6(1):1–8CrossRef
47.
Zurück zum Zitat Sutmuller RPM, Brok MHMGMd, Kramer M, Bennink EJ, Toonen LWJ, Kullberg BJ, Joosten LA, Akira S, Netea MG, Adema GJ, Sutmuller RP et al (2006) Toll-like receptor 2 controls expansion and function of regulatory T cells. J Clin Investig. 116(2):485–494PubMedPubMedCentralCrossRef Sutmuller RPM, Brok MHMGMd, Kramer M, Bennink EJ, Toonen LWJ, Kullberg BJ, Joosten LA, Akira S, Netea MG, Adema GJ, Sutmuller RP et al (2006) Toll-like receptor 2 controls expansion and function of regulatory T cells. J Clin Investig. 116(2):485–494PubMedPubMedCentralCrossRef
48.
Zurück zum Zitat Duerfeldt AS, Peterson LB, Maynard JC, Ng CL, Eletto D, Ostrovsky O, Shinogle HE, Moore DS, Argon Y, Nicchitta CV (2012) Development of a Grp94 inhibitor. J Am Chem Soc 134(23):9796–9804PubMedPubMedCentralCrossRef Duerfeldt AS, Peterson LB, Maynard JC, Ng CL, Eletto D, Ostrovsky O, Shinogle HE, Moore DS, Argon Y, Nicchitta CV (2012) Development of a Grp94 inhibitor. J Am Chem Soc 134(23):9796–9804PubMedPubMedCentralCrossRef
49.
Zurück zum Zitat Hiscott J (2007) Convergence of the NF-kappaB and IRF pathways in the regulation of the innate antiviral response. Cytokine Growth Factor Rev 18(5–6):483–490PubMedCrossRef Hiscott J (2007) Convergence of the NF-kappaB and IRF pathways in the regulation of the innate antiviral response. Cytokine Growth Factor Rev 18(5–6):483–490PubMedCrossRef
50.
Zurück zum Zitat Severa M, Fitzgerald KA (2007) TLR-mediated activation of type i ifn during antiviral immune responses: fighting the battle to win the war. Curr Top Microbiol Immunol 316(1):167–192PubMed Severa M, Fitzgerald KA (2007) TLR-mediated activation of type i ifn during antiviral immune responses: fighting the battle to win the war. Curr Top Microbiol Immunol 316(1):167–192PubMed
51.
52.
Zurück zum Zitat Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S (2004) A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. Nat Cell Biol 6(2):97–105PubMedCrossRef Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S (2004) A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. Nat Cell Biol 6(2):97–105PubMedCrossRef
53.
Zurück zum Zitat Field NLW, Daniels M, Howell S, Daviet L, Boshoff C, Collins M (2003) KSHV vFLIP binds to IKK-gamma to activate IKK. J Cell Sci 116(18):3721–3728PubMedCrossRef Field NLW, Daniels M, Howell S, Daviet L, Boshoff C, Collins M (2003) KSHV vFLIP binds to IKK-gamma to activate IKK. J Cell Sci 116(18):3721–3728PubMedCrossRef
54.
Zurück zum Zitat Citri A, Harari D, Shohat G, Ramakrishnan P, Gan J, Lavi S, Eisenstein M, Kimchi A, Wallach D, Pietrokovski S (2006) Hsp90 recognizes a common surface on client kinases. J Biol Chem 281(20):14361–14369PubMedCrossRef Citri A, Harari D, Shohat G, Ramakrishnan P, Gan J, Lavi S, Eisenstein M, Kimchi A, Wallach D, Pietrokovski S (2006) Hsp90 recognizes a common surface on client kinases. J Biol Chem 281(20):14361–14369PubMedCrossRef
55.
Zurück zum Zitat Lewis J, Devin A, Miller A, Lin Y, Rodriguez Y, Neckers L, Liu ZG (2000) Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation. J Biol Chem 275(14):10519–10526PubMedCrossRef Lewis J, Devin A, Miller A, Lin Y, Rodriguez Y, Neckers L, Liu ZG (2000) Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation. J Biol Chem 275(14):10519–10526PubMedCrossRef
56.
Zurück zum Zitat Lee MN, Roy M, Ong SE, Mertins P, Villani AC, Li W, Dotiwala F, Sen J, Doench JG, Orzalli MH (2013) Identification of regulators of the innate immune response to cytosolic DNA and retroviral infection by an integrative approach. Nat Immunol 14(2):179PubMedCrossRef Lee MN, Roy M, Ong SE, Mertins P, Villani AC, Li W, Dotiwala F, Sen J, Doench JG, Orzalli MH (2013) Identification of regulators of the innate immune response to cytosolic DNA and retroviral infection by an integrative approach. Nat Immunol 14(2):179PubMedCrossRef
57.
Zurück zum Zitat Chen G, Cao P, Goeddel DV (2002) TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. Mol Cell 9(2):401–410PubMedCrossRef Chen G, Cao P, Goeddel DV (2002) TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. Mol Cell 9(2):401–410PubMedCrossRef
58.
Zurück zum Zitat Eames HL, Udalova IA (2014) Interferon regulatory factors: role in transcriptional regulation of macrophage plasticity and activation. Springer, New York Eames HL, Udalova IA (2014) Interferon regulatory factors: role in transcriptional regulation of macrophage plasticity and activation. Springer, New York
59.
Zurück zum Zitat Wendel HG, De SE, Fridman JS, Malina A, Ray S, Kogan S, Cordoncardo C, Pelletier J, Lowe SW (2004) Survival signalling by Akt and eIF4E in oncogenesis and cancer therapy. Nature 428(6980):332–337PubMedCrossRef Wendel HG, De SE, Fridman JS, Malina A, Ray S, Kogan S, Cordoncardo C, Pelletier J, Lowe SW (2004) Survival signalling by Akt and eIF4E in oncogenesis and cancer therapy. Nature 428(6980):332–337PubMedCrossRef
60.
Zurück zum Zitat Jane EP, Premkumar DR, Morales A, Foster KA, Pollack IF (2014) Inhibition of phosphatidylinositol 3-kinase/AKT signaling by NVP-BKM120 promotes ABT-737-induced toxicity in a caspase-dependent manner through mitochondrial dysfunction and DNA damage response in established and primary cultured glioblastoma cells. J Pharmacol Exp Ther 350(1):22PubMedPubMedCentralCrossRef Jane EP, Premkumar DR, Morales A, Foster KA, Pollack IF (2014) Inhibition of phosphatidylinositol 3-kinase/AKT signaling by NVP-BKM120 promotes ABT-737-induced toxicity in a caspase-dependent manner through mitochondrial dysfunction and DNA damage response in established and primary cultured glioblastoma cells. J Pharmacol Exp Ther 350(1):22PubMedPubMedCentralCrossRef
61.
Zurück zum Zitat Tu Y, Gardner A, Lichtenstein A (2000) The phosphatidylinositol 3-kinase/AKT kinase pathway in multiple myeloma plasma cells: roles in cytokine-dependent survival and proliferative responses. Cancer Res 60(23):6763–6770PubMed Tu Y, Gardner A, Lichtenstein A (2000) The phosphatidylinositol 3-kinase/AKT kinase pathway in multiple myeloma plasma cells: roles in cytokine-dependent survival and proliferative responses. Cancer Res 60(23):6763–6770PubMed
62.
Zurück zum Zitat Fillmore GC, Wang Q, Carey MJ, Kim CH, Elenitoba-Johnson KS, Lim MS (2005) Expression of Akt (protein kinase B) and its isoforms in malignant lymphomas. Leuk Lymphoma 46(12):1765PubMedCrossRef Fillmore GC, Wang Q, Carey MJ, Kim CH, Elenitoba-Johnson KS, Lim MS (2005) Expression of Akt (protein kinase B) and its isoforms in malignant lymphomas. Leuk Lymphoma 46(12):1765PubMedCrossRef
63.
Zurück zum Zitat Slupianek A, Nieborowskaskorska M, Hoser G, Morrione A, Majewski M, Xue L, Morris SW, Wasik MA, Skorski T (2001) Role of phosphatidylinositol 3-kinase-akt pathway in nucleophosmin/anaplastic lymphoma kinase-mediated lymphomagenesis. Cancer Res 61(5):2194–2199PubMed Slupianek A, Nieborowskaskorska M, Hoser G, Morrione A, Majewski M, Xue L, Morris SW, Wasik MA, Skorski T (2001) Role of phosphatidylinositol 3-kinase-akt pathway in nucleophosmin/anaplastic lymphoma kinase-mediated lymphomagenesis. Cancer Res 61(5):2194–2199PubMed
64.
Zurück zum Zitat Dutton A, Reynolds GM, Dawson CW, Young LS, Murray PG (2005) Constitutive activation of phosphatidyl-inositide 3 kinase contributes to the survival of Hodgkin’s lymphoma cells through a mechanism involving Akt kinase and mTOR. J Pathol 205(4):498PubMedCrossRef Dutton A, Reynolds GM, Dawson CW, Young LS, Murray PG (2005) Constitutive activation of phosphatidyl-inositide 3 kinase contributes to the survival of Hodgkin’s lymphoma cells through a mechanism involving Akt kinase and mTOR. J Pathol 205(4):498PubMedCrossRef
65.
Zurück zum Zitat Morrison JA, Gulley ML, Pathmanathan R, Raabtraub N (2004) Differential signaling pathways are activated in the Epstein-Barr virus-associated malignancies nasopharyngeal carcinoma and Hodgkin lymphoma. Cancer Res 64(15):5251–5260PubMedCrossRef Morrison JA, Gulley ML, Pathmanathan R, Raabtraub N (2004) Differential signaling pathways are activated in the Epstein-Barr virus-associated malignancies nasopharyngeal carcinoma and Hodgkin lymphoma. Cancer Res 64(15):5251–5260PubMedCrossRef
66.
Zurück zum Zitat Jaffe ES (2001) Pathology and genetics of tumours of haematopoietic and lymphoid tissues. IARC Press, France Jaffe ES (2001) Pathology and genetics of tumours of haematopoietic and lymphoid tissues. IARC Press, France
67.
Zurück zum Zitat Sun X, Barlow EA, Ma S, Hagemeier SR, Duellman SJ, Burgess RR, Tellam J, Khanna R, Kenney SC (2010) Hsp90 inhibitors block outgrowth of EBV-infected malignant cells in vitro and in vivo through an EBNA1-dependent mechanism. Proc Natl Acad Sci USA 107(7):3146–3151PubMedPubMedCentralCrossRef Sun X, Barlow EA, Ma S, Hagemeier SR, Duellman SJ, Burgess RR, Tellam J, Khanna R, Kenney SC (2010) Hsp90 inhibitors block outgrowth of EBV-infected malignant cells in vitro and in vivo through an EBNA1-dependent mechanism. Proc Natl Acad Sci USA 107(7):3146–3151PubMedPubMedCentralCrossRef
68.
Zurück zum Zitat Gao L, Harhaj EW (2013) HSP90 Protects the human T-cell leukemia virus type 1 (HTLV-1) tax oncoprotein from proteasomal degradation to support NF-κB activation and HTLV-1 replication. J Virol 87(24):13640–13654PubMedPubMedCentralCrossRef Gao L, Harhaj EW (2013) HSP90 Protects the human T-cell leukemia virus type 1 (HTLV-1) tax oncoprotein from proteasomal degradation to support NF-κB activation and HTLV-1 replication. J Virol 87(24):13640–13654PubMedPubMedCentralCrossRef
69.
Zurück zum Zitat Tsou YL, Lin YW, Chang HW, Lin HY, Shao HY, Yu SL, Liu CC, Chitra E, Sia C, Chow YH (2013) Heat shock protein 90: role in enterovirus 71 entry and assembly and potential target for therapy. Plos One 8(10):e77133–e77133PubMedPubMedCentralCrossRef Tsou YL, Lin YW, Chang HW, Lin HY, Shao HY, Yu SL, Liu CC, Chitra E, Sia C, Chow YH (2013) Heat shock protein 90: role in enterovirus 71 entry and assembly and potential target for therapy. Plos One 8(10):e77133–e77133PubMedPubMedCentralCrossRef
70.
Zurück zum Zitat Burch AD, Weller SK (2005) Herpes simplex virus type 1 DNA polymerase requires the mammalian chaperone hsp90 for proper localization to the nucleus. J Virol 79(16):10740–10749PubMedPubMedCentralCrossRef Burch AD, Weller SK (2005) Herpes simplex virus type 1 DNA polymerase requires the mammalian chaperone hsp90 for proper localization to the nucleus. J Virol 79(16):10740–10749PubMedPubMedCentralCrossRef
72.
Zurück zum Zitat Chase G, Tao D, Fodor E, Bo WL, Mayer D, Schwemmle M, Brownlee G (2008) Hsp90 inhibitors reduce influenza virus replication in cell culture. Virology 377(2):431–439PubMedCrossRef Chase G, Tao D, Fodor E, Bo WL, Mayer D, Schwemmle M, Brownlee G (2008) Hsp90 inhibitors reduce influenza virus replication in cell culture. Virology 377(2):431–439PubMedCrossRef
73.
Zurück zum Zitat Momose F, Naito T, Yano K, Sugimoto S, Morikawa Y, Nagata K (2002) Identification of Hsp90 as a stimulatory host factor involved in influenza virus RNA synthesis. J Biol Chem 277(47):45306–45314PubMedCrossRef Momose F, Naito T, Yano K, Sugimoto S, Morikawa Y, Nagata K (2002) Identification of Hsp90 as a stimulatory host factor involved in influenza virus RNA synthesis. J Biol Chem 277(47):45306–45314PubMedCrossRef
74.
Zurück zum Zitat Naito T, Momose F, Kawaguchi A, Nagata K (2007) Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits. J Virol 81(3):1339–1349PubMedCrossRef Naito T, Momose F, Kawaguchi A, Nagata K (2007) Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits. J Virol 81(3):1339–1349PubMedCrossRef
75.
Zurück zum Zitat Panella S, Marcocci ME, Celestino I, Valente S, Zwergel C, Li PD, Nencioni L, Mai A, Palamara AT, Simonetti G (2016) MC1568 inhibits HDAC6/8 activity and influenza A virus replication in lung epithelial cells: role of Hsp90 acetylation. Future Med Chem 8(17):2017–2031 Panella S, Marcocci ME, Celestino I, Valente S, Zwergel C, Li PD, Nencioni L, Mai A, Palamara AT, Simonetti G (2016) MC1568 inhibits HDAC6/8 activity and influenza A virus replication in lung epithelial cells: role of Hsp90 acetylation. Future Med Chem 8(17):2017–2031
76.
Zurück zum Zitat Kawashima D, Kanda T, Murata T, Saito S, Sugimoto A, Narita Y, Tsurumi T (2013) Nuclear transport of Epstein-Barr virus DNA polymerase is dependent on the BMRF1 polymerase processivity factor and molecular chaperone Hsp90. J Virol 87(11):6482–6491PubMedPubMedCentralCrossRef Kawashima D, Kanda T, Murata T, Saito S, Sugimoto A, Narita Y, Tsurumi T (2013) Nuclear transport of Epstein-Barr virus DNA polymerase is dependent on the BMRF1 polymerase processivity factor and molecular chaperone Hsp90. J Virol 87(11):6482–6491PubMedPubMedCentralCrossRef
77.
Zurück zum Zitat Vendeville A, Rayne F, Bonhoure A, Bettache N, Montcourrier P, Beaumelle B (2004) HIV-1 Tat enters T cells using coated pits before translocating from acidified endosomes and eliciting biological responses. Mol Biol Cell 15(5):2347–2360PubMedPubMedCentralCrossRef Vendeville A, Rayne F, Bonhoure A, Bettache N, Montcourrier P, Beaumelle B (2004) HIV-1 Tat enters T cells using coated pits before translocating from acidified endosomes and eliciting biological responses. Mol Biol Cell 15(5):2347–2360PubMedPubMedCentralCrossRef
78.
Zurück zum Zitat Vozzolo L, Loh B, Gane PJ, Tribak M, Zhou L, Anderson I, Nyakatura E, Jenner RG, Selwood D, Fassati A (2010) Gyrase B inhibitor impairs HIV-1 replication by targeting Hsp90 and the capsid protein. J Biol Chem 285(50):39314–39328PubMedPubMedCentralCrossRef Vozzolo L, Loh B, Gane PJ, Tribak M, Zhou L, Anderson I, Nyakatura E, Jenner RG, Selwood D, Fassati A (2010) Gyrase B inhibitor impairs HIV-1 replication by targeting Hsp90 and the capsid protein. J Biol Chem 285(50):39314–39328PubMedPubMedCentralCrossRef
79.
Zurück zum Zitat Sun X, Bristol JA, Iwahori S, Hagemeier SR, Meng Q, Barlow EA, Fingeroth JD, Tarakanova VL, Kalejta RF, Kenney SC (2013) Hsp90 Inhibitor 17-DMAG decreases expression of conserved herpesvirus protein kinases and reduces virus production in Epstein-Barr virus-infected cells. J Virol 87(18):10126–10138PubMedPubMedCentralCrossRef Sun X, Bristol JA, Iwahori S, Hagemeier SR, Meng Q, Barlow EA, Fingeroth JD, Tarakanova VL, Kalejta RF, Kenney SC (2013) Hsp90 Inhibitor 17-DMAG decreases expression of conserved herpesvirus protein kinases and reduces virus production in Epstein-Barr virus-infected cells. J Virol 87(18):10126–10138PubMedPubMedCentralCrossRef
80.
Zurück zum Zitat Czar MJ, Galigniana MD, Silverstein AM, Pratt WB (1997) Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus†. Biochemistry 36(25):7776–7785PubMedCrossRef Czar MJ, Galigniana MD, Silverstein AM, Pratt WB (1997) Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus†. Biochemistry 36(25):7776–7785PubMedCrossRef
82.
Zurück zum Zitat Okamoto T, Nishimura Y, Ichimura T, Suzuki K, Miyamura T, Suzuki T, Moriishi K, Matsuura Y (2006) Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90. Embo J 25(20):5015–5025PubMedPubMedCentralCrossRef Okamoto T, Nishimura Y, Ichimura T, Suzuki K, Miyamura T, Suzuki T, Moriishi K, Matsuura Y (2006) Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90. Embo J 25(20):5015–5025PubMedPubMedCentralCrossRef
83.
Zurück zum Zitat Taguwa S, Okamoto T, Abe T, Mori Y, Suzuki T, Moriishi K, Matsuura Y (2008) Human butyrate-Induced transcript 1 interacts with hepatitis C virus NS5A and regulates viral replication. J Virol 82(6):2631–2641PubMedCrossRef Taguwa S, Okamoto T, Abe T, Mori Y, Suzuki T, Moriishi K, Matsuura Y (2008) Human butyrate-Induced transcript 1 interacts with hepatitis C virus NS5A and regulates viral replication. J Virol 82(6):2631–2641PubMedCrossRef
84.
Zurück zum Zitat Okamoto T, Omori H, Kaname Y, Abe T, Nishimura Y, Suzuki T, Miyamura T, Yoshimori T, Moriishi K, Matsuura Y (2008) A single-amino-acid mutation in hepatitis C virus NS5A disrupting FKBP8 interaction impairs viral replication. J Virol 82(7):3480–3489PubMedPubMedCentralCrossRef Okamoto T, Omori H, Kaname Y, Abe T, Nishimura Y, Suzuki T, Miyamura T, Yoshimori T, Moriishi K, Matsuura Y (2008) A single-amino-acid mutation in hepatitis C virus NS5A disrupting FKBP8 interaction impairs viral replication. J Virol 82(7):3480–3489PubMedPubMedCentralCrossRef
85.
Zurück zum Zitat Waxman L, Whitney M, Pollok BA, Kuo LC, Darke PL (2001) Host cell factor requirement for hepatitis C virus enzyme maturation. Proc Natl Acad Sci USA 98(24):13931–13935PubMedPubMedCentralCrossRef Waxman L, Whitney M, Pollok BA, Kuo LC, Darke PL (2001) Host cell factor requirement for hepatitis C virus enzyme maturation. Proc Natl Acad Sci USA 98(24):13931–13935PubMedPubMedCentralCrossRef
86.
Zurück zum Zitat Hu J, Flores D, Toft D, Wang X, Nguyen D (2004) Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function. J Virol 78(23):13122–13131PubMedPubMedCentralCrossRef Hu J, Flores D, Toft D, Wang X, Nguyen D (2004) Requirement of heat shock protein 90 for human hepatitis B virus reverse transcriptase function. J Virol 78(23):13122–13131PubMedPubMedCentralCrossRef
87.
88.
Zurück zum Zitat Hu J, Anselmo D (2000) In vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: posttranslational activation by Hsp90. J Virol 74(24):11447–11455PubMedPubMedCentralCrossRef Hu J, Anselmo D (2000) In vitro reconstitution of a functional duck hepatitis B virus reverse transcriptase: posttranslational activation by Hsp90. J Virol 74(24):11447–11455PubMedPubMedCentralCrossRef
89.
Zurück zum Zitat Wang X, Grammatikakis N, Hu J (2002) Role of p50/CDC37 in hepadnavirus assembly and replication. J Biol Chem 277(27):24361–24367PubMedCrossRef Wang X, Grammatikakis N, Hu J (2002) Role of p50/CDC37 in hepadnavirus assembly and replication. J Biol Chem 277(27):24361–24367PubMedCrossRef
90.
Zurück zum Zitat Vashist S, Urena L, Gonzalez-Hernandez MB, Choi J, De RA, Rocha-Pereira J, Neyts J, Hwang S, Wobus CE, Goodfellow I (2015) Molecular chaperone hsp90 is a therapeutic target for noroviruses. J Virol 89(12):6352–6363PubMedPubMedCentralCrossRef Vashist S, Urena L, Gonzalez-Hernandez MB, Choi J, De RA, Rocha-Pereira J, Neyts J, Hwang S, Wobus CE, Goodfellow I (2015) Molecular chaperone hsp90 is a therapeutic target for noroviruses. J Virol 89(12):6352–6363PubMedPubMedCentralCrossRef
91.
Zurück zum Zitat Connor JH, Mckenzie MO, Parks GD, Lyles DS (2007) Antiviral activity and RNA polymerase degradation following Hsp90 inhibition in a range of negative strand viruses. Virology 362(1):109–119PubMedPubMedCentralCrossRef Connor JH, Mckenzie MO, Parks GD, Lyles DS (2007) Antiviral activity and RNA polymerase degradation following Hsp90 inhibition in a range of negative strand viruses. Virology 362(1):109–119PubMedPubMedCentralCrossRef
93.
Zurück zum Zitat Geller R, Vignuzzi M, Andino R, Frydman J (2007) Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractor. Genes Dev 21(2):195–205PubMedPubMedCentralCrossRef Geller R, Vignuzzi M, Andino R, Frydman J (2007) Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractor. Genes Dev 21(2):195–205PubMedPubMedCentralCrossRef
94.
Zurück zum Zitat Chen W, Sin SH, Wen KW, Damania B, Dittmer DP (2012) Hsp90 inhibitors are efficacious against Kaposi Sarcoma by enhancing the degradation of the essential viral gene LANA, of the viral co-receptor EphA2 as well as other client proteins. PLoS Pathog 8(11):276–287 Chen W, Sin SH, Wen KW, Damania B, Dittmer DP (2012) Hsp90 inhibitors are efficacious against Kaposi Sarcoma by enhancing the degradation of the essential viral gene LANA, of the viral co-receptor EphA2 as well as other client proteins. PLoS Pathog 8(11):276–287
95.
Zurück zum Zitat Miyata Y, Yahara I (2000) p53-independent association between SV40 large T antigen and the major cytosolic heat shock protein, HSP90. Oncogene 19(11):1477–1484PubMedCrossRef Miyata Y, Yahara I (2000) p53-independent association between SV40 large T antigen and the major cytosolic heat shock protein, HSP90. Oncogene 19(11):1477–1484PubMedCrossRef
96.
Zurück zum Zitat Ehrenkranz NJ, Meyer KF (2014) Multi-faceted proteomic characterization of host protein complement of rift valley fever virus virions and identification of specific heat shock proteins, including HSP90, as important viral host factors. Plos One 9(5):e93483CrossRef Ehrenkranz NJ, Meyer KF (2014) Multi-faceted proteomic characterization of host protein complement of rift valley fever virus virions and identification of specific heat shock proteins, including HSP90, as important viral host factors. Plos One 9(5):e93483CrossRef
97.
Zurück zum Zitat Hung CY, Tsai MC, Wu YP, Wang RY (2011) Identification of heat-shock protein 90 beta in Japanese encephalitis virus-induced secretion proteins. J Gen Virol 92(Pt 12):2803–2809PubMedCrossRef Hung CY, Tsai MC, Wu YP, Wang RY (2011) Identification of heat-shock protein 90 beta in Japanese encephalitis virus-induced secretion proteins. J Gen Virol 92(Pt 12):2803–2809PubMedCrossRef
98.
Zurück zum Zitat Smith DR, Mccarthy S, Chrovian A, Olinger G, Stossel A, Geisbert TW, Hensley LE, Connor JH (2010) Inhibition of heat-shock protein 90 reduces Ebola virus replication. Antivir Res 87(2):187–194PubMedPubMedCentralCrossRef Smith DR, Mccarthy S, Chrovian A, Olinger G, Stossel A, Geisbert TW, Hensley LE, Connor JH (2010) Inhibition of heat-shock protein 90 reduces Ebola virus replication. Antivir Res 87(2):187–194PubMedPubMedCentralCrossRef
99.
Zurück zum Zitat Czar MJ, Galigniana MD, Silverstein AM, Pratt WB (1997) Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus. Biochemistry 36(25):7776–7785PubMedCrossRef Czar MJ, Galigniana MD, Silverstein AM, Pratt WB (1997) Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus. Biochemistry 36(25):7776–7785PubMedCrossRef
100.
Zurück zum Zitat Chou CK, Wang LH, Lin HM, Chi CW (1992) Glucocorticoid stimulates hepatitis B viral gene expression in cultured human hepatoma cells. Hepatology 16(1):13–18PubMedCrossRef Chou CK, Wang LH, Lin HM, Chi CW (1992) Glucocorticoid stimulates hepatitis B viral gene expression in cultured human hepatoma cells. Hepatology 16(1):13–18PubMedCrossRef
101.
Zurück zum Zitat Chalepakis G, Arnemann J, Slater E, Brüller HJ, Gross B, Beato M (1988) Differential gene activation by glucocorticoids and progestins through the hormone regulatory element of mouse mammary tumor virus. Cell 53(3):371–382PubMedCrossRef Chalepakis G, Arnemann J, Slater E, Brüller HJ, Gross B, Beato M (1988) Differential gene activation by glucocorticoids and progestins through the hormone regulatory element of mouse mammary tumor virus. Cell 53(3):371–382PubMedCrossRef
102.
Zurück zum Zitat Chou CK, Wang LH, Lin HM, Chi CW (1992) Glucocorticoid stimulates hepatitis B viral gene expression in cultured human hepatoma cells. Hepatology 16(1):13–18PubMedCrossRef Chou CK, Wang LH, Lin HM, Chi CW (1992) Glucocorticoid stimulates hepatitis B viral gene expression in cultured human hepatoma cells. Hepatology 16(1):13–18PubMedCrossRef
103.
Zurück zum Zitat Li YH, Tao PZ, Liu YZ, Jiang JD (2004) Geldanamycin, a ligand of heat shock protein 90, inhibits the replication of herpes simplex virus type 1 in vitro. Antimicrob Agents Chemother 48(3):867–872PubMedPubMedCentralCrossRef Li YH, Tao PZ, Liu YZ, Jiang JD (2004) Geldanamycin, a ligand of heat shock protein 90, inhibits the replication of herpes simplex virus type 1 in vitro. Antimicrob Agents Chemother 48(3):867–872PubMedPubMedCentralCrossRef
104.
Zurück zum Zitat Brice A, Moseley GW (2013) Viral interactions with microtubules: orchestrators of host cell biology? Future Virol 8(3):229–243CrossRef Brice A, Moseley GW (2013) Viral interactions with microtubules: orchestrators of host cell biology? Future Virol 8(3):229–243CrossRef
105.
Zurück zum Zitat Radtke K, Döhner K, Sodeik B (2006) Viral interactions with the cytoskeleton: a hitchhiker’s guide to the cell. Cell Microbiol 8(3):387–400PubMedCrossRef Radtke K, Döhner K, Sodeik B (2006) Viral interactions with the cytoskeleton: a hitchhiker’s guide to the cell. Cell Microbiol 8(3):387–400PubMedCrossRef
106.
Zurück zum Zitat Kannan H (2009) The hepatitis E virus open reading frame 3 product interacts with microtubules and interferes with their dynamics. J Virol 83(13):6375–6382PubMedPubMedCentralCrossRef Kannan H (2009) The hepatitis E virus open reading frame 3 product interacts with microtubules and interferes with their dynamics. J Virol 83(13):6375–6382PubMedPubMedCentralCrossRef
107.
Zurück zum Zitat Perdiz D, Mackeh R, Poüs C, Baillet A (2010) The ins and outs of tubulin acetylation: more than just a post-translational modification? Cell Signal 23(5):763–771PubMedCrossRef Perdiz D, Mackeh R, Poüs C, Baillet A (2010) The ins and outs of tubulin acetylation: more than just a post-translational modification? Cell Signal 23(5):763–771PubMedCrossRef
108.
Zurück zum Zitat Husain M, Gupta C (1997) Interactions of viral matrix protein and nucleoprotein with the host cell cytoskeletal actin in influenza viral infection. Curr Sci 73(1):40–47 Husain M, Gupta C (1997) Interactions of viral matrix protein and nucleoprotein with the host cell cytoskeletal actin in influenza viral infection. Curr Sci 73(1):40–47
109.
Zurück zum Zitat Xuan C, Qiao W, Gao J, Liu M, Zhang X, Cao Y, Chen Q, Geng Y, Zhou J (2007) Regulation of microtubule assembly and stability by the transactivator of transcription protein of Jembrana disease virus. J Biol Chem 282(39):28800–28806PubMedCrossRef Xuan C, Qiao W, Gao J, Liu M, Zhang X, Cao Y, Chen Q, Geng Y, Zhou J (2007) Regulation of microtubule assembly and stability by the transactivator of transcription protein of Jembrana disease virus. J Biol Chem 282(39):28800–28806PubMedCrossRef
110.
Zurück zum Zitat Basha W, Kitagawa R, Uhara M, Imazu H, Uechi K, Tanaka J (2005) Geldanamycin, a potent and specific inhibitor of Hsp90, inhibits gene expression and replication of human cytomegalovirus. Antivir Chem Chemother 16(2):135–146PubMedCrossRef Basha W, Kitagawa R, Uhara M, Imazu H, Uechi K, Tanaka J (2005) Geldanamycin, a potent and specific inhibitor of Hsp90, inhibits gene expression and replication of human cytomegalovirus. Antivir Chem Chemother 16(2):135–146PubMedCrossRef
111.
Zurück zum Zitat Staff PO (2015) Heat shock protein 90 positively regulates chikungunya virus replication by stabilizing viral non-structural protein nsP2 during infection. Plos One 10(6):e100531 Staff PO (2015) Heat shock protein 90 positively regulates chikungunya virus replication by stabilizing viral non-structural protein nsP2 during infection. Plos One 10(6):e100531
112.
Zurück zum Zitat Hu J, Toft DO, Seeger C (1997) Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids. Embo J 16(1):59–68PubMedPubMedCentralCrossRef Hu J, Toft DO, Seeger C (1997) Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids. Embo J 16(1):59–68PubMedPubMedCentralCrossRef
113.
Zurück zum Zitat Taldone T, Sun W, Chiosis G (2009) Discovery and development of heat shock protein 90 inhibitors. Bioorg Med Chem 17(6):2225–2235PubMedCrossRef Taldone T, Sun W, Chiosis G (2009) Discovery and development of heat shock protein 90 inhibitors. Bioorg Med Chem 17(6):2225–2235PubMedCrossRef
114.
Zurück zum Zitat Solit DB, Zheng FF, Drobnjak M, Münster PN, Higgins B, Verbel D, Heller G, Tong W, Cordoncardo C, Agus DB (2002) 17-Allylamino-17-demethoxygeldanamycin induces the degradation of androgen receptor and HER-2/neu and inhibits the growth of prostate cancer xenografts. Clin Cancer Res Off J Am Assoc Cancer Res 8(5):986–993 Solit DB, Zheng FF, Drobnjak M, Münster PN, Higgins B, Verbel D, Heller G, Tong W, Cordoncardo C, Agus DB (2002) 17-Allylamino-17-demethoxygeldanamycin induces the degradation of androgen receptor and HER-2/neu and inhibits the growth of prostate cancer xenografts. Clin Cancer Res Off J Am Assoc Cancer Res 8(5):986–993
115.
Zurück zum Zitat Liao ZY, Zhen YS (2001) Advances in antitumor activity of the hsp90 inhibitor geldanamycin. Yao xue xue bao (Acta pharmaceutica Sinica) 36(9):716–720 Liao ZY, Zhen YS (2001) Advances in antitumor activity of the hsp90 inhibitor geldanamycin. Yao xue xue bao (Acta pharmaceutica Sinica) 36(9):716–720
116.
Zurück zum Zitat Jez JM, Chen JC, Rastelli G, Stroud RM, Santi DV (2003) Crystal structure and molecular modeling of 17-DMAG in complex with human Hsp90. Chem Biol 10(4):361–368PubMedCrossRef Jez JM, Chen JC, Rastelli G, Stroud RM, Santi DV (2003) Crystal structure and molecular modeling of 17-DMAG in complex with human Hsp90. Chem Biol 10(4):361–368PubMedCrossRef
117.
Zurück zum Zitat Shen G, Wang M, Welch TR, Blagg BSJ (2006) Design, synthesis, and structureactivity relationships for chimeric inhibitors of Hsp90. J Org Chem 71(20):7618–7631PubMedCrossRef Shen G, Wang M, Welch TR, Blagg BSJ (2006) Design, synthesis, and structureactivity relationships for chimeric inhibitors of Hsp90. J Org Chem 71(20):7618–7631PubMedCrossRef
118.
Zurück zum Zitat Roe SM, Obrien R, Ladbury JE, Piper PW, Pearl LH, Prodromou C (1999) Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J Med Chem 42(2):260–266PubMedCrossRef Roe SM, Obrien R, Ladbury JE, Piper PW, Pearl LH, Prodromou C (1999) Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J Med Chem 42(2):260–266PubMedCrossRef
119.
Zurück zum Zitat Schumacher JA, Crockett DK, Elenitoba-Johnson KS, Lim MS (2007) Proteome-wide changes induced by the Hsp90 inhibitor, geldanamycin in anaplastic large cell lymphoma cells. Proteomics 7(15):2603–2616PubMedCrossRef Schumacher JA, Crockett DK, Elenitoba-Johnson KS, Lim MS (2007) Proteome-wide changes induced by the Hsp90 inhibitor, geldanamycin in anaplastic large cell lymphoma cells. Proteomics 7(15):2603–2616PubMedCrossRef
120.
Zurück zum Zitat Agnew EB, Wilson RH, Grem JL, Neckers L, Bi D, Takimoto CH (2001) Measurement of the novel antitumor agent 17-(allylamino)-17-demethoxygeldanamycin in human plasma by high-performance liquid chromatography. J Chromatogr B Biomed Sci Appl 755(1–2):237–243PubMedCrossRef Agnew EB, Wilson RH, Grem JL, Neckers L, Bi D, Takimoto CH (2001) Measurement of the novel antitumor agent 17-(allylamino)-17-demethoxygeldanamycin in human plasma by high-performance liquid chromatography. J Chromatogr B Biomed Sci Appl 755(1–2):237–243PubMedCrossRef
121.
Zurück zum Zitat Gao J, Xiao S, Liu X, Wang L, Zhang X, Ji Q, Yue W, Mo D, Chen Y (2014) Inhibition of HSP90 attenuates porcine reproductive and respiratory syndrome virus production in vitro. Virol J 11(1):1–9CrossRef Gao J, Xiao S, Liu X, Wang L, Zhang X, Ji Q, Yue W, Mo D, Chen Y (2014) Inhibition of HSP90 attenuates porcine reproductive and respiratory syndrome virus production in vitro. Virol J 11(1):1–9CrossRef
122.
Zurück zum Zitat Ujino S, Yamaguchi S, Shimotohno K, Takaku H (2009) Heat-shock protein 90 is essential for stabilization of the hepatitis C virus nonstructural protein NS3. J Biol Chem 284(11):6841–6846PubMedPubMedCentralCrossRef Ujino S, Yamaguchi S, Shimotohno K, Takaku H (2009) Heat-shock protein 90 is essential for stabilization of the hepatitis C virus nonstructural protein NS3. J Biol Chem 284(11):6841–6846PubMedPubMedCentralCrossRef
123.
Zurück zum Zitat Kim MG, Moon JS, Kim EJ, Lee SH, Oh JW (2012) Destabilization of PDK1 by Hsp90 inactivation suppresses hepatitis C virus replication through inhibition of PRK2-mediated viral RNA polymerase phosphorylation. Biochem Biophys Res Commun 421(1):112PubMedCrossRef Kim MG, Moon JS, Kim EJ, Lee SH, Oh JW (2012) Destabilization of PDK1 by Hsp90 inactivation suppresses hepatitis C virus replication through inhibition of PRK2-mediated viral RNA polymerase phosphorylation. Biochem Biophys Res Commun 421(1):112PubMedCrossRef
124.
Zurück zum Zitat Chung CS, Chen CH, Ho MY, Huang CY, Liao CL, Chang W (2006) Vaccinia virus proteome: identification of proteins in vaccinia virus intracellular mature virion particles. J Virol 80(5):2127–2140PubMedPubMedCentralCrossRef Chung CS, Chen CH, Ho MY, Huang CY, Liao CL, Chang W (2006) Vaccinia virus proteome: identification of proteins in vaccinia virus intracellular mature virion particles. J Virol 80(5):2127–2140PubMedPubMedCentralCrossRef
125.
Zurück zum Zitat Rice JW, Veal JM, Fadden RP, Barabasz AF, Partridge JM, Barta TE, Dubois LG, Huang KH, Mabbett SR, Silinski MA, Steed PM, Hall SE (2008) Small molecule inhibitors of Hsp90 potently affect inflammatory disease pathways and exhibit activity in models of rheumatoid arthritis. Arthritis Rheum 58(12):3765–3775. doi:10.1002/art.24047 PubMedCrossRef Rice JW, Veal JM, Fadden RP, Barabasz AF, Partridge JM, Barta TE, Dubois LG, Huang KH, Mabbett SR, Silinski MA, Steed PM, Hall SE (2008) Small molecule inhibitors of Hsp90 potently affect inflammatory disease pathways and exhibit activity in models of rheumatoid arthritis. Arthritis Rheum 58(12):3765–3775. doi:10.​1002/​art.​24047 PubMedCrossRef
Metadaten
Titel
HSP90: a promising broad-spectrum antiviral drug target
verfasst von
Yiliang Wang
Fujun Jin
Rongze Wang
Feng Li
Yanting Wu
Kaio Kitazato
Yifei Wang
Publikationsdatum
05.08.2017
Verlag
Springer Vienna
Erschienen in
Archives of Virology / Ausgabe 11/2017
Print ISSN: 0304-8608
Elektronische ISSN: 1432-8798
DOI
https://doi.org/10.1007/s00705-017-3511-1

Weitere Artikel der Ausgabe 11/2017

Archives of Virology 11/2017 Zur Ausgabe

Leitlinien kompakt für die Innere Medizin

Mit medbee Pocketcards sicher entscheiden.

Seit 2022 gehört die medbee GmbH zum Springer Medizin Verlag

Update Innere Medizin

Bestellen Sie unseren Fach-Newsletter und bleiben Sie gut informiert.