WO2016207366A1 - Méthodes et compositions pharmaceutiques de traitement d'infections virales - Google Patents

Méthodes et compositions pharmaceutiques de traitement d'infections virales Download PDF

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Publication number
WO2016207366A1
WO2016207366A1 PCT/EP2016/064696 EP2016064696W WO2016207366A1 WO 2016207366 A1 WO2016207366 A1 WO 2016207366A1 EP 2016064696 W EP2016064696 W EP 2016064696W WO 2016207366 A1 WO2016207366 A1 WO 2016207366A1
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Prior art keywords
virus
ifn
catenin
licl
cells
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Ceased
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PCT/EP2016/064696
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English (en)
Inventor
Eliette BONNEFOY
Charbel Massaad
Vasco MARCATO
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Centre National de la Recherche Scientifique CNRS
Institut National de la Sante et de la Recherche Medicale INSERM
Universite Paris Descartes
Original Assignee
Centre National de la Recherche Scientifique CNRS
Institut National de la Sante et de la Recherche Medicale INSERM
Universite Paris Descartes
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Publication of WO2016207366A1 publication Critical patent/WO2016207366A1/fr
Anticipated expiration legal-status Critical
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    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K33/00—Medicinal preparations containing inorganic active ingredients
    • A61K33/14—Alkali metal chlorides; Alkaline earth metal chlorides

Definitions

  • one object of the present invention relates to a method of treating a viral infection in a subject in need thereof comprising administering to the subject a therapeutically effective amount of an inhibitor of glycogen synthase kinase 3 (GSK3).
  • GSK3 glycogen synthase kinase 3
  • Treatment may be for any purpose, including the therapeutic treatment of subjects suffering from a viral infection, as well as the prophylactic treatment of subjects who do not suffer from a viral infection (e.g., subjects identified as being at high risk a viral infection).
  • treatment refers to reversing, alleviating, inhibiting the progress of a disease or disorder as described herein (i.e. a viral infection), or delaying, eliminating or reducing the incidence or onset of a disorder or disease as described herein, as compared to that which would occur in the absence of the measure taken.
  • the daily dosage of the products may be varied over a wide range from 0.01 to 1,000 mg per adult per day.
  • the compositions contain 0.01, 0.05, 0.1, 0.5, 1.0, 2.5, 5.0, 10.0, 15.0, 25.0, 50.0, 100, 250 and 500 mg of the active ingredient for the symptomatic adjustment of the dosage to the subject to be treated.
  • a medicament typically contains from about 0.01 mg to about 500 mg of the active ingredient, preferably from 1 mg to about 100 mg of the active ingredient.
  • An effective amount of the drug is ordinarily supplied at a dosage level from 0.0002 mg/kg to about 20 mg/kg of body weight per day, especially from about 0.001 mg/kg to 7 mg/kg of body weight per day.
  • anti-viral compounds typically include but are not limited to ACH-1625 (Achillion); Glycosylated interferon (Alios Biopharma); ANA598, ANA773 (Anadys Pharm); ATI-0810 (Arisyn Therapeutics); AVL-181 (Avila Therapeutics); LOCTERON® (Biolex); CTS-1027 (Conatus); SD-101 (Dynavax Technologies); Clemizole (Eiger Biopharmaceuticals); GS-9190 (Gilead Sciences); GI-5005 (Globallmmune BioPharma); Resiquimod/R-848 (Graceway Pharmaceuticals); Albinterferon alpha-2b (Human Genome Sciences); IDX-184, IDX-320, IDX-375 (Idenix); IMO-2125 (Idera Pharmaceuticals); INX-189 (Inhibitex); ITCA-638 (Intarcia Therapeutics); ITMN- 191/RG7227
  • saline solutions monosodium or disodium phosphate, sodium, potassium, calcium or magnesium chloride and the like or mixtures of such salts
  • dry, especially freeze-dried compositions which upon addition, depending on the case, of sterilized water or physiological saline, permit the constitution of injectable solutions.
  • the pharmaceutical forms suitable for injectable use include sterile aqueous solutions or dispersions; formulations including sesame oil, peanut oil or aqueous propylene glycol; and sterile powders for the extemporaneous preparation of sterile injectable solutions or dispersions. In all cases, the form must be sterile and must be fluid to the extent that easy syringability exists.
  • ⁇ -catenin was analyzed by Western blot (C) in nuclear extracts from L929 cells either non treated (NT) or treated with 20 mM LiCl (LiCl) during 24h.
  • IFN- ⁇ mRNA (D and H) and Oaslb or IRF7 m NA (E) were analyzed by RT-qPCR: in non-infected L929 cells either non-treated (NT) or LiCl treated (LiCl) (D and E); at different times post-infection (p.i) in L929 cells mock- or NDV-infected, either non-treated (NT) or pre-treated with LiCl (LiCl) (H).
  • AML12 cells were either non-treated (NT) or treated with 20mM LiCl (LiCl) during 24h and either non-infected (A-C) or NDV-infected (D).
  • NT non-treated
  • LiCl LiCl
  • D NDV-infected
  • a and B Cells were labeled with an anti- ⁇ - catenin antibody (a, d) and a DNA intercalating agent to visualize the nucleus (ToPro3; b, e). Nuclei were outlined as shown in merge images (c, f), and total green pixel intensity corresponding to ⁇ -catenin labeling in the nucleus was quantified (B).
  • BMDM bone marrow-derived macrophages
  • Monolayer cultures of L929 cells in 96-well plates were incubated with LiCl for 24 h before VSV infection. Before VSV infection, the medium containing LiCl was removed. Viruses were diluted in medium with serum (2% final concentration) and added directly to the culture medium. The monolayers were stained with crystal violet as vital dye 24 h after VSV infection or fixed 8h after VSV infection for immunofluorescence analysis.
  • L929 cells either non-treated or treated with LiCl for 24 h were infected with RVFVZH548 and incubated under an overlay consisting of DMEM, 2% fetal calf serum, antibiotics and 1% agarose at 37°C. At 3 day p.i., the lytic plaques were counted after staining with a solution of crystal violet.
  • mice were conducted according to the French and European regulations on care and protection of laboratory animals (EC Directive 86/609, French Law 2001-486 issued on June 6, 2001) and the National Institutes of Health Animal Welfare (Insurance #A5476-01 issued on 02/07/2007).
  • Experimental protocols were approved by the Animal Ethics Committee #1 of the Comite Regional d'Ethique pour V Experimentation Animale (CREEA), He de France (N°2012-0025), and carried out in compliance with Institut Pasteur Biosafety Committee.
  • LiCl treatment enhances constitutive IFN- ⁇ gene expression.
  • IFN- ⁇ gene expression in non-infected cells, corresponding to an IRF3-NF-KB-ATF2/c-Jun independent expression that we have considered as constitutive IFN- ⁇ expression, before and after nuclear accumulation of ⁇ -catenin.
  • IFN- ⁇ gene expression was carried out in murine fibroblastic L929 cells, which are potent IFN- ⁇ producer cells.
  • the role of the NRDII region containing a TCF binding site during LiCl-dependent promoter activation was also analyzed after virus infection. As shown in Fig. 3B, LiCl treatment enhanced the virus-induced activity of the WT330 promoter but not that of the WT110 promoter. Therefore, the presence of the NRDII region containing a TCF-binding site was also required for the LiCl-dependent enhancement of the virus-induced transcriptional capacity of the IFN- ⁇ promoter. The presence of only the VRE region, containing the IRF3 binding site (promoter WT110), was not sufficient to either recruit ⁇ -catenin or mediate LiCl enhancement of the constitutive as well as virus-induced transcriptional capacity of the IFN- ⁇ promoter.
  • the canonical Wnt/p-catenin pathway is a major target of Rift Valley fever virus.
  • RVFV ZH548 strain of the virus that codes for a non-structural NSs protein, suppresses IFN- ⁇ expression and is highly pathogenic causing severe illness in men and animals (51-53)
  • RVFV ZH548ANSs strain ANSs
  • the viral NSs protein which is a major factor responsible of RVFV pathogenicity, has the characteristic to form filamentous structures in nuclei of infected cells abnormally trapping within these structures transcription factors and co-factors of the host (21,55).
  • RVFV NSs protein a major factor responsible of RVFV pathogenicity
  • NSs The viral NSs protein, which is a major factor responsible of RVFV pathogenicity, has the characteristic to form filamentous structures in nuclei of infected cells abnormally trapping within these structures transcription factors and co-factors of the host (21,55).
  • Table I genes associated with the canonical Wnt/ -catenin pathway were identified as interacting with NSs (Table I) (56).
  • DNA regulatory sequences associated with genes coding for casein kinases (Csnkld, Csnklg2, Csnklg3 and Csnk2a2) known to positively regulate the canonical Wnt/ -catenin signaling pathway at different levels were present among cellular DNA regions targeted by NSs.
  • infection with the avirulent ANSs strain strongly activated IFN- ⁇ gene expression in the three cell types tested, whereas infection with the virulent ZH strain maintained the IFN- ⁇ expression in an abnormally repressed state.
  • ⁇ -catenin was analyzed in the liver and brain of mice that were either non- infected, or infected with ANSs or ZH strains.
  • the liver and brain are two main organs targeted during RVFV infection (58). Mice were euthanized at days 3 and 5 p.i. and the liver and brain were removed; one half of each organ was used for total protein purification and Western blot analysis and the other half for RNA purification and RT-qPCR analysis.
  • results shown here indicate that in vivo, ⁇ -catenin is targeted during RVFV infection with the level of ⁇ -catenin diminished in the liver of mice that were unable to efficiently inhibit virus production.
  • Virus-induced IFN- ⁇ expression depends on the presence of several transcription factors and co-factors that synergize to give rise to a maximum of expression (16-27).
  • RVFV infection counteracts the transcriptional activation of the IFN- ⁇ expression by abnormally maintaining the IFN- ⁇ promoter region associated to a transcriptionally repressive environment (16, 21).
  • LiCl inhibits PRRSV infection by enhancing Wnt/ -catenin pathway and suppressing inflammatory responses.
  • HIV-1 Human immunodeficiency virus type 1 transactivator of transcription through its intact core and cysteine-rich domains inhibits Wnt/p-catenin signaling in astrocytes: relevance to HIV neuropathogenesis. J. Neurosci. 32: 16306-13.
  • Type-1 interferon signaling mediates neuro-inflammatory events in models of Alzheimer's disease. Neurobiol. Aging 35: 1012-23.

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  • Health & Medical Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Inorganic Chemistry (AREA)
  • Medicinal Chemistry (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Epidemiology (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Animal Behavior & Ethology (AREA)
  • General Health & Medical Sciences (AREA)
  • Public Health (AREA)
  • Veterinary Medicine (AREA)
  • Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)

Abstract

La présente invention concerne des méthodes et des compositions pharmaceutiques pour le traitement d'infections virales. La présente invention concerne en particulier une méthode de traitement d'une infection virale chez un sujet le requérant, qui consiste à administrer au sujet une dose thérapeutiquement efficace d'un inhibiteur de glycogène synthase kinase 3 (GSK3).
PCT/EP2016/064696 2015-06-26 2016-06-24 Méthodes et compositions pharmaceutiques de traitement d'infections virales Ceased WO2016207366A1 (fr)

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EP15306011.6 2015-06-26
EP15306011 2015-06-26

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WO2016207366A1 true WO2016207366A1 (fr) 2016-12-29

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Cited By (4)

* Cited by examiner, † Cited by third party
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CN106822176A (zh) * 2017-03-13 2017-06-13 中国农业科学院兰州兽医研究所 一种以氯化锂为有效成分的口蹄疫病毒抑制剂
CN114028390A (zh) * 2021-09-26 2022-02-11 中山大学肿瘤防治中心（中山大学附属肿瘤医院、中山大学肿瘤研究所） 化合物kya1797k制备抗rna病毒药物中的应用
CN114377009A (zh) * 2020-10-21 2022-04-22 中国医学科学院药物研究所 Sb216763在制备抗流感病毒药物中的应用
CN114717265A (zh) * 2022-04-14 2022-07-08 中国医学科学院医学生物学研究所 一种适用于柯萨奇病毒a6培养的新型稳转细胞系及其应用

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EP2433636A1 (fr) 2010-09-27 2012-03-28 Medizinische Universität Wien Traitement de maladies malignes

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EP0328026A1 (fr) 1988-02-10 1989-08-16 F. Hoffmann-La Roche Ag Pyrroles substitués
EP0384349A1 (fr) 1989-02-23 1990-08-29 F. Hoffmann-La Roche Ag Pyrroles substitués
DE3914764A1 (de) 1989-05-05 1990-11-08 Goedecke Ag Maleinimid-derivate und deren verwendung als arzneimittel
EP0397060A2 (fr) 1989-05-05 1990-11-14 Gödecke Aktiengesellschaft Dérivés de maléinimide et leur utilisation comme médicament
DE4005969A1 (de) 1990-02-26 1991-08-29 Boehringer Mannheim Gmbh Neue trisubstituierte pyrrole, verfahren zu ihrer herstellung sowie arzneimittel, die diese verbindungen enthalten
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EP0470490A1 (fr) 1990-08-07 1992-02-12 F. Hoffmann-La Roche Ag Pyrroles substituées
EP0508792A1 (fr) 1991-04-11 1992-10-14 Schering Corporation Agents antitumoraux et antipsoriasis
EP0540956A1 (fr) 1991-11-04 1993-05-12 F. Hoffmann-La Roche Ag Procédé de fabrication de maléimides substitués
WO1993018766A1 (fr) 1992-03-20 1993-09-30 The Wellcome Foundation Limited Autres derives d'indole presentant une action antivirale
WO1993018765A1 (fr) 1992-03-20 1993-09-30 The Wellcome Foundation Limited Derives d'indole presentant une action antivirale
DE4217964A1 (de) 1992-05-30 1993-12-02 Goedecke Ag Indolocarbazol-Imide und deren Verwendung
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WO2000021927A2 (fr) 1998-10-08 2000-04-20 Smithkline Beecham Plc Procede et composes
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WO2003004472A1 (fr) 2001-07-05 2003-01-16 Astrazeneca Ab Nouveaux composes
CH695757A5 (de) * 2001-09-24 2006-08-31 Heinz Forster Pharmazeutische Zusammensetzung.
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WO2003082853A1 (fr) 2002-03-28 2003-10-09 Astrazeneca Ab Nouveaux composes
EP1739087A1 (fr) 2002-08-02 2007-01-03 Vertex Pharmaceuticals Incorporated Compositions comprenant des composés pyrazoles et leur utilisation comme inhibiteurs de gsk-3
US7595319B2 (en) 2002-12-17 2009-09-29 Astrazeneca Ab Compounds having selective inhibiting effect at GSK3
WO2005051392A1 (fr) 2003-11-20 2005-06-09 Children's Hospital Medical Center Inhibiteurs de gtpase et procedes d'utilisation correspondants
WO2006001754A1 (fr) 2004-06-24 2006-01-05 Astrazeneca Ab Nouveaux derives de 5-aryl-1h-pyrrolo [2, 3b] pyridine-3-carboxamide ou d'acide 5-aryl-1h-pyrrolo [2, 3b] pyridine-3-carboxylique
US20090041863A1 (en) 2004-09-17 2009-02-12 Hallahan Dennis E Use of GSK3 inhibitors in combination with radiation therapies
WO2007031878A2 (fr) 2005-07-27 2007-03-22 Exonhit Therapeutics Sa Methodes de traitement de troubles nerveux
WO2007016539A2 (fr) 2005-07-29 2007-02-08 Children's Hospital Medical Center Inhibiteurs de gtpase et methodes d'utilisation et structure cristalline de la gtpase rac-1
WO2007040438A2 (fr) 2005-10-03 2007-04-12 Astrazeneca Ab Derives d'imidazo(4,5-b) pyridine utilises comme inhibiteurs de la glycogene synthase kinase 3 pour le traitement de la demence et de troubles neurodegeneratifs
WO2007040440A1 (fr) 2005-10-03 2007-04-12 Astrazeneca Ab Nouveaux derives de pyrimidine et leur utilisation en therapie et pour la production d'un medicament pour la prevention et/ou le traitement de la maladie d'alzheimer
WO2007040436A1 (fr) 2005-10-03 2007-04-12 Astrazeneca Ab Utilisation de derives de pyrimidine dans la production d'un medicament pour la prevention et/ou le traitement de la maladie d'alzheimer
WO2007040439A1 (fr) 2005-10-03 2007-04-12 Astrazeneca Ab Nouveau composes ii
WO2008002244A2 (fr) 2006-06-27 2008-01-03 Astrazeneca Ab Nouveaux composés 384
WO2008002245A2 (fr) 2006-06-27 2008-01-03 Astrazeneca Ab Nouveaux composés 385
WO2008016994A2 (fr) * 2006-08-01 2008-02-07 Rush University Medical Center Exploitation de la signalisation wnt pour limiter la réplication du vih
WO2009007457A2 (fr) 2007-07-12 2009-01-15 Exonhit Therapeutics Sa Composés et procédés pour moduler les gtpases rho
US20090233993A1 (en) 2008-03-06 2009-09-17 Burnham Institute For Medical Research Compositions and methods for inhibiting gsk3 activity and uses thereof
EP2433636A1 (fr) 2010-09-27 2012-03-28 Medizinische Universität Wien Traitement de maladies malignes

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