Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autor principal: Strasser, Richard
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2013
Materias:
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
_version_ 1782278820008558592
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