Protein Expression-Yeast

Nielsen, Klaus

doi:10.1016/b978-0-12-420070-8.00012-x

Cited by 19 publications

(9 citation statements)

References 108 publications

(173 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In vitro cellulose biosynthesis by heterologously expressed and purified plant CESAs has been achieved with single CESAs from hybrid aspen (PttCESA8), the moss Physcomitrella patens (PpCESA5), and six CESAs from bamboo (Bambusa oldhamii) . Production of functional plant CESAs requires expression in a eukaryotic organism such as yeast, as opposed to bacterial expression. − Eukaryotic expression systems are favorable for plant protein expression likely due to compatible translational mechanisms and post-translational modifications . However, purification of active CESAs is challenging, requiring detergent solubilization, affinity purification, chromatographic separation, and reconstitution into proteoliposomes, − thereby limiting the scale at which pure CESAs are isolated.…”

Section: Enzymatic Polysaccharide Synthesis With Glycosyltrasferasesmentioning

confidence: 99%

“…141−143 Eukaryotic expression systems are favorable for plant protein expression likely due to compatible translational mechanisms and post-translational modifications. 144 However, purification of active CESAs is challenging, requiring detergent solubilization, affinity purification, chromatographic separation, and reconstitution into proteoliposomes, 141−143 thereby limiting the scale at which pure CESAs are isolated. Additionally, the physical and mechanical properties of cellulosic products from recombinant plant CESAs are not well characterized, although the products from PttCESA8 are partially resistant to acid hydrolysis suggesting coalescence of glucans into crystals.…”

Section: ■ Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Enzymatic Synthesis of Artificial Polysaccharides

Smith

Ortiz-Soto

Roth

et al. 2020

ACS Sustainable Chem. Eng.

View full text Add to dashboard Cite

Polysaccharides are the most important renewable polymers on Earth and hold an enormous potential for the production of ecofriendly functional materials. In addition to being sustainable, they have superior properties to synthetic polymers, particularly in the biomedical field where biocompatibility and biodegradability are vital. Derivatization of polysaccharides obtained from plant biomass paves the path forward for the design and manufacturing of advanced materials with specific properties adapted to meet definitive needs. However, these advances have been severely limited due to issues with establishing structure− property relationships, which are hampered by the heterogeneity of target polysaccharides and the random distribution of functional groups obtained after their chemical modification. An accurate correlation of structure−property relationships at multiple length scales requires substrates with defined sizes, sequences, and substitution patterns. Such tailor-made polysaccharides may be obtained by implementing a bottom-up approach, starting from monosaccharide or oligosaccharide building blocks followed by their polymerization and substitution through catalysis by different carbohydrate-active enzymes such as glycosynthases, phosphorylases, sucrases, and glycosyltransferases. Recent progress in the enzymatic synthesis of artificial polysaccharides is reviewed, with an emphasis on the potential of the synthesized products, either as new materials or as tools to study structure−property relationships. The obtained information will guide future developments of rationally designed biobased materials for industrial and biomedical applications.

show abstract

Section: Enzymatic Polysaccharide Synthesis With Glycosyltrasferasesmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

Enzymatic Synthesis of Artificial Polysaccharides

Smith

Ortiz-Soto

Roth

et al. 2020

ACS Sustainable Chem. Eng.

View full text Add to dashboard Cite

show abstract

“…Unlike E. coli, yeasts can secrete recombinant proteins extracellularly, which makes the downstream purification process simpler and less costly. The inclusion of certain PTMs in this eukaryotic expression system also often facilitates proper folding of the recombinant protein [69]. Several currently licensed hepatitis B vaccines, such as Engerix-B ® , Recombivax HB, and HEPLISAV-B, use recombinant hepatitis B surface antigens (HBsAg) synthesized in yeast [70].…”

Section: Yeastsmentioning

confidence: 99%

Recombinant Protein Vaccines, a Proven Approach Against Coronavirus Pandemics

Pollet

Chen

Strych

2020

Preprint

View full text Add to dashboard Cite

With the COVID-19 pandemic now ongoing for close to a year, people all over the world are still waiting for a vaccine to become available. The initial focus of accelerated global research and development efforts to bring a vaccine to market as soon as possible was on novel platform technologies that promised speed but had limited history in the clinic. In contrast, recombinant protein vaccines, with numerous examples in the clinic for many years, missed out on the early wave of investments from government and industry. Emerging data are now surfacing suggesting that recombinant protein vaccines indeed might offer an advantage or complement to the nucleic acid or viral vector vaccines that will likely reach the clinic faster. Here, we summarize the current public information on the nature and on the development status of recombinant subunit antigens and adjuvants targeting SARS-CoV-2 infections.

show abstract

“…Although a few biologics are still produced in E. coli (e.g., IL-2, as described in section Interleukin-2), the lack of N-glycans that ensure quality control during folding ( 306 ) makes prokaryotic production untenable for most glycoproteins including mAbs. Yeast ( S. cerevisiae and Pichia pastoris ) provide another high productivity, low cost production platform ( 307 , 308 ) and—being eukaryotic cells—do have N-glycans; yeast glycans, however, tend to be highly mannosylated which reduces serum longevity thus compromising pharmacokinetics and also impacting downstream effector functions ( 309 ). Even though efforts have been made to “humanize” yeast glycosylation, these cells have not become a widely-accepted biomanufacturing platform ( 309 ).…”

Section: Design Considerations and Biomanufacturingmentioning

confidence: 99%

Improving Immunotherapy Through Glycodesign

et al. 2018

View full text Add to dashboard Cite

Immunotherapy is revolutionizing health care, with the majority of high impact “drugs” approved in the past decade falling into this category of therapy. Despite considerable success, glycosylation—a key design parameter that ensures safety, optimizes biological response, and influences the pharmacokinetic properties of an immunotherapeutic—has slowed the development of this class of drugs in the past and remains challenging at present. This article describes how optimizing glycosylation through a variety of glycoengineering strategies provides enticing opportunities to not only avoid past pitfalls, but also to substantially improve immunotherapies including antibodies and recombinant proteins, and cell-based therapies. We cover design principles important for early stage pre-clinical development and also discuss how various glycoengineering strategies can augment the biomanufacturing process to ensure the overall effectiveness of immunotherapeutics.

show abstract

Protein Expression-Yeast

Cited by 19 publications

References 108 publications

Enzymatic Synthesis of Artificial Polysaccharides

Enzymatic Synthesis of Artificial Polysaccharides

Recombinant Protein Vaccines, a Proven Approach Against Coronavirus Pandemics

Improving Immunotherapy Through Glycodesign

Contact Info

Product

Resources

About