Academic Journal
An oligosaccharyltransferase from Leishmania major increases the N‐glycan occupancy on recombinant glycoproteins produced in Nicotiana benthamiana
العنوان: | An oligosaccharyltransferase from Leishmania major increases the N‐glycan occupancy on recombinant glycoproteins produced in Nicotiana benthamiana |
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المؤلفون: | Castilho, Alexandra, Beihammer, Gernot, Pfeiffer, Christina, Göritzer, Kathrin, Montero‐Morales, Laura, Vavra, Ulrike, Maresch, Daniel, Grünwald‐Gruber, Clemens, Altmann, Friedrich, Steinkellner, Herta, Strasser, Richard |
المساهمون: | Austrian Science Fund |
المصدر: | Plant Biotechnology Journal ; volume 16, issue 10, page 1700-1709 ; ISSN 1467-7644 1467-7652 |
بيانات النشر: | Wiley |
سنة النشر: | 2018 |
المجموعة: | Wiley Online Library (Open Access Articles via Crossref) |
الوصف: | Summary N‐glycosylation is critical for recombinant glycoprotein production as it influences the heterogeneity of products and affects their biological function. In most eukaryotes, the oligosaccharyltransferase is the central‐protein complex facilitating the N‐glycosylation of proteins in the lumen of the endoplasmic reticulum ( ER ). Not all potential N‐glycosylation sites are recognized in vivo and the site occupancy can vary in different expression systems, resulting in underglycosylation of recombinant glycoproteins. To overcome this limitation in plants, we expressed Lm STT 3D, a single‐subunit oligosaccharyltransferase from the protozoan Leishmania major transiently in Nicotiana benthamiana, a well‐established production platform for recombinant proteins. A fluorescent protein‐tagged Lm STT 3D variant was predominately found in the ER and co‐located with plant oligosaccharyltransferase subunits. Co‐expression of Lm STT 3D with immunoglobulins and other recombinant human glycoproteins resulted in a substantially increased N‐glycosylation site occupancy on all N‐glycosylation sites except those that were already more than 90% occupied. Our results show that the heterologous expression of Lm STT 3D is a versatile tool to increase N‐glycosylation efficiency in plants. |
نوع الوثيقة: | article in journal/newspaper |
اللغة: | English |
DOI: | 10.1111/pbi.12906 |
الاتاحة: | http://dx.doi.org/10.1111/pbi.12906 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fpbi.12906 https://onlinelibrary.wiley.com/doi/pdf/10.1111/pbi.12906 |
Rights: | http://creativecommons.org/licenses/by/4.0/ |
رقم الانضمام: | edsbas.568B64 |
قاعدة البيانات: | BASE |
DOI: | 10.1111/pbi.12906 |
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