A gene responsible for prolyl-hydroxylation of moss-produced recombinant human erythropoietin

Parsons, Juliana; Altmann, Friedrich; Graf, Manuela; Stadlmann, Johannes; Reski, Ralf; Decker, Eva L.

doi:10.1038/srep03019

Cited by 56 publications

(66 citation statements)

References 52 publications

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“…These O-mannose structures differ from mammalian a-dystroglycan-type O-mannosylation and may cause unwanted side effects when present on recombinant glycoproteins. Plants can convert exposed proline residues adjacent to O-glycosylation sites of recombinant proteins into hydroxyproline residues [85], which can be further modified by arabinosyltransferases leading to the presence of small arabinose chains ( Figure 5D) [86].…”

Section: What Are the Targets For O-glycanengineering?mentioning

confidence: 99%

Using glyco-engineering to produce therapeutic proteins

Dicker

Strasser

2015

Expert Opinion on Biological Therapy

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Glyco-engineering of expression platforms is increasingly recognized as an important strategy to improve biopharmaceuticals. A better understanding and control of the factors leading to glycan heterogeneity will allow simplified production of recombinant glycoprotein therapeutics with less variation in terms of glycosylation. Further technological advances will have a major impact on manufacturing processes and may provide a completely new class of glycoprotein therapeutics with customized functions.

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Section: What Are the Targets For O-glycanengineering?mentioning

confidence: 99%

Using glyco-engineering to produce therapeutic proteins

Dicker

Strasser

2015

Expert Opinion on Biological Therapy

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“…This gene was integrated into the Physcomitrella patens genome by “knockin” into the xylosyltransferase or fucosyltransferase locus [103]. To avoid unwanted O -glycosylation of human proteins produced in moss, a gene responsible for prolylhydroxylation was identified and deleted from the genome [104]. The first human protein produced in the moss system was the vascular endothelial growth factor (VEGF) [105], which has a central function in angiogenesis and cancer [106].…”

Section: Cell Factory Potentials In Macroalgae and Lower Plantsmentioning

confidence: 99%

Algal Cell Factories: Approaches, Applications, and Potentials

Fu¹,

Chaiboonchoe²,

Khraiwesh

et al. 2016

Marine Drugs

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With the advent of modern biotechnology, microorganisms from diverse lineages have been used to produce bio-based feedstocks and bioactive compounds. Many of these compounds are currently commodities of interest, in a variety of markets and their utility warrants investigation into improving their production through strain development. In this review, we address the issue of strain improvement in a group of organisms with strong potential to be productive “cell factories”: the photosynthetic microalgae. Microalgae are a diverse group of phytoplankton, involving polyphyletic lineage such as green algae and diatoms that are commonly used in the industry. The photosynthetic microalgae have been under intense investigation recently for their ability to produce commercial compounds using only light, CO2, and basic nutrients. However, their strain improvement is still a relatively recent area of work that is under development. Importantly, it is only through appropriate engineering methods that we may see the full biotechnological potential of microalgae come to fruition. Thus, in this review, we address past and present endeavors towards the aim of creating productive algal cell factories and describe possible advantageous future directions for the field.

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“…Such plant-specific modifications are unwanted and can be eliminated by knockout of the responsible enzymes like prolyl 4-hydroxylases. This engineering approach has been successfully carried out in a moss-based expression system 26 and similar strategies are currently developed for higher plants like N. benthamiana .…”

Section: Engineering Of Mucin-type-o-glycans On Recombinant Iga1 In Nmentioning

confidence: 99%

Glyco-engineering for the production of recombinant IgA1 with distinct mucin-type O-glycans in plants

2016

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IgA nephropathy (IgAN) is a common autoimmune disease that is characterized by formation and deposition of IgA1-containing immune complexes frequently leading to end-stage kidney disease. The IgA1 in these immune complexes carries aberrantly glycosylated O-glycans. In circulating IgA1 these galactose-deficient mucin-type O-glycans are bound by autoantibodies and thus, contribute to immune complex formation and pathogenesis. Even though the disease is associated with the overproduction of aberrant O-glycans on IgA1, specific structure-function-studies of mucin-type O-glycans are limited. Compared to other expression hosts, plants offer the opportunity for de novo synthesis of O-glycans on recombinant glycoproteins as they are lacking the mammalian O-glycosylation pathway. Recently, we demonstrated that Nicotiana benthamiana are suitable for the generation of distinct O-glycans on recombinant IgA1. Here, we expand our engineering repertoire by in planta generation of galactose-deficient and α2,6-sialylated O-glycans which are the prevailing glycans detected on IgA1 from patients with IgAN.

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A gene responsible for prolyl-hydroxylation of moss-produced recombinant human erythropoietin

Cited by 56 publications

References 52 publications

Using glyco-engineering to produce therapeutic proteins

Using glyco-engineering to produce therapeutic proteins

Algal Cell Factories: Approaches, Applications, and Potentials

Glyco-engineering for the production of recombinant IgA1 with distinct mucin-type O-glycans in plants

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