Using glyco-engineering to produce therapeutic proteins

Dicker, Martina; Strasser, Richard

doi:10.1517/14712598.2015.1069271

Cited by 71 publications

(51 citation statements)

References 104 publications

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“…Recently, glyco-engineering technique has been used to produce recombinant therapeutic proteins with optimized efficacy, half-life, specificity, and antigenicity. Glyco-engineering of expression platforms is progressively documented as an essential approach to advance biopharmaceuticals (Ferrer-Miralles et al, 2009;Dicker and Strasser, 2015). The technique has been applied to in vivo expression systems that include mammalian cells, insect cells, yeast, and plants for the production of recombinant proteins.…”

Section: Engineered Immunomodulatory Antibodiesmentioning

confidence: 99%

Antibody Engineering for Pursuing a Healthier Future

et al. 2017

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Since the development of antibody-production techniques, a number of immunoglobulins have been developed on a large scale using conventional methods. Hybridoma technology opened a new horizon in the production of antibodies against target antigens of infectious pathogens, malignant diseases including autoimmune disorders, and numerous potent toxins. However, these clinical humanized or chimeric murine antibodies have several limitations and complexities. Therefore, to overcome these difficulties, recent advances in genetic engineering techniques and phage display technique have allowed the production of highly specific recombinant antibodies. These engineered antibodies have been constructed in the hunt for novel therapeutic drugs equipped with enhanced immunoprotective abilities, such as engaging immune effector functions, effective development of fusion proteins, efficient tumor and tissue penetration, and high-affinity antibodies directed against conserved targets. Advanced antibody engineering techniques have extensive applications in the fields of immunology, biotechnology, diagnostics, and therapeutic medicines. However, there is limited knowledge regarding dynamic antibody development approaches. Therefore, this review extends beyond our understanding of conventional polyclonal and monoclonal antibodies. Furthermore, recent advances in antibody engineering techniques together with antibody fragments, display technologies, immunomodulation, and broad applications of antibodies are discussed to enhance innovative antibody production in pursuit of a healthier future for humans.

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Section: Engineered Immunomodulatory Antibodiesmentioning

confidence: 99%

Antibody Engineering for Pursuing a Healthier Future

et al. 2017

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“…Moreover, glycosylation is probably the most important quality attribute of therapeutic glycoproteins, because the pharmacokinetic effects of undesired glycosylation patterns can be decreased drug efficacy or increased antigenicity (Bertozzi et al, 2009;Butler and Spearman, 2014). Recent advances in glycoengineering and descriptions of how effector genes can be used to modulate glycosylation have been described in recent reviews (Bennun et al, 2016;Dicker and Strasser, 2015;Spahn and Lewis, 2014). Because of scope limitations, only misfolding/aggregation and propeptide processing in relation to effector genes will be described here.…”

Section: Product Qualitymentioning

confidence: 99%

Improving the secretory capacity of Chinese hamster ovary cells by ectopic expression of effector genes: Lessons learned and future directions

Hansen

Pristovšek

Kildegaard

et al. 2017

Biotechnology Advances

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“…Engineering N‐ glycosylation in diatom may be undertaken for production of recombinant mAbs with humanized glycan structures, to optimize their stability, efficacy and biological function. Similar glyco‐engineering efforts have already been successfully implemented in plants and moss which are now able to produce recombinant biopharmaceuticals with humanized N ‐glycosylation. Such developments would broaden future possibilities of using alga‐based systems for production of innovative biopharmaceuticals, to‐me version, or biobetters, designed for new therapeutic applications.…”

Section: Discussionmentioning

confidence: 99%

Alga‐Made Anti‐Hepatitis B Antibody Binds to Human Fcγ Receptors

Vanier

Stelter

Vanier

et al. 2017

Biotechnology Journal

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Microalgae are unicellular eukaryotic organisms which represent an emerging alternative to other cell biofactories commonly used to produce monoclonal antibodies. Microalgae display several biotechnological advantages such as their rapid growth rate and their phototrophic lifestyle allowing low production costs as protein expression is solar-fueled. Recently, a fully assembled recombinant IgG antibody directed against Hepatitis B surface antigen is produced and secreted in the culture medium of the diatom Phaeodactylum tricornutum. A biochemical characterization of this recombinant antibody demonstrated that the Asn-297 is N-glycosylated by oligomannosides. In the immune system, antibodies interact with effector molecules and cells through their Fc part and the recognition of Fcγ receptors (FcγR) which are important for inducing phagocytosis of opsonized microbes. Interactions between IgG and FcγR are influenced by the N-glycan structures present on the Asn-297. In this study, the authors characterized the binding capacity of the anti-hepatitis B recombinant IgG produced in P. tricornutum to two human Fcγ receptors (FcγRI and IIIa) using a cellular binding assay and surface plasmon resonance (SPR). This allowed us to demonstrate that the alga-made antibody is able to bind FcγRI with a reduced affinity and engages FcyRIIIa with 3-times higher affinity compared to a control human IgG1.

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Using glyco-engineering to produce therapeutic proteins

Cited by 71 publications

References 104 publications

Antibody Engineering for Pursuing a Healthier Future

Antibody Engineering for Pursuing a Healthier Future

Improving the secretory capacity of Chinese hamster ovary cells by ectopic expression of effector genes: Lessons learned and future directions

Alga‐Made Anti‐Hepatitis B Antibody Binds to Human Fcγ Receptors

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