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Enhanced secretion of human α1-antitrypsin expressed with a novel glycosylation module in tobacco BY-2 cell culture.

Authors :
Zhang N
Wright T
Caraway P
Xu J
Source :
Bioengineered [Bioengineered] 2019 Dec; Vol. 10 (1), pp. 87-97.
Publication Year :
2019

Abstract

Expression of recombinant proteins fused to a novel glycomodule tag, termed hydroxyproline (Hyp)-O-glycosylated peptides (HypGP), was earlier found to boost secreted protein yields up to 500-fold in plant cell culture. Here, this technology was applied to the expression of human protease inhibitor α1-antitrypsin (AAT) in tobacco BY-2 cell culture. A designer HypGP tag composed of a 'Ala-Pro' motif of 20 units, or (AP) <subscript>20</subscript> , was engineered either at the N- or C-terminal end of AAT. The (AP) <subscript>20</subscript> tag substantially increased the secreted yields of the recombinant AAT up to 34.7 mg/L. However, the (AP) <subscript>20</subscript> -tagged AAT products were frequently subjected to proteolytic processing. The intact AAT-(AP) <subscript>20</subscript> along with some of the truncated AAT domains exhibited desired biological activity in inhibiting elastase. The results from this research demonstrated that the designer (AP) <subscript>20</subscript> module engineered in BY-2 cells could function as a molecular carrier to substantially enhance the secreted yields of the recombinant AAT.

Details

Language :
English
ISSN :
2165-5987
Volume :
10
Issue :
1
Database :
MEDLINE
Journal :
Bioengineered
Publication Type :
Academic Journal
Accession number :
30957636
Full Text :
https://doi.org/10.1080/21655979.2019.1604037