Taliglucerase alfa: An enzyme replacement therapy using plant cell expression technology

Grabowski, Gregory A.; Golembo, Myriam; Shaaltiel, Yoseph

doi:10.1016/j.ymgme.2014.02.011

Cited by 123 publications

(65 citation statements)

References 43 publications

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“…Taliglucerase alfa is the first FDA‐approved plant cell‐expressed human recombinant therapeutic protein 6 and is indicated for treatment of adults with type 1 GD in the United States, Israel, Brazil, Australia, Canada, Chile, and other countries; it is also approved for treatment of children in the United States, Australia, Canada, Israel, Mexico, and other countries, and for hematologic manifestations in pediatric patients with type 3 GD in Canada. The taliglucerase alfa production system offers the ability for rapid scale‐up and is not susceptible to contamination with mammalian pathogens 7. The current report expands the database of the long‐term safety and efficacy of taliglucerase alfa in patients who have been previously treated with imiglucerase.…”

Section: Introductionmentioning

confidence: 84%

Enzyme replacement therapy with taliglucerase alfa: 36‐month safety and efficacy results in adult patients with Gaucher disease previously treated with imiglucerase

Pastores

Shankar

Petakov³

et al. 2016

American J Hematol

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Taliglucerase alfa is the first available plant cell‐expressed human recombinant therapeutic protein. It is indicated for treatment of patients with type 1 Gaucher disease (GD) in adult and pediatric patients in several countries. Study PB‐06‐002 examined the safety and efficacy of taliglucerase alfa for 9 months in patients who previously received imiglucerase. The results of adult patients from Study PB‐06‐002 who continued receiving taliglucerase alfa in extension Study PB‐06‐003 for up to 36 months are reported here. Eighteen patients received at least one dose of taliglucerase alfa in Study PB‐06‐003; 10 patients completed 36 total months of therapy, and four patients who transitioned to commercial drug completed 30–33 months of treatment. In patients who completed 36 total months of treatment, mean percent (±standard error) changes from baseline/time of switch to taliglucerase alfa to 36 months were as follows: hemoglobin concentration, −1.0% (±1.9%; n = 10); platelet count, +9.3% (±9.8%; n = 10); spleen volume measured in multiples of normal (MN), −19.8% (±9.9%; n = 7); liver volume measured in MN, +0.9% (±5.4%; n = 8); chitotriosidase activity, −51.5% (±8.1%; n = 10); and CCL18 concentration, −36.5 (±8.0%; n = 10). Four patients developed antidrug antibodies, including one with evidence of neutralizing activity in vitro. All treatment‐related adverse events were mild or moderate and transient. The 36‐month results of switching from imiglucerase to taliglucerase alfa treatment in adults with GD provide further data on the clinical safety and efficacy of taliglucerase alfa beyond the initial 9 months of the original study. www.clinicaltrials.gov identifier NCT00705939. Am. J. Hematol. 91:661–665, 2016. © 2016 Wiley Periodicals, Inc.

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Section: Introductionmentioning

confidence: 84%

Enzyme replacement therapy with taliglucerase alfa: 36‐month safety and efficacy results in adult patients with Gaucher disease previously treated with imiglucerase

Pastores

Shankar

Petakov³

et al. 2016

American J Hematol

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“…Recently, the first plant-produced recombinant biopharmaceutical, a recombinant human glucocerebrosidase, has been approved for enzyme replacement therapy in humans and is commercially available in the United States (Grabowski et al, 2014). Many biopharmaceutical proteins like human immunoglobulins or hormones are glycosylated and the composition of the glycans very often affect protein–protein interactions leading to altered efficacies of the recombinant drugs or unwanted side-effects like fast clearance from the blood or increased immunogenicity.…”

Section: Implications For Plant Biotechnologymentioning

confidence: 99%

Biological significance of complex N-glycans in plants and their impact on plant physiology

Strasser

2014

Front. Plant Sci.

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Asparagine (N)-linked protein glycosylation is a ubiquitous co- and post-translational modification which can alter the biological function of proteins and consequently affects the development, growth, and physiology of organisms. Despite an increasing knowledge of N-glycan biosynthesis and processing, we still understand very little about the biological function of individual N-glycan structures in plants. In particular, the N-glycan-processing steps mediated by Golgi-resident enzymes create a structurally diverse set of protein-linked carbohydrate structures. Some of these complex N-glycan modifications like the presence of β1,2-xylose, core α1,3-fucose or the Lewis a-epitope are characteristic for plants and are evolutionary highly conserved. In mammals, complex N-glycans are involved in different cellular processes including molecular recognition and signaling events. In contrast, the complex N-glycan function is still largely unknown in plants. Here, in this short review, I focus on important recent developments and discuss their implications for future research in plant glycobiology and plant biotechnology.

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“…Some of them have been already licensed, such as the enzyme glucocerebrosidase (taliglucerase alfa, Protalix™) against Gaucher’s disease, or are very close to implementation, such as a vaccine against influenza (haemagglutinins assembled into virus-like particles, Medicago Inc.) (Grabowski et al 2014; Ward et al 2014). Nowadays, most of biopharmaceuticals are produced using transient expression systems based on virus-derived vectors or agroinfiltration (Thuenemann et al 2013; Yusibov et al 2013).…”

Section: Introductionmentioning

confidence: 99%

Micropropagation of transgenic lettuce containing HBsAg as a method of mass-scale production of standardised plant material for biofarming purposes

et al. 2016

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Key message Micropropagation protocol of transgenic lettuce bearing S-, M- and L-HBsAg was developed for increased production of uniformised material for oral vaccine preparation. AbstractEffective manufacturing of plant-based biopharmaceuticals, including oral vaccines, depends on sufficient content of a protein of interest in the initial material and its efficient conversion into an administrable formulation. However, stable production of plants with a uniformised antigen content is equally important for reproducible processing. This can be provided by micropropagation techniques. Here, we present a protocol for micropropagation of transgenic lettuce lines bearing HBV surface antigens: S-, M- and L-HBsAg. These were multiplied through axillary buds to avoid the risk of somaclonal variation. Micropropagation effectiveness reached 3.5–5.7 per passage, which implies potential production of up to 6600 plant clones within a maximum 5 months. Multiplication and rooting rates were statistically homogenous for most transgenic and control plants. For most lines, more than 90 % of clones obtained via in vitro micropropagation had HBsAg content as high as reference plants directly developed from seeds. Clones were also several times more uniform in HBsAg expression. Variation coefficients of HBsAg content did not exceed 10 % for approximately 40–85 % of clones, or reached a maximum 20 % for 90 % of all clones. Tissue culture did not affect total and leaf biomass yields. Seed production for clones was decreased insignificantly and did not impact progeny condition. Micropropagation facilitates a substantial increase in the production of lettuce plants with high and considerably equalised HBsAg contents. This, together with the previously reported optimisation of plant tissue processing and its long-term stability, constitutes a successive step in manufacturing of a standardised anti-HBV oral vaccine of reliable efficacy.

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Taliglucerase alfa: An enzyme replacement therapy using plant cell expression technology

Cited by 123 publications

References 43 publications

Enzyme replacement therapy with taliglucerase alfa: 36‐month safety and efficacy results in adult patients with Gaucher disease previously treated with imiglucerase

Enzyme replacement therapy with taliglucerase alfa: 36‐month safety and efficacy results in adult patients with Gaucher disease previously treated with imiglucerase

Biological significance of complex N-glycans in plants and their impact on plant physiology

Micropropagation of transgenic lettuce containing HBsAg as a method of mass-scale production of standardised plant material for biofarming purposes

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