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Engineering of human-type O-glycosylation in Nicotiana benthamiana plants
Therapeutic properties of recombinant proteins are very often affected by the composition and heterogeneity of their glycans. Conventional expression systems for recombinant pharmaceutical proteins typically do not address this problem and produce a mixture of glycoforms that are neither identical t...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Landes Bioscience
2013
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3728188/ https://www.ncbi.nlm.nih.gov/pubmed/23147167 http://dx.doi.org/10.4161/bioe.22857 |
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author | Strasser, Richard |
author_facet | Strasser, Richard |
author_sort | Strasser, Richard |
collection | PubMed |
description | Therapeutic properties of recombinant proteins are very often affected by the composition and heterogeneity of their glycans. Conventional expression systems for recombinant pharmaceutical proteins typically do not address this problem and produce a mixture of glycoforms that are neither identical to human glycans nor optimized for enhanced efficacy. In terms of glycosylation, plants offer certain advantages over mammalian cells as the N-glycosylation pathway of plants is comparably simple and a typical mammalian O-glycosylation pathway is not present at all. During the last ten years we have developed a plant-based expression platform for the generation of recombinant glycoproteins with defined N-glycans. Now we have extended our tool-box for glyco-engineering in the tobacco related species Nicotiana benthamiana toward the production of tailored mucin-type O-glycans on recombinant proteins. |
format | Online Article Text |
id | pubmed-3728188 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Landes Bioscience |
record_format | MEDLINE/PubMed |
spelling | pubmed-37281882013-08-02 Engineering of human-type O-glycosylation in Nicotiana benthamiana plants Strasser, Richard Bioengineered Commentary Therapeutic properties of recombinant proteins are very often affected by the composition and heterogeneity of their glycans. Conventional expression systems for recombinant pharmaceutical proteins typically do not address this problem and produce a mixture of glycoforms that are neither identical to human glycans nor optimized for enhanced efficacy. In terms of glycosylation, plants offer certain advantages over mammalian cells as the N-glycosylation pathway of plants is comparably simple and a typical mammalian O-glycosylation pathway is not present at all. During the last ten years we have developed a plant-based expression platform for the generation of recombinant glycoproteins with defined N-glycans. Now we have extended our tool-box for glyco-engineering in the tobacco related species Nicotiana benthamiana toward the production of tailored mucin-type O-glycans on recombinant proteins. Landes Bioscience 2013-07-01 2012-11-12 /pmc/articles/PMC3728188/ /pubmed/23147167 http://dx.doi.org/10.4161/bioe.22857 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited. |
spellingShingle | Commentary Strasser, Richard Engineering of human-type O-glycosylation in Nicotiana benthamiana plants |
title | Engineering of human-type O-glycosylation in Nicotiana benthamiana plants |
title_full | Engineering of human-type O-glycosylation in Nicotiana benthamiana plants |
title_fullStr | Engineering of human-type O-glycosylation in Nicotiana benthamiana plants |
title_full_unstemmed | Engineering of human-type O-glycosylation in Nicotiana benthamiana plants |
title_short | Engineering of human-type O-glycosylation in Nicotiana benthamiana plants |
title_sort | engineering of human-type o-glycosylation in nicotiana benthamiana plants |
topic | Commentary |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3728188/ https://www.ncbi.nlm.nih.gov/pubmed/23147167 http://dx.doi.org/10.4161/bioe.22857 |
work_keys_str_mv | AT strasserrichard engineeringofhumantypeoglycosylationinnicotianabenthamianaplants |