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  1. AU="Fletcher Samuel P"
  2. AU="Amici, Carla"
  3. AU=Chubb S A Paul
  4. AU="Hindi, Yousef"
  5. AU="Aljohani, Eman"
  6. AU=Jun Seah Ivan Yu
  7. AU="Pickavance, Georgia C"
  8. AU="Howard, Brittany L"
  9. AU="de Sousa Alves Neri, Julianna Lys"
  10. AU="Elizabeth Noble"
  11. AU="Nicole Shaver"
  12. AU=Siegel Vivian
  13. AU="Calméjane, Louis"
  14. AU="Lombardi, S."
  15. AU="Hartmann, H"
  16. AU="Furuya Junior, Carlos Kyoshi"
  17. AU="Bo, L J"
  18. AU="Baxter, J"
  19. AU="Liu, Zhenhong"
  20. AU="Xiaochun Deng"
  21. AU="Anderson, Ciorsdan"
  22. AU="Xiaofang Zhang"
  23. AU=Stincarelli Maria Alfreda AU=Stincarelli Maria Alfreda
  24. AU="McNabb, Warren C."
  25. AU="Seker, Demet"
  26. AU="Braman, Sidney S"
  27. AU="Yerke, Lisa"
  28. AU="Antonella Lettieri"
  29. AU="Valdiviezo, Jesús"

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  1. Artikel: Optimization of recombinant protein expression in the chloroplasts of green algae.

    Fletcher, Samuel P / Muto, Machiko / Mayfield, Stephen P

    Advances in experimental medicine and biology

    2007  Band 616, Seite(n) 90–98

    Abstract: Through advances in molecular and genetic techniques, protein expression in the chloroplasts of green algae has been optimized for high-level expression. Recombinant proteins expressed in algae have the potential to provide novel and safe treatment of ... ...

    Abstract Through advances in molecular and genetic techniques, protein expression in the chloroplasts of green algae has been optimized for high-level expression. Recombinant proteins expressed in algae have the potential to provide novel and safe treatment of disease and infection where current, high-cost drugs are the only option, or worse, where therapeutic drugs are not available due to their prohibitively high-cost to manufacture. Optimization of recombinant protein expression in Chlamydomonas reinhardtii chloroplasts has been accomplished by employing chloroplast codon bias and combinatorial examination of promoter and UTR combinations. In addition, as displayed by the expression of an anti-herpes antibody, the C. reinhardtii chloroplast is capable of correctly folding and assembling complex mammalian proteins. These data establish algal chloroplasts as a system for the production of complex human therapeutic proteins in soluble and active form, and at significantly reduced time and cost compared to existing production systems. Production of recombinant proteins in algal chloroplasts may enable further development of safe, efficacious and cost-effective protein therapeutics.
    Mesh-Begriff(e) Animals ; Chlamydomonas reinhardtii/physiology ; Chloroplasts/genetics ; Chloroplasts/metabolism ; Gene Expression Regulation ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism
    Chemische Substanzen Recombinant Proteins
    Sprache Englisch
    Erscheinungsdatum 2007
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ISSN 2214-8019 ; 0065-2598
    ISSN (online) 2214-8019
    ISSN 0065-2598
    DOI 10.1007/978-0-387-75532-8_8
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Translational control of recombinant human acetylcholinesterase accumulation in plants

    Geyer Brian C / Fletcher Samuel P / Griffin Tagan A / Lopker Michael J / Soreq Hermona / Mor Tsafrir S

    BMC Biotechnology, Vol 7, Iss 1, p

    2007  Band 27

    Abstract: Abstract Background Codon usage differences are known to regulate the levels of gene expression in a species-specific manner, with the primary factors often cited to be mRNA processing and accumulation. We have challenged this conclusion by expressing ... ...

    Abstract Abstract Background Codon usage differences are known to regulate the levels of gene expression in a species-specific manner, with the primary factors often cited to be mRNA processing and accumulation. We have challenged this conclusion by expressing the human acetylcholinesterase coding sequence in transgenic plants in its native GC-rich sequence and compared to a matched sequence with (dicotyledonous) plant-optimized codon usage and a lower GC content. Results We demonstrate a 5 to 10 fold increase in accumulation levels of the "synaptic" splice variant of human acetylcholinesterase in Nicotiana benthamiana plants expressing the optimized gene as compared to the native human sequence. Both transient expression assays and stable transformants demonstrated conspicuously increased accumulation levels. Importantly, we find that the increase is not a result of increased levels of acetylcholinesterase mRNA, but rather its facilitated translation, possibly due to the reduced energy required to unfold the sequence-optimized mRNA. Conclusion Our findings demonstrate that codon usage differences may regulate gene expression at different levels and anticipate translational control of acetylcholinesterase gene expression in its native mammalian host as well.
    Schlagwörter Biotechnology ; TP248.13-248.65 ; Chemical technology ; TP1-1185 ; Technology ; T ; DOAJ:Biotechnology ; DOAJ:Life Sciences ; DOAJ:Biology and Life Sciences
    Thema/Rubrik (Code) 580
    Sprache Englisch
    Erscheinungsdatum 2007-05-01T00:00:00Z
    Verlag BioMed Central
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  3. Artikel ; Online: Translational control of recombinant human acetylcholinesterase accumulation in plants.

    Geyer, Brian C / Fletcher, Samuel P / Griffin, Tagan A / Lopker, Michael J / Soreq, Hermona / Mor, Tsafrir S

    BMC biotechnology

    2007  Band 7, Seite(n) 27

    Abstract: Background: Codon usage differences are known to regulate the levels of gene expression in a species-specific manner, with the primary factors often cited to be mRNA processing and accumulation. We have challenged this conclusion by expressing the human ...

    Abstract Background: Codon usage differences are known to regulate the levels of gene expression in a species-specific manner, with the primary factors often cited to be mRNA processing and accumulation. We have challenged this conclusion by expressing the human acetylcholinesterase coding sequence in transgenic plants in its native GC-rich sequence and compared to a matched sequence with (dicotyledonous) plant-optimized codon usage and a lower GC content.
    Results: We demonstrate a 5 to 10 fold increase in accumulation levels of the "synaptic" splice variant of human acetylcholinesterase in Nicotiana benthamiana plants expressing the optimized gene as compared to the native human sequence. Both transient expression assays and stable transformants demonstrated conspicuously increased accumulation levels. Importantly, we find that the increase is not a result of increased levels of acetylcholinesterase mRNA, but rather its facilitated translation, possibly due to the reduced energy required to unfold the sequence-optimized mRNA.
    Conclusion: Our findings demonstrate that codon usage differences may regulate gene expression at different levels and anticipate translational control of acetylcholinesterase gene expression in its native mammalian host as well.
    Mesh-Begriff(e) Acetylcholinesterase/biosynthesis ; Acetylcholinesterase/genetics ; Base Composition ; Codon/genetics ; Genetic Enhancement/methods ; Humans ; Plants, Genetically Modified/metabolism ; Protein Biosynthesis/genetics ; Protein Engineering/methods ; Nicotiana/enzymology ; Nicotiana/genetics
    Chemische Substanzen Codon ; Acetylcholinesterase (EC 3.1.1.7)
    Sprache Englisch
    Erscheinungsdatum 2007-05-30
    Erscheinungsland England
    Dokumenttyp Evaluation Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2052746-9
    ISSN 1472-6750 ; 1472-6750
    ISSN (online) 1472-6750
    ISSN 1472-6750
    DOI 10.1186/1472-6750-7-27
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel ; Online: Plant-derived human acetylcholinesterase-R provides protection from lethal organophosphate poisoning and its chronic aftermath.

    Evron, Tama / Geyer, Brian C / Cherni, Irene / Muralidharan, Mrinalini / Kilbourne, Jacquelyn / Fletcher, Samuel P / Soreq, Hermona / Mor, Tsafrir S

    FASEB journal : official publication of the Federation of American Societies for Experimental Biology

    2007  Band 21, Heft 11, Seite(n) 2961–2969

    Abstract: Therapeutically valuable proteins are often rare and/or unstable in their natural context, calling for production solutions in heterologous systems. A relevant example is that of the stress-induced, normally rare, and naturally unstable "read-through" ... ...

    Abstract Therapeutically valuable proteins are often rare and/or unstable in their natural context, calling for production solutions in heterologous systems. A relevant example is that of the stress-induced, normally rare, and naturally unstable "read-through" human acetylcholinesterase variant, AChE-R. AChE-R shares its active site with the synaptic AChE-S variant, which is the target of poisonous organophosphate anticholinesterase insecticides such as the parathion metabolite paraoxon. Inherent AChE-R overproduction under organophosphate intoxication confers both short-term protection (as a bioscavenger) and long-term neuromuscular damages (as a regulator). Here we report the purification, characterization, and testing of human, endoplasmic reticulum-retained AChE-R(ER) produced from plant-optimized cDNA in Nicotiana benthamiana plants. AChE-R(ER) purified to homogeneity showed indistinguishable biochemical properties, with IC50 = 10(-7) M for the organophosphate paraoxon, similar to mammalian cell culture-derived AChE. In vivo titration showed dose-dependent protection by intravenously injected AChE-R(ER) of FVB/N male mice challenged with a lethal dose of paraoxon, with complete elimination of short-term clinical symptoms at near molar equivalence. By 10 days postexposure, AChE-R prophylaxis markedly limited postexposure increases in plasma murine AChE-R levels while minimizing the organophosphate-induced neuromuscular junction dismorphology. Our findings present plant-produced AChE-R(ER) as a bimodal agent, conferring both short- and long-term protection from organophosphate intoxication.
    Mesh-Begriff(e) Acetylcholinesterase/genetics ; Acetylcholinesterase/isolation & purification ; Acetylcholinesterase/metabolism ; Animals ; Binding Sites/drug effects ; Humans ; Insecticides/toxicity ; Lethal Dose 50 ; Male ; Mice ; Muscle, Skeletal/drug effects ; Neuromuscular Junction/drug effects ; Neuromuscular Junction/metabolism ; Organophosphorus Compounds/toxicity ; Paraoxon/toxicity ; Plants, Genetically Modified ; Polyethylene Glycols/chemistry ; Recombinant Proteins/metabolism ; Survival Rate ; Tissue Distribution/drug effects ; Nicotiana/genetics
    Chemische Substanzen Insecticides ; Organophosphorus Compounds ; Recombinant Proteins ; Polyethylene Glycols (3WJQ0SDW1A) ; Acetylcholinesterase (EC 3.1.1.7) ; Paraoxon (Q9CX8P80JW)
    Sprache Englisch
    Erscheinungsdatum 2007-05-02
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 639186-2
    ISSN 1530-6860 ; 0892-6638
    ISSN (online) 1530-6860
    ISSN 0892-6638
    DOI 10.1096/fj.07-8112com
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel: Plant-derived human acetylcholinesterase-R provides protection from lethal organophosphate poisoning and its chronic aftermath

    Evron, Tama / Geyer, Brian C / Cherni, Irene / Muralidharan, Mrinalini / Kilbourne, Jacquelyn / Fletcher, Samuel P / Soreq, Hermona / Mor, Tsafrir S

    FASEB journal. 2007 Sept., v. 21, no. 11

    2007  

    Abstract: Therapeutically valuable proteins are often rare and/or unstable in their natural context, calling for production solutions in heterologous systems. A relevant example is that of the stress-induced, normally rare, and naturally unstable "read-through" ... ...

    Abstract Therapeutically valuable proteins are often rare and/or unstable in their natural context, calling for production solutions in heterologous systems. A relevant example is that of the stress-induced, normally rare, and naturally unstable "read-through" human acetylcholinesterase variant, AChE-R. AChE-R shares its active site with the synaptic AChE-S variant, which is the target of poisonous organophosphate anticholinesterase insecticides such as the parathion metabolite paraoxon. Inherent AChE-R overproduction under organophosphate intoxication confers both short-term protection (as a bioscavenger) and long-term neuromuscular damages (as a regulator). Here we report the purification, characterization, and testing of human, endoplasmic reticulum-retained AChE-RER produced from plant-optimized cDNA in Nicotiana benthamiana plants. AChE-RER purified to homogeneity showed indistinguishable biochemical properties, with IC₅₀ = 10⁻⁷ M for the organophosphate paraoxon, similar to mammalian cell culture-derived AChE. In vivo titration showed dose-dependent protection by intravenously injected AChE-RER of FVB/N male mice challenged with a lethal dose of paraoxon, with complete elimination of short-term clinical symptoms at near molar equivalence. By 10 days postexposure, AChE-R prophylaxis markedly limited postexposure increases in plasma murine AChE-R levels while minimizing the organophosphate-induced neuromuscular junction dismorphology. Our findings present plant-produced AChE-RER as a bimodal agent, conferring both short- and long-term protection from organophosphate intoxication.--Evron, T., Geyer, B. C., Cherni, I., Muralidharan, M., Kilbourne, J., Fletcher, S. P., Soreq, H., Mor, T. S. Plant-derived human acetylcholinesterase-R provides protection from lethal organophosphate poisoning and its chronic aftermath.
    Sprache Englisch
    Erscheinungsverlauf 2007-09
    Umfang p. 2961-2969.
    Erscheinungsort The Federation of American Societies for Experimental Biology
    Dokumenttyp Artikel
    ZDB-ID 639186-2
    ISSN 1530-6860 ; 0892-6638
    ISSN (online) 1530-6860
    ISSN 0892-6638
    Datenquelle NAL Katalog (AGRICOLA)

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  6. Artikel: Purification of transgenic plant-derived recombinant human acetylcholinesterase-R.

    Geyer, Brian C / Muralidharan, Mrinalini / Cherni, Irene / Doran, Jeffrey / Fletcher, Samuel P / Evron, Tama / Soreq, Hermona / Mor, Tsafrir S

    Chemico-biological interactions

    2005  Band 157-158, Seite(n) 331–334

    Abstract: Nicotiana benthamiana plants were engineered to express a codon-optimized gene encoding the human acetylcholinesterase-R (AChE) isoform. The transgenic plants expressed the protein at >0.4% of total soluble protein, and the plant-produced enzyme was ... ...

    Abstract Nicotiana benthamiana plants were engineered to express a codon-optimized gene encoding the human acetylcholinesterase-R (AChE) isoform. The transgenic plants expressed the protein at >0.4% of total soluble protein, and the plant-produced enzyme was purified to homogeneity. Following lysis, procainamide affinity chromatography and anion-exchange chromatography, more than 400-fold purification was achieved and electrophoretic purity was obtained. This pure protein is kinetically indistinguishable from the only commercially available source of human acetylcholinesterase, which is produced in mammalian cell culture. Thus, we have demonstrated a model system for the production of acetylcholinesterase, which is not susceptible to the quantitative limitations or mammalian pathogens associated with purification from mammalian cell culture or human serum.
    Mesh-Begriff(e) Acetylcholinesterase/biosynthesis ; Acetylcholinesterase/genetics ; Acetylcholinesterase/isolation & purification ; Acetylcholinesterase/metabolism ; Cell Line ; Electrophoresis, Polyacrylamide Gel ; Humans ; Kinetics ; Plants, Genetically Modified ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Nicotiana/genetics ; Tobacco Mosaic Virus/genetics
    Chemische Substanzen Recombinant Proteins ; Acetylcholinesterase (EC 3.1.1.7)
    Sprache Englisch
    Erscheinungsdatum 2005-11-02
    Erscheinungsland Ireland
    Dokumenttyp Journal Article
    ZDB-ID 218799-1
    ISSN 1872-7786 ; 0009-2797
    ISSN (online) 1872-7786
    ISSN 0009-2797
    DOI 10.1016/j.cbi.2005.10.097
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  7. Artikel: Tissue distribution of cholinesterases and anticholinesterases in native and transgenic tomato plants.

    Fletcher, Samuel P / Geyer, Brian C / Smith, Amy / Evron, Tama / Joshi, Lokesh / Soreq, Hermona / Mor, Tsafrir S

    Plant molecular biology

    2004  Band 55, Heft 1, Seite(n) 33–43

    Abstract: Acetylcholinesterase, a major component of the central and peripheral nervous systems, is ubiquitous among multicellular animals, where its main function is to terminate synaptic transmission by hydrolyzing the neurotransmitter, acetylcholine. However, ... ...

    Abstract Acetylcholinesterase, a major component of the central and peripheral nervous systems, is ubiquitous among multicellular animals, where its main function is to terminate synaptic transmission by hydrolyzing the neurotransmitter, acetylcholine. However, previous reports describe cholinesterase activities in several plant species and we present data for its presence in tomato plants. Ectopic expression of a recombinant form of the human enzyme and the expression pattern of the transgene and the accumulation of its product in transgenic tomato plants are described. Levels of acetylcholinesterase activity in different tissues are closely effected by and can be separated from alpha-tomatine, an anticholinesterase steroidal glycoalkaloid. The recombinant enzyme can also be separated from the endogenous cholinesterase activity by its subcellular localization and distinct biochemical properties. Our results provide evidence for the co-existence in tomato plants of both acetylcholinesterase activity and a steroidal glycoalkaloid with anticholinesterase activity and suggest spatial mutual exclusivity of these antagonistic activities. Potential functions, including roles in plant-pathogen interactions are discussed.
    Mesh-Begriff(e) Acetylcholinesterase/genetics ; Acetylcholinesterase/metabolism ; Catalysis ; Cholinesterase Inhibitors/metabolism ; Cholinesterases/genetics ; Cholinesterases/metabolism ; Gene Expression Regulation, Enzymologic ; Humans ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Lycopersicon esculentum/genetics ; Lycopersicon esculentum/metabolism ; Plant Roots/enzymology ; Plant Roots/genetics ; Plants, Genetically Modified/genetics ; Plants, Genetically Modified/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Tomatine/metabolism ; Transgenes/genetics
    Chemische Substanzen Cholinesterase Inhibitors ; Isoenzymes ; Recombinant Proteins ; Tomatine (31U6547O08) ; Acetylcholinesterase (EC 3.1.1.7) ; Cholinesterases (EC 3.1.1.8)
    Sprache Englisch
    Erscheinungsdatum 2004-05
    Erscheinungsland Netherlands
    Dokumenttyp Comparative Study ; Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 778032-1
    ISSN 1573-5028 ; 0167-4412
    ISSN (online) 1573-5028
    ISSN 0167-4412
    DOI 10.1007/s11103-004-0394-9
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