Expression of recombinant human acetylcholinesterase in transgenic tomato plants

Mor, Tsafrir S.; Sternfeld, M.; Soreq, Hermona; Arntzen, Charles J.; Mason, Hugh S.

doi:10.1002/bit.10012

Cited by 58 publications

(63 citation statements)

References 44 publications

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“…Transgenic plants have been proposed as a means to economically produce proteins such as antibodies, vaccines, and enzymes (Mor et al, 2001;Peterson and Arntzen, 2004;Twyman et al, 2003;Witcher et al, 1998). In particular, there is a projected shortage in manufacturing capacity for therapeutic antibodies that perhaps plant biotechnology can help alleviate (Peterson and Arntzen, 2004).…”

Section: Introductionmentioning

confidence: 96%

High‐level transient expression of recombinant protein in lettuce

Joh

Wróblewski

Ewing

et al. 2005

Biotech & Bioengineering

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Transient expression following agroinfiltration of plant tissue was investigated as a system for producing recombinant protein. As a model system, Agrobacterium tumefaciens containing the beta-glucuronidase (GUS) gene was vacuum infiltrated into lettuce leaf disks. Infiltration with a suspension of 10(9) colony forming units/mL followed by incubation for 72 h at 22 degrees C in continuous darkness produced a maximum of 0.16% GUS protein based on dry tissue or 1.1% GUS protein based on total soluble protein. This compares favorably to expression levels for commercially manufactured GUS protein from transgenic corn seeds. A. tumefaciens culture medium pH between 5.6 and 7.0 and surfactant concentrations < or = 100 ppm in the vacuum infiltration did not affect GUS expression, while infiltration with an A. tumefaciens density of 10(7) and 10(8) colony forming units/mL, incubation at 29 degrees C, and a surfactant concentration of 1,000 ppm significantly reduced expression. Incubation in continuous light caused lettuce to produce GUS protein more rapidly, but final levels did not exceed the GUS production in leaves incubated in continuous darkness after 72 h at 22 degrees C. The kinetics of GUS expression during incubation in continuous light and dark were represented well using a logistic model, with rate constants of 0.30 and 0.29/h, respectively. To semi-quantitatively measure the GUS expression in large numbers of leaf disks, a photometric enhancement of the standard histochemical staining method was developed. A linear relationship with an R2 value of 0.90 was determined between log10 (% leaf darkness) versus log10 (GUS activity). Although variability in expression level was observed, agroinfiltration appears to be a promising technology that could potentially be scaled up to produce high-value recombinant proteins in planta.

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Section: Introductionmentioning

confidence: 96%

High‐level transient expression of recombinant protein in lettuce

Joh

Wróblewski

Ewing

et al. 2005

Biotech & Bioengineering

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“…Bu amaçla insan asetilkolinesteraz enzimi rekombinant hücre kültürü teknikleri kullanılarak insan embriyonik böbrek hücreleri (HEK293), Escherichia coli ve bitkilerde eksprese edilmiştir [22][23][24][25][26]. Ancak deney hayvanlarında yapılan farmokokinetik çalışmalar ister memeli hücresinde ister bakteride eksprese edilmiş olsun dolaşımdaki yarı ömrünün çok kısa olduğunu göstermiştir [22,23].…”

Section: Yüksek Miktarlarda Ache üRetimi Ve Yarı öMür Problemiunclassified

Usage potential of acetylcholinesterase as a bioscavenger in organophasphate poisoning

Küçükkılınç¹

2014

Turk J Bioch

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“…In plants, as in any other eukaryotic organism, cotranslational transport of the peptide into the ER is facilitated by a short N-terminal signal peptide which is subsequently cleaved. Mammalian signal peptides are also functional in plants and could guide proteins to the plant ER, as it was shown for erythropoietin (Matsumoto et al, 1995) and human acetylcholine esterase (Mor et al, 2001). For recombinant proteins, usually a genuine plant SP is translationally fused to the protein of interest to allow efficient ER-localization.…”

Section: The Secretory Pathway and Proteolytic Cleavagementioning

confidence: 99%

Biopharmaceuticals from Plants: A Multitude of Options for Posttranslational Modifications

Warzecha

2008

Biotechnology and Genetic Engineering Reviews

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In 1982 the first recombinant therapeutic, human insulin, was introduced into the market and started a new branch of pharmaceutical development, manufacture, and therapy options. To date, more than 130 recombinant protein therapeutics have been approved by the US Food and Drug Administration (FDA) and many more are being developed world wide. With the increasing number of protein therapeutics the number of potential production organisms is also expanding, and posttranslational modification of proteins has become a topic of special focus. One major difference between smallmolecule drugs and protein therapeutics is that the latter are reliant on a host organism for their production and this can have a large influence on the final structure and can ultimately affect the pharmacokinetics, immunogenicity, and the function of the protein depending on the production process. Plants can be efficiently used as production systems for recombinant proteins thereby offering a variety of options for transgene targeting and modification. This review is intended to give an overview about the potential of plants to serve as a production system for therapeutic and prophylactic biopharmaceuticals with respect to posttranslational modifications.

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Expression of recombinant human acetylcholinesterase in transgenic tomato plants

Cited by 58 publications

References 44 publications

High‐level transient expression of recombinant protein in lettuce

High‐level transient expression of recombinant protein in lettuce

Usage potential of acetylcholinesterase as a bioscavenger in organophasphate poisoning

Biopharmaceuticals from Plants: A Multitude of Options for Posttranslational Modifications

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