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Glyco-Engineering

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Cover of 'Glyco-Engineering'

Table of Contents

  1. Altmetric Badge
    Book Overview
  2. Altmetric Badge
    Chapter 1 Current Approaches to Engineering N -Linked Protein Glycosylation in Bacteria
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    Chapter 2 Inverse Metabolic Engineering for Enhanced Glycoprotein Production in Escherichia coli
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    Chapter 3 GlycoSNAP: A High-Throughput Screening Methodology for Engineering Designer Glycosylation Enzymes
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    Chapter 4 Production of Glycoproteins with Asparagine-Linked N -Acetylglucosamine in Escherichia coli
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    Chapter 5 Glyco-engineering O-Antigen-Based Vaccines and Diagnostics in E. coli
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    Chapter 6 Progress in Yeast Glycosylation Engineering.
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    Chapter 7 Protein Production with a Pichia pastoris OCH1 Knockout Strain in Fed-Batch Mode.
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    Chapter 8 Engineering the Pichia pastoris N-Glycosylation Pathway Using the GlycoSwitch Technology
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    Chapter 9 Development of a Valuable Yeast Strain Using a Novel Mutagenesis Technique for the Effective Production of Therapeutic Glycoproteins.
  11. Altmetric Badge
    Chapter 10 An Overview and History of Glyco-Engineering in Insect Expression Systems.
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    Chapter 11 Glyco-Engineering
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    Chapter 12 Glyco-Engineering
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    Chapter 13 Engineering N-Glycosylation Pathway in Insect Cells: Suppression of β-N-Acetylglucosaminidase and Expression of β-1,4-Galactosyltransferase.
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    Chapter 14 N-Glyco-Engineering in Plants: Update on Strategies and Major Achievements
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    Chapter 15 Glyco-Engineering
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    Chapter 16 Im“plant”ing of Mammalian Glycosyltransferase Gene into Plant Suspension-Cultured Cells Using Agrobacterium-Mediated Transformation
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    Chapter 17 Transient Glyco-Engineering of N. benthamiana Aiming at the Synthesis of Multi-antennary Sialylated Proteins
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    Chapter 18 Subcellular Targeting of Proteins Involved in Modification of Plant N- and O-Glycosylation
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    Chapter 19 Assembly of Multigene Constructs Using Golden Gate Cloning.
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    Chapter 20 Strategies for Engineering Protein N-Glycosylation Pathways in Mammalian Cells
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    Chapter 21 Glycan Remodeling with Processing Inhibitors and Lectin-Resistant Eukaryotic Cells
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    Chapter 22 Production of Highly Sialylated Recombinant Glycoproteins Using Ricinus communis Agglutinin-I-Resistant CHO Glycosylation Mutants
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    Chapter 23 Metabolic Glyco-Engineering in Eukaryotic Cells and Selected Applications
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    Chapter 24 Evaluation of Quenching and Extraction Methods for Nucleotide/Nucleotide Sugar Analysis
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    Chapter 25 Chemoenzymatic Glyco-engineering of Monoclonal Antibodies
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    Chapter 26 Chemical Polysialylation of Recombinant Human Proteins
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    Chapter 27 Site-Specific Glycosylation Profiling Using Liquid Chromatography-Tandem Mass Spectrometry (LC-MS)
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    Chapter 28 Mass Spectrometric Analysis of Oligo- and Polysialic Acids
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    Chapter 29 Isomer-Specific Analysis of Released N-Glycans by LC-ESI MS/MS with Porous Graphitized Carbon
Attention for Chapter 8: Engineering the Pichia pastoris N-Glycosylation Pathway Using the GlycoSwitch Technology
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Chapter title
Engineering the Pichia pastoris N-Glycosylation Pathway Using the GlycoSwitch Technology
Chapter number 8
Book title
Glyco-Engineering
Published in
Methods in molecular biology, January 2015
DOI 10.1007/978-1-4939-2760-9_8
Pubmed ID
Book ISBNs
978-1-4939-2759-3, 978-1-4939-2760-9
Authors

Laukens, Bram, De Wachter, Charlot, Callewaert, Nico, Bram Laukens, Charlot De Wachter, Nico Callewaert

Abstract

Pichia pastoris is an important host for recombinant protein production. As a protein production platform, further development for therapeutic glycoproteins has been hindered by the high-mannose-type N-glycosylation common to yeast and fungi. Such N-glycans can complicate downstream processing, might be immunogenic or cause the rapid clearance of the glycoprotein from circulation. In recent years, much effort has gone to engineering the N-glycosylation pathway of Pichia pastoris to mimic the human N-glycosylation pathway. This can be of pivotal importance to generate the appropriate glycoforms of therapeutically relevant glycoproteins or to gain a better understanding of structure-function relationships.This chapter describes the methodology to create such glyco-engineered Pichia pastoris strains using the GlycoSwitch(®). This strategy consists of the disruption of an endogenous glycosyltransferase and the heterologous expression of a glycosidase or glycosyltransferase targeted to the Endoplasmic Reticulum or the Golgi of the host. For each step in the process, we describe the transformation procedure, small-scale screening and we also describe how to perform DNA-Sequencer-Aided Fluorophore-Assisted Capillary Electrophoresis (DSA-FACE) to select for clones with the appropriate N-glycosylation profile. The steps described in this chapter can be followed in an iterative fashion in order to generate clones of Pichia pastoris expressing heterologous proteins with humanized N-glycans.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 85 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United Kingdom 1 1%
Austria 1 1%
Unknown 83 98%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 17 20%
Student > Master 15 18%
Student > Bachelor 15 18%
Researcher 10 12%
Student > Doctoral Student 2 2%
Other 5 6%
Unknown 21 25%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 29 34%
Agricultural and Biological Sciences 14 16%
Chemical Engineering 6 7%
Engineering 4 5%
Immunology and Microbiology 3 4%
Other 7 8%
Unknown 22 26%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 18 June 2015.
All research outputs
#20,280,315
of 22,813,792 outputs
Outputs from Methods in molecular biology
#9,908
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Outputs of similar age
#295,827
of 353,106 outputs
Outputs of similar age from Methods in molecular biology
#636
of 997 outputs
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