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与三种N-糖基化酶瞬时共表达可在(此处原文未明确具体表达系统)中产生GalNAc-α-糖基化的粒细胞集落刺激因子。

Transient co-expression with three -glycosylation enzymes allows production of GalNAc--glycosylated Granulocyte-Colony Stimulating Factor in .

作者信息

Ramírez-Alanis Israel A, Renaud Justin B, García-Lara Silverio, Menassa Rima, Cardineau Guy A

机构信息

1School of Engineering and Sciences, Tecnologico de Monterrey, Campus Monterrey, Av. Eugenio Garza Sada 2501 Sur, C.P. 64849 Monterrey, NL Mexico.

3Agriculture and Agri-Food Canada, London, ON Canada.

出版信息

Plant Methods. 2018 Nov 6;14:98. doi: 10.1186/s13007-018-0363-y. eCollection 2018.

DOI:10.1186/s13007-018-0363-y
PMID:30410568
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6219069/
Abstract

BACKGROUND

Expression of economically relevant proteins in alternative expression platforms, especially plant expression platforms, has gained significant interest in recent years. A special interest in working with plants as bioreactors for the production of pharmaceutical proteins is related to low production costs, product safety and quality. Among the different properties that plants can also offer for the production of recombinant proteins, protein glycosylation is crucial since it may have an impact on pharmaceutical functionality and/or stability.

RESULTS

The pharmaceutical glycoprotein human Granulocyte-Colony Stimulating Factor was transiently expressed in plants and subjected to mammalian-specific mucin-type -glycosylation by co-expressing the pharmaceutical protein together with the glycosylation machinery responsible for such post-translational modification.

CONCLUSIONS

The pharmaceutical glycoprotein human Granulocyte-Colony Stimulating Factor can be expressed in plants via agroinfiltration with its native mammalian-specific mucin-type -glycosylation.

摘要

背景

近年来,在替代表达平台,特别是植物表达平台中表达具有经济价值的蛋白质引起了广泛关注。将植物用作生产药用蛋白质的生物反应器的特别兴趣与低成本、产品安全性和质量有关。在植物可用于生产重组蛋白的不同特性中,蛋白质糖基化至关重要,因为它可能会影响药物功能和/或稳定性。

结果

药用糖蛋白人粒细胞集落刺激因子在植物中瞬时表达,并通过与负责这种翻译后修饰的糖基化机制共表达药用蛋白,使其进行哺乳动物特异性粘蛋白型糖基化。

结论

药用糖蛋白人粒细胞集落刺激因子可通过农杆菌浸润在植物中表达,并具有其天然的哺乳动物特异性粘蛋白型糖基化。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95c2/6219069/bc4902d61581/13007_2018_363_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95c2/6219069/e111aabffdee/13007_2018_363_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95c2/6219069/f2e737575c54/13007_2018_363_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95c2/6219069/d8828dfa705e/13007_2018_363_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95c2/6219069/a2e6c9c25b98/13007_2018_363_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95c2/6219069/bc4902d61581/13007_2018_363_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95c2/6219069/e111aabffdee/13007_2018_363_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95c2/6219069/f2e737575c54/13007_2018_363_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95c2/6219069/d8828dfa705e/13007_2018_363_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95c2/6219069/a2e6c9c25b98/13007_2018_363_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95c2/6219069/bc4902d61581/13007_2018_363_Fig5_HTML.jpg

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