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

References

• Blank CA, Brantly M. Clinical features and molecular characteristics of alpha 1-antitrypsin deficiency. Ann Allergy. 1994;72(2): 105–120.
   Google Scholar
• Brode SK, Ling SC, Chapman KR. Alpha-1 antitrypsin deficiency: a commonly overlooked cause of lung disease. CMAJ. 2012;184(12):1365–1371.
   Google Scholar
• Alkins SA, O‘Malley P. Should health-care systems pay for replacement therapy in patients with alpha(1)-antitrypsin deficiency? A critical review and cost-effectiveness analysis. Chest. 2000;117(3):875–880.
   Google Scholar
• Krishnan B, Hedstrom L, Hebert DN, et al. Expression and purification of active recombinant human alpha-1 antitrypsin (aat) from Escherichia coli. Methods Mol Biol. 2017;1639:195–209.
   Google Scholar
• Khatami M, Hosseini SN, Hasannia S. Co-expression of alpha-1 antitrypsin with cytoplasmic domain of v-SNARE in Pichia pastoris: preserving biological activity of alpha-1 antitrypsin. Biotechnol Appl Biochem. 2018;65(2):181-187.
   Google Scholar
• Paterson T, Innes J, Moore S. Approaches to maximizing stable expression of alpha 1-antitrypsin in transformed CHO cells. Appl Microbiol Biotechnol. 1994;40(5):691–698.
   Google Scholar
• Castilho A, Windwarder M, Gattinger P, et al. Proteolytic and N-glycan processing of human alpha1-antitrypsin expressed in Nicotiana benthamiana. Plant Physiol. 2014;166(4):1839–1851.
   Google Scholar
• Agarwal S, Singh R, Sanyal I, et al. Expression of modified gene encoding functional human alpha-1-antitrypsin protein in transgenic tomato plants. Transgenic Res. 2008;17(5):881–896.
   Google Scholar
• Nadai M, Bally J, Vitel M, et al. High-level expression of active human alpha1-antitrypsin in transgenic tobacco chloroplasts. Transgenic Res. 2009;18(2):173–183.
   Google Scholar
• Hellwig S, Drossard J, Twyman RM, et al. Plant cell cultures for the production of recombinant proteins. Nat Biotechnol. 2004;22(11):1415–1422.
   Google Scholar
• Huang TK, McDonald KA. Bioreactor engineering for recombinant protein production in plant cell suspension cultures. Biochem Eng J. 2009;45:168–184.
   Google Scholar
• Santos RB, Abranches R, Fischer R, et al. Putting the spotlight back on plant suspension cultures. Front Plant Sci. 2016;7:297.
   Google Scholar
• Xu J, Dolan MC, Medrano G, et al. Green factory: plants as bioproduction platforms for recombinant proteins. Biotechnol Adv. 2012;30(5):1171–1184.
   Google Scholar
• Terashima M, Murai Y, Kawamura M, et al. Production of functional human alpha 1-antitrypsin by plant cell culture. Appl Microbiol Biotechnol. 1999;52(4):516–523.
   Google Scholar
• Huang J, Sutliff TD, Wu L, et al. Expression and purification of functional human alpha-1-antitrypsin from cultured plant cells. Biotechnol Prog. 2001;17(1):126-133.
   Google Scholar
• Trexler MM, McDonald KA, Jackman AP. Bioreactor production of human alpha(1)-antitrypsin using metabolically regulated plant cell cultures. Biotechnol Prog. 2002;18(3):501–508.
   Google Scholar
• McDonald KA, Hong LM, Trombly DM, et al. Production of human alpha-1-antitrypsin from transgenic rice cell culture in a membrane bioreactor. Biotechnol Prog. 2005;21(3):728-734.
   Google Scholar
• Xu J, Ge X, Dolan MC. Towards high-yield production of pharmaceutical proteins with plant cell suspension cultures. Biotechnol Adv. 2011;29(3):278–299.
   Google Scholar
• Kieliszewski MJ, Xu J, Meyer G (2015) Nucleic acid for plant expression of a fusion protein comprising hydroxyproline O-glycosylation glycomodule. US Patent No. 9006410
   Google Scholar
• Xu J, Okada S, Tan L, et al. Human growth hormone expressed in tobacco cells as an arabinogalactan-protein fusion glycoprotein has a prolonged serum life. Transgenic Res. 2010;19(5):849–867.
   Google Scholar
• Xu J, Tan L, Goodrum KJ, et al. High-yields and extended serum half-life of human interferon alpha2b expressed in tobacco cells as arabinogalactan-protein fusions. Biotechnol Bioeng. 2007;97(5):997–1008.
   Google Scholar
• Xu J, Tan L, Lamport DTA, et al. The O-Hyp glycosylation code in tobacco and Arabidopsis and a proposed role of Hyp-glycans in secretion. Phytochem. 2008;69(8):1631–1640.
   Google Scholar
• Kieliszewski MJ, Shpak E. Synthetic genes for the elucidation of glycosylation codes for arabinogalactan-proteins and other hydroxyproline-rich glycoproteins. Cell Mol Life Sci. 2001;58(10):1386–1398.
   Google Scholar
• Zhang N, Gonzalez M, Savary B, et al. High-yield secretion of recombinant proteins expressed in tobacco cell culture with a designer glycopeptide tag: process development. Biotechnol J. 2016b;11(4):497–506.
   Google Scholar
• Ramos-Martinez EM, Fimognari L, Sakuragi Y. High-yield secretion of recombinant proteins from the microalga Chlamydomonas reinhardtii. Plant Biotechnol J. 2017;15(9):1214–1224.
   Google Scholar
• Tan L, Varnai P, Lamport DTA, et al. Plant O-hydroxyproline arabinogalactans are composed of repeating trigalactosyl subunits with short bifurcated side chains. J Biol Chem. 2010;285(32):24575–24583.
   Google Scholar
• Tan L, Leykam JF, Kieliszewski MJ. Glycosylation motifs that direct arabinogalactan addition to arabinogalactan-proteins. Plant Physiol. 2003;132(3):1362–1369.
   Google Scholar
• Kieliszewski MJ. The latest hype on Hyp-O-glycosylation codes. Phytochem. 2001;57(3):319–323.
   Google Scholar
• Showalter AM. Structure and function of plant cell wall proteins. Plant Cell. 1993;5(1):9–23.
   Google Scholar
• Shpak E, Leykam JF, Kieliszewski MJ. Synthetic genes for glycoprotein design and the elucidation of hydroxyproline-O-glycosylation codes. Proc Natl Acad Sci USA. 1999;96(26):14736–14741.
   Google Scholar
• An G. High efficiency transformation of cultured tobacco cells. Plant Physiol. 1985;79(2):568–570.
   Google Scholar
• Schenk RU, Hildebrandt AC. Medium and techniques for induction and growth of monocotyledonous and dicotyledonous plant cell cultures. Can J Bot. 1972;50:199–204.
   Google Scholar
• Zhang N, Dolan M, Wu D, et al. Dramatic secretion of recombinant protein expressed in tobacco cells with a designer glycopeptide tag is highly impacted by medium composition. Plant Cell Rep. 2016a;35(12):2513–2522.
   Google Scholar
• Xu J, Kieliszewski M. Enhanced accumulation of secreted human growth hormone by transgenic tobacco cells correlates with the introduction of an N-glycosylation site. J Biotechnol. 2011;154(1):54–59.
   Google Scholar
• Shpak E, Barbar E, Leykam JF, et al. Contiguous hydroxyproline residues direct hydroxyproline arabinosylation in Nicotiana tabacum. J Biol Chem. 2001;276(14):11272–11278.
   Google Scholar
• Kolarich D, Weber A, Turecek PL, et al. Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms. Proteomics. 2006;6(11):3369–3380.
   Google Scholar
• Kitazawa K, Tryfona T, Yoshimi Y, et al. beta-galactosyl Yariv reagent binds to the beta-1,3-galactan of arabinogalactan proteins. Plant Physiol. 2013;161(3):1117–1126.
   Google Scholar
• Travis J, Salvesen GS. Human plasma proteinase inhibitors. Annu Rev Biochem. 1983;52:655–709.
   Google Scholar