Malattia Gene mutato Distrofia muscolare di Duchenne Distrofina
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Malattia Gene mutato Distrofia muscolare di Duchenne Distrofina
Malattia Gene mutato Distrofia muscolare di Duchenne (DMD) Distrofina Distrofia muscolare di Becker (BMD) Distrofina Distrofia muscolare di EmeryDreifuss Emerina, lamina A o lamina C Distrofia dei cingoli (LGMD) Piu' di 15 geni diversi autosomiche dominanti LGMD 1A: miotilina LGMD 1B: lamina A/C LGMD 1C: caveolina 3 ed altre autosomiche recessive LGMD 2A: calpaina-3 LGMD 2B: disferlina LGMD 2C: γ-sarcoglicano LGMD 2D: α-sarcoglicano LGMD 2E: β-sarcoglicano LGMD 2F: δ-sarcoglicano ed altre Distrofia facio-scapolo-omerale o di Non noto Lnadouzy-Dejerine (FSHD) Distrofia miotonica o malattia di Steinert (MMD) DMPK (DM1) e ZNF9 (DM2) Distrofia oculo-faringea (OPMD) Poly(A)-binding protein nuclear 1 (PABPN1) Distrofia muscolare distale (DD) Almeno 8 geni diversi (disferlina, titina, desmina ed altri) Distrofia muscolare congenita (CMD) Geni diversi (Laminina α2 – merosina, fukutina, collagene di tipo VI, integrina a7, ed altri) Challenges to gene therapy for DMD La DMD ha un decorso ingravescente e devastante (esaurimento delle cellule satelliti). Alla nascita, i bambini maschi affetti sembrano normali, ed i primi sintomi insorgono tra i 3 ed i 5 anni di vita sotto forma di blanda debolezza muscolare, che si manifesta con la difficolta' nel salire le scale, alzarsi nella posizione seduta o con l'incespicare di frequente. Con il passare del tempo, la muscolatura si indebolisce progressivamente. Solitamente entro i 10 anni di vita gli individui affetti sono costretti sulla sedia a rotelle, e molti decedono entro il 20 anno di eta'. Gene therapy requires delivery of a new gene to the vast majority of muscles in the body - a daunting challenge, since muscle tissues makes up >40% of body mass The dystrophyn mRNA is 14 kb in size. A delivery vector must be identify that can carry this expression cassette; alternatively, truncated version of the gene can be used Non esistono attualmente terapie per la malatia, se non quelle di supporto. Oltre al muscolo scheletrico, i pazienti con DMD mostrano un interessamento piu' o meno marcato del cuore che spesso evolve in una forma franca di cardiomiopatia dilatativa. Muscle transduction must not trigger toxic or immunological reactions that are harmful to the patient or that lead to further muscle damage Vectors for muscle gene therapy • Ad “gutless”: Ad vectors have relative large cloning capacity, can be grown at high titers and display relative efficient infection of muscle. However, traditional Ad vectors elicit a robust cellular immune response • AAV: AAV vectors are of great interest as they efficiently infect muscle and persist for years. New serotypes available • Plasmid DNA: displays a remarkable ability to transfer genes to muscle, specially if coupled with high pressure injection and/or electroporation The first clinical trial, closed in 2006, entailed the injection of a plasmid containing the whole dystrophin cDNA under the control of the CMV promoter into the radialis muscle of 9 DMD/BMD patients. However, dystrophin expression resulted too low and not homogenous. Different strategies can be used to increased transduction efficiency, including polymeres, ultrasounds (with microbubbles), and electroporation INFEZIONE PRODUTTIVA Agenti che inducono uno stress cellulare AAV Infezioni virali Adenovirus Herpesvirus Papillomavirus Taxonomy Agenti fisici Raggi gamma Raggi X UV Family: Parvovirus Subfamily: Parvovirinae Genus: Dependovirus Type: AAV 1-5 INFEZIONE LATENTE Metil-metan sulfonato Mitomicina c Cisplatino Idrossiurea Inibitori della topoisomerasi Inibitori delle proteasi Heat shock Agenti chimici Ad Replicazione del DNA virale Morphology Particles are icosahedral, non-enveloped, 18-26 nm diameter, 50% protein (VP1-3) 50% DNA. Resistant to inactivation by solvents, pH and heat. 19p13.3 19q13.2 19p13.2 19p13.1 19p12 19q12 19q13.31 19q13.32 19q13.33 19q13.41 Genome 19q13.1 19q13.42 Linear, non-segmented, ssDNA ~5 kb. AAVs package equal amounts of (+) and (-) strands. Produzione di nuove particelle virali e lisi della cellula AAVS1 19q13.2 19q13.3 19q13.43 19q13.4 Integrazione nel cromosoma 19q13.3 Xie et al. 2002 Therapeutic gene Rep-Cap Helper plasmid AAV vector Ad helper genes RBS’ C Rep binding site (RBS) 6 hrs CPE 293 cells 3’ 5’ B A CaPo4 transfection Terminal resolution site (trs) 5’ and 3’ Inverted Terminal Repeats have a predicted hammer-head like secondary structure During AAV replication Rep bind the ITR and cleaves one strand 48 hrs Freeze/Thaw Amm sulf fractionation rAAV CsCl gradient purification Collect and dialyze fractions Titration by QC-PCR Assay for transgene expression Xie et al. 2002 1. Based on a widely diffused, non pathogenic virus AAV Heart 2. Vectors retain less that 10% of the viral genome Tibialis anterior Ad 3. Vectors do not express viral proteins (not inflammatory and not immunogenic); permit long term persistence in vivo Diaphragm AAV-lacZ 3’ Skeletal muscle 4. Expression of the therapeutic gene can be driven by any desirable promoter 5. High titer vector preparations can be obtained by virion purification 6. Cells are transduced at high multiplicity of infection; mixing of different rAAV preparations results the simultaneous expression of gene combinations in vivo AAV-lacZ Heart wt AAV p5 TR p19 p46 Rep polyA Cap TR rAAV vector Therapeutic gene TR Neurons AAV-GFP Retina AAVLacO.14 Mre11 Merge AAVLacO.14 Rad50 Merge HU TR AAV-LacZ polyA Promoter AAVLacO.14 (14 8-mers, 112 LacO repeats) LacO (8-mer) HU 3’ HeLa LacR-EGFP HU 3’ Nbs1 Merge HU AAVLacO.14 Untreated (+) Merge (-) rAAV foci (+) DNA synthesis and/or +/- strand annealing HU (-) Inhibition of vector DNA processing Untreated AAVLacO.14 P-S343-Nbs1 Binding to cellular DDR proteins 1.5 Mre11 Rad50 Nbs1 1.0 0.5 0.0 NH H Efficient transduction Parvovirus Recettore AAV1 Acido sialico (legami α2-3-N e α2-6N) AAV2 Proteoglicani contenenti eparansolfati (HSPG) Corecettori: integrina αvβ5, FGFR1, HGF-R Sierotipo (in ordine di efficienza) AAV3 Proteoglicani contenenti eparansolfati (HSPG) Fegato AAV8, AAV9 AAV4 Acido sialico (legami α2-3-O) Muscolo scheletrico AAV5 Acido sialico (legami α2-3-O e α2-3N) Recettore del PDGF (PDGFR) AAV1, AAV7, AAV6, AAV8, AAV9, AAV2, AAV3 oso centrale Sistema nervo AAV5, AAV1, AAV4, AAV2 Acido sialico (legami α2-3-N e α2-6N) Occhio AAV5, AAV4, AAV1, AAV6 AAV6 http:// www.icgeb.org/ avu-corefacility.html Organo AAV7 Non noto AAV8 Recettore della laminina (LamR) Epitelio pigmentato Heart Liver Fotorecettori AAV5 AAV9 Non noto (LamR?) Polmone AAV5, AAV9 Parvovirus B19 Antigene P dei globuli rossi Cuore AAV9. AAV8 CPV (parvovirus canino) Recettore della trasferrina Acido sialico (acido N-glicolilneuraminico, NeuGC) Pancreas AAV8 Rene AAV2 FPV (parvovirus della panleucopenia felina) Recettore della trasferrina Tibialis anterior Diaphragm Helper Plasmids Neurons, Muscle The AVU produces, purifies, titers and characterizes research-grade recombinant AAV vectors Rep Cap1 Ad (E2A, VA, E4) Neurons, Muscle Cap2 Muscle Cap3 Neurons Cap4 Lung, Heart Cap5 Both rAAV2 or hybrid vectors pseudotyped with capsid of serotypes from 1 to 9 are reproducibility obtained at a sterility and purity grade suitable for in vitro and animal experimentation Endothelium, Muscle Cap6 or Muscle Rep Cap7 Ad (E2A, VA, E4) Liver, Heart Cap8 Rep5 CapBAV Ad (E2A, VA, E4) http:// www.icgeb.org/ avu-corefacility.html Angiogenesis &Endothelial function huVEGF-A165 huVEGF-A165 (Tet-ON) huVEGF-A165-HA huVEGF-A121 muVEGF-A164 muVEGF-A120 huVEGF-D full length huVEGF-D processed huVEGF-B VEGF/FGF4 Angiopoietin 1 Semaphorin 3A PlGF PDGF-B TRAIL HIF-1α-VP16 Netrin1 Development &Regeneration Islet-1 Msx-1 Notch ICD Cripto c-Myc Klf4 Oct3/4 Sox2 Cardiac &muscle function IGF-1 Melusin ZASP1 Ghrelin Cytokines &Chemokines RANTES Interleukin 1β Interleukin 1β NG RGMa MCP-1 MIP-1a PET Imaging HSV-1 TK HSV-1 TKsl39 HIV-1 Tat-HSV-1 TK HIV-1 Tat-HSV-1 TKSL39 HIV-1 HIV-1 Tat HIV-1 Tat-SP Apoptosis Bcl-2 shRNAs FLK1 Zacfu6/hairpin Sh-Amb1 Sh-Amb2 ZacU6 GFP Inflammation IκB-α Antibodies ScFv-D18 (anti-Prp) ScFv-TG (anti-TG) Immune function CTLA-4 ADAMTS13 Extracellular matrix Timp-1 Pentraxin-3 Cell cycle &Cancer p27* Ras Mutated Ras cMyc HPV E7 Reporters LacO binding site repeats LacZ GFP GFP (Tet-ON) HPV E6 E7 Others Cre-GFP CFTR-YFP DCN ErB4DCF NRG1IIIb3 Calpain1 Calpain2 PA3 PE8 Cap-YFP Medical Condition Cancer Disease Gene Route Phase Status PI Prostate cancer GM-CSF Ex vivo, intradermal I-III 4 Open/2 Completed Gillison ML, Drake C, Corman JM, Curti B, Urba WJ Dummer R Melanoma B7-2, IL-12 Ex vivo, intradermal I 1 Open Cardiovascular Heart failure SERCA-2a Intracoronary I 2 Open London B, Jessup M Infectious diseases HIV-1 vaccination HIV-1 gag-pro-prt Intramuscular I 2 Open Clumeck N, van Lunzen J Monogenic diseases Lipoprotein Lipase deficiency Lipoprotein Lipase S447X Intramuscular I-II 1 Open Stroes E Leber amaurosis RPE65 Intraocular I 2 Open Byrne B, Jacobson S, Maguirre A Hemophilia B FIX Intramuscular/Liver I 2 Completed/1 Under review Manno C, Glader B, Nienhuis A Cystic fibrosis CFTR Intranasal, Intrapulmonary I-II 6 Completed Gardner P, Aitken M Limb girdle distrophy Sarcoglycan Intramuscular I 8 Open/2 Completed Mendell J Duchenne muscular Dystrophy Minidystrophin Intramuscular I 1 Open Mendell J alpha1-antitrypsin deficiency AAT Intramuscular I 2 Open Flotte T Parkinson disease GAD, AADC-2, Neurturin Intracranial I-II 2 Open/ 1 Completed Marks W, Verhagen L Alzheimer disease NGF Intracranial I-II 1 Completed Bennett D Intractable epilepsy NPY Intracranial I 1 Open During M Canavan disease Aspartocyclase Intracranial I 1 Open/ 2 Completed Seashore MR, Freeze A, Leone P Late infantile neuronal ceroid lipofuscinosis Tripeptydil peptidase Intracranial I 1 Open Crystal R Amyotrophic Lateral Sclerosis EAAT2 Intracranial I 1 Under review During M Rheumatoid arthritis TNFR:Fc Intra-articular I 2 Open Mease P hpAP Intranasal/ Intrabronchial I 2 Open Aitken M Neurological diseases Others Gene marking minidistrofine (~6-7 kb) e microdistrofine (~4 kb) Queste versioni ridotte della distrofina presentano delezioni comuni della regione centrale a bastoncello e nel dominio C-terminale della proteina parentale, lasciando intatti i domini funzionali essenziali della proteina, in particolare quello ricco in cisteine (CR) Genetically engineered metabolic factory to treat genetic diseases Gene transfer by AAV, Ad, LV, DNA vectors Lung Liver Ectopic production of genetically engineered protein products (Factor IX, Lysosomal enzymes, AAT-1, Epo, ecc) Delivery into the circulation Hemophilia • Affects 1:5,000 males – 80% hemophilia A due to Factor VIII deficiency – 20% hemophilia B due to Factor IX deficiency • Results in spontaneous bleeding, which can be fatal • Treated with prophylactic or therapeutic infusion of the deficient factor • Correction to 1% of normal activity would reduce spontaneous bleeding • Correction to 10% of normal activity would eliminate most spontaneous bleeding Muscle Historic Overview on Hemophilia Therapy Gene Therapy Approaches for Hemophilia: Replacement therapy: blood transfusion since ‘70s Recombinant FVIII/FIX infusion since ‘90s • Liver-directed • Muscle-directed Gene Therapy Approaches for Hemophilia: • • • • • Existence of small (KO mice) and large (dog) animal models Easy assessment of efficacy (coagulation tests) Small correction should be sufficient (1%) Liver-directed, Muscle-directed Expensive therapy available • Bone marrow-directed • Transplantation of genetically-modified fibroblasts Transplantation of genetically-modified Fibroblasts 1, 2, 5 - FVIII (>8 kb) 3, 4 - FIX (1.4 kb) working only after hepatectomy (in animals so far) Gutless vectors? One patient so far. At 7 days: persistent elevation of transaminases = low therapeutic index No additional patients enrolled Blood, 2004 Intra-portal injection Tail vein injection M. Kay, K. High Phase I Trial: 8 adult men with severe hemophilia B (<1% baseline F.IX) F.IX expression close to the site of injection up to 10 months after treatment; no evidence for inflammation Circulating levels of F.IX were less than what is required for therapeutic effect Lethal autosomal recessive disease 70 000 individuals affected worldwide; 1 in 3000 Caucasian births High morbidity and mortality F.IX activity assay and transaminase levels (AST, ALT) plotted as a function of time in weeks after vector administration in subjects E, F and G CF Lung The cystic fibrosis transmembrane conductance regulator (CFTR) Normal Lung Airway gene transfer Adenovirus In the absence of epithelial damage inefficient gene transfer in CF patients Cellular and humoral immune responses against the virus Adeno-associated virus Several trials carried out in the nose, sinus and single lobes of CF patients (Vector from Targeted Genetics Corp). Evidence of safety and limited efficacy Repeated administrations feasible Gene cloned in 1989 Natural variant serotypes more effective First GT clinical trial in 1993 Nonviral gene transfer Lipid-plasmid complexes w/wo chemical modifications Offers several advantages over viral methods but are still less efficient Delivery of gene transfer vectors to lung: physical barriers and innate immune responses CF: gene therapy experience >30 Clinical trial protocols, most of which completed Strategies to enhance gene transfer to airway epithelia 1 Vector delivered from the basolateral surface 2 Transient tight junctions disruption 3 Modification of the apical membrane 4 New formulation and delivery methods 5 Engineered or natural vectors with improved binding and entry properties 1 Mucus 2 Glycocalyx 3 Cilia 4 Macrophages 5 Humoral immune responses Using the lung as a metabolic factory for secretion of therapeutic proteins into the circulation Factors limiting the duration of transgene expression in airway epithelia 1 Promoter shut-off 2 Loss of transgene from cells: particular problem for nonviral vectors 3 Bacterial DNA contained in plasmid vectors can generate an inflammatory response 4 Immune response against viral vector or transgene 5 Limited life-span of differentiated airway cells Vector administration to the lung might target the conducting airway epithelium, the alveolar epithelium, or both. Secretion of protein products from the basolateral membrane of epithelial cells must diffuse through the interstitium (composed of fibroblasts and connective tissue) and across vascular endothelial cells, to be delivered into the blood (as marked by arrows). The alveolar epithelia of the lung, which contain a prominent population of Type I pneumocytes, are in close proximity to the lung capillary network, making them ideal gene therapy targets for systemic delivery of proteins.