دورية أكاديمية
Recent Advances Toward Engineering Glycoproteins Using Modified Yeast Display Platforms.
| العنوان: | Recent Advances Toward Engineering Glycoproteins Using Modified Yeast Display Platforms. |
|---|---|
| المؤلفون: | Shenoy A; Biochemistry and Molecular Biology Department, University of Georgia, Athens, GA, USA., Barb AW; Biochemistry and Molecular Biology Department, University of Georgia, Athens, GA, USA. adambarb@uga.edu. |
| المصدر: | Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2022; Vol. 2370, pp. 185-205. |
| نوع المنشور: | Journal Article; Review |
| اللغة: | English |
| بيانات الدورية: | Publisher: Humana Press Country of Publication: United States NLM ID: 9214969 Publication Model: Print Cited Medium: Internet ISSN: 1940-6029 (Electronic) Linking ISSN: 10643745 NLM ISO Abbreviation: Methods Mol Biol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Totowa, NJ : Humana Press Original Publication: Clifton, N.J. : Humana Press, |
| مواضيع طبية MeSH: | Saccharomyces cerevisiae*/genetics , Saccharomyces cerevisiae*/metabolism, Glycoproteins/genetics ; Glycoproteins/metabolism ; Glycosylation ; Humans ; Protein Engineering ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism |
| مستخلص: | Yeast are capable recombinant protein expression hosts that provide eukaryotic posttranslational modifications such as disulfide bond formation and N-glycosylation. This property has been used to create surface display libraries for protein engineering; however, yeast surface display (YSD) with common laboratory strains has limitations in terms of diversifying glycoproteins due to the incorporation of high levels of mannose residues which often obscure important epitopes and are immunogenic in humans. Developing new strains for efficient and appropriate display will require combining existing technologies to permit efficient glycoprotein engineering. Foundational efforts generating knockout strains lacking characteristic hypermannosylation reactions exhibited morphological defects and poor growth. Later strains with "humanized" N-glycosylation machinery surmounted these limitations by targeting a small suite of glycosylhydrolase and glycosyltransferase enzymes from other taxa to the endoplasmic reticulum and Golgi. Advanced yeast strains also provide key modifications at the glycan termini that are essential for the full function of many glycoproteins. Here we review progress toward glycoprotein engineering when glycosylation is required for full function using advanced yeast expression platforms and the suitability of each for YSD of glycoproteins. (© 2022. Springer Science+Business Media, LLC, part of Springer Nature.) |
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| فهرسة مساهمة: | Keywords: Glycoengineering; Glycosylhydrolase; Glycosyltransferase; Yeast surface display |
| المشرفين على المادة: | 0 (Glycoproteins) 0 (Recombinant Proteins) |
| تواريخ الأحداث: | Date Created: 20211006 Date Completed: 20220106 Latest Revision: 20220106 |
| رمز التحديث: | 20240628 |
| DOI: | 10.1007/978-1-0716-1685-7_9 |
| PMID: | 34611870 |
| قاعدة البيانات: | MEDLINE |
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