Conference Scene: Molecular pharming: manufacturing medicines in plants

Lössl, Andreas Günter; Clarke, Jihong Liu

doi:10.2217/imt.12.146

Cited by 5 publications

(2 citation statements)

References 21 publications

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“…The first human protein with pharmaceutical potential expressed in transgenic tobacco was human serum albumin in 1990 [234,235]. Today, the expression platform has been greatly improved and several plant-derived proteins have even entered clinical studies [236,237].…”

Section: Plantsmentioning

confidence: 99%

Emerging Alternative Production Systems

Sommer

Laux

Frenzel

et al. 2014

Handbook of Therapeutic Antibodies

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The market of recombinant protein pharmaceuticals is growing rapidly. Among those, recombinant antibodies are the fastest growing group and a large number of new antibody products are in clinical and preclinical development. Since most conventional cost-effective microbial expression systems are not yet applicable for the expression of fully functional immunoglobulin G (IgG) antibodies, almost all of the currently marketed therapeutic recombinant antibody products are produced from animal cell culture processes that are associated with relative high operating expenses. Thus, to make broad use of recombinant antibody therapeutics more affordable, alternative production systems with improved efficiency and reduced operating expenses are highly desirable.IgG currently is the dominant antibody format for therapeutics. As a heterotetrameric molecule with numerous disulfide bonds and several glycosylation sites IgG makes itself a challenging candidate for heterologous expression, especially in prokaryotes. Glycosylation of the fragment crystallizable (Fc) region has been shown to be essential for mediating effector functions such as antibody-dependent cell-mediated cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC) [1]. Furthermore, the glycosylation pattern strongly influences the efficiency of the induction of effector functions by antibodies [2, 3]. For applications that depend on the immunological effector functions of the antibody therefore eukaryotic production systems with suitable glycosylation capabilities are necessary.Antibody fragments such as single chain fragment variable (scFv) and fragment antigen binding (Fab) are less complex and the antigen-binding activity is independent of glycosylation, which makes them qualified for prokaryotic expression systems. Certainly, these fragments are incapable of mediating immunological effector functions but for numerous applications this is not necessary or even unwanted.Besides the two traditional expression systems, Escherichia coli for antibody fragments and Chinese hamster ovarian (CHO) or myeloma cells for IgG antibodies, numerous alternative expression systems are currently under development.

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Section: Plantsmentioning

confidence: 99%

Emerging Alternative Production Systems

Sommer

Laux

Frenzel

et al. 2014

Handbook of Therapeutic Antibodies

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“…The term "molecular pharming," blend of pharmaceutical and farming, surfaced in the literature in the 1980s to refer to the production of high-value compounds in transgenic animals. Nowadays, the expression is mainly employed to the production of recombinant pharmaceutically relevant proteins or secondary products in plants [1][2][3].…”

Section: Introductionmentioning

confidence: 99%

Prospects for the Production of Recombinant Therapeutic Proteins and Peptides in Plants: Special Focus on Angiotensin I-Converting Enzyme Inhibitory (ACEI) Peptides

Gomes¹,

Oliveira²,

Vieira³

et al. 2020

Genetic Engineering - A Glimpse of Techniques and Applications

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Molecular pharming is a cost-effective, scalable, and safe system to produce high-quality and biologically active recombinant therapeutic proteins. Thus, plants are emerging alternative platform for the production of pharmaceutically relevant proteins such as vaccines, antibodies, antibody derivatives, and some serumderived proteins. Additionally, plants have also been used to produce bioactive and immunogenic peptides. The efficacy, selectivity, specificity, and low toxicity make them particularly well-suited therapeutic agents for various indications, for instance, cardiovascular and infectious diseases, immunological disorders, and cancer. In the broad range of known bioactive peptides, angiotensin I-converting enzyme inhibitory (ACEI) peptides derived from food proteins have attracted particular attention for their ability to prevent hypertension. So far, several ACEI peptides have been identified in food proteins, mainly in milk, eggs, and plants. The industrial production of ACEI peptides is based on enzymatic proteolysis of whole food proteins, which leads to the release of small bioactive peptides with ACE-inhibitory activity. The problems associated to such procedures, namely, cost and loss of functional properties, have demonstrated the need to develop more straightforward methods to produce ACEI peptides. One viable hypothesis, discussed in this chapter, is to genetically engineer crop plants to produce and deliver antihypertensive peptides.

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Emerging Alternative Production Systems

Jostock¹

2007

Handbook of Therapeutic Antibodies

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Conference Scene: Molecular pharming: manufacturing medicines in plants

Cited by 5 publications

References 21 publications

Emerging Alternative Production Systems

Emerging Alternative Production Systems

Prospects for the Production of Recombinant Therapeutic Proteins and Peptides in Plants: Special Focus on Angiotensin I-Converting Enzyme Inhibitory (ACEI) Peptides

Emerging Alternative Production Systems

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