Expression of the functional recombinant human glycosyltransferase GalNAcT2 in Escherichia coli

Microbial Cell Factories

Volumn 14, Issue 1, 2015, Pages

  Lauber, Jennifer ^a   Handrick, René ^a   Leptihn, Sebastian ^b   Dürre, Peter ^c   Gaisser, Sabine ^a  

^a BIBERACH UNIVERSITY OF APPLIED SCIENCES   (Germany)

^b UNIVERSITY OF HOHENHEIM   (Germany)

^c UNIVERSITY OF ULM   (Germany)

Author keywords

Enzymatic activity glycosyltransferase; Erv1p PDI co expression; Escherichia coli; Filgrastim; Glycosyltransferase GalNAcT2; In vitro glycosylation; Protein expression; Recombinant glycosyltransferase; Secondary structure glycosyltransferase

Indexed keywords

GLYCOSYLTRANSFERASE; POLYHISTIDINE TAG; POLYPEPTIDE N ACETYLGALACTOSAMINYLTRANSFERASE 2; UNCLASSIFIED DRUG; GRANULOCYTE COLONY STIMULATING FACTOR; HIS-HIS-HIS-HIS-HIS-HIS; HISTIDINE; HYBRID PROTEIN; N ACETYLGALACTOSAMINYLTRANSFERASE; OLIGOPEPTIDE; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE;

AFFINITY CHROMATOGRAPHY; ARTICLE; CIRCULAR DICHROISM; CODON; COLORIMETRY; CYTOPLASM; ELECTROSPRAY MASS SPECTROMETRY; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; GLYCOSYLATION; LIGHT SCATTERING; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; PROTEIN EXPRESSION; PROTEIN SECONDARY STRUCTURE; AMINO ACID SEQUENCE; BIOSYNTHESIS; CHEMISTRY; GENE VECTOR; GENETICS; HUMAN; IMMUNOBLOTTING; ISOLATION AND PURIFICATION; MASS SPECTROMETRY; METABOLISM; MOLECULAR GENETICS; MOLECULAR WEIGHT; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN FOLDING; SIZE EXCLUSION CHROMATOGRAPHY;

ESCHERICHIA COLI; HEXAPODA; MAMMALIA;

AMINO ACID SEQUENCE; CHROMATOGRAPHY, AFFINITY; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; COLORIMETRY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; GENETIC VECTORS; GLYCOSYLATION; GRANULOCYTE COLONY-STIMULATING FACTOR; HISTIDINE; HUMANS; IMMUNOBLOTTING; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; N-ACETYLGALACTOSAMINYLTRANSFERASES; OLIGOPEPTIDES; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 84924064692     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/s12934-014-0186-0     Document Type: Article

References (38)

1. Skretas G, Carroll S, DeFrees S, Schwartz MF, Johnson KF, Georgiou G. Expression of active human sialyltransferase ST6GalNAcI in Escherichia coli. Microb Cell Fact. 2009;8:50.
2. Walsh G, Jefferis R. Post-translational modifications in the context of therapeutic proteins. Nat Biotechnol. 2006;24:1241-52.
3. Lobstein J, Emrich CA, Jeans C, Faulkner M, Riggs P, Berkmen M. SHuffle, a novel Escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasm. Microb Cell Fact. 2012;11:56.
4. Huang CJ, Lin H, Yang X. Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements. J Ind Microbiol Biotechnol. 2012;39:383-99.
5. Demain AL, Vaishnav P. Production of recombinant proteins by microbes and higher organisms. Biotechnol Adv. 2009;27:297-306.
6. Merritt JH, Ollis AA, Fisher AC, DeLisa MP. Glycans-by-design: engineering bacteria for the biosynthesis of complex glycans and glycoconjugates. Biotechnol Bioeng. 2013;110:1550-64.
7. Nothaft H, Szymanski CM. Protein glycosylation in bacteria: sweeter than ever. Nat Rev Microbiol. 2010;8:765-78.
8. White T, Bennett EP, Takio K, Sorensen T, Bonding N, Clausen H. Purification and cDNA cloning of a human UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. J Biol Chem. 1995;270:24156-65.
9. Wildt S, Gerngross TU. The humanization of N-glycosylation pathways in yeast. Nat Rev Microbiol. 2005;3:119-28.
10. Fritz TA, Raman J, Tabak LA. Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferase-2. J Biol Chem. 2005;281:8613-9.
11. Schwarz F, Huang W, Li C, Schulz BL, Lizak C, Palumbo A, et al. A combined method for producing homogeneous glycoproteins with eukaryotic N-glycosylation. Nat Chem Biol. 2010;6:264-6.
12. Walsh G. Post-translational modifications of protein biopharmaceuticals. Drug Discov Today. 2010;15:773-80.
13. Valderrama-Rincon JD, Fisher AC, Merritt JH, Fan YY, Reading CA, Chhiba K, et al. An engineered eukaryotic protein glycosylation pathway in Escherichia coli. Nat Chem Biol. 2012;8:434-6.
14. Iwashkiw JA, Seper A, Weber BS, Scott NE, Vinogradov E, Stratilo C, et al. Identification of a general O-linked protein glycosylation system in Acinetobacter baumannii and its role in virulence and biofilm formation. PLoS Pathog. 2012;8:e1002758.
15. Faridmoayer A, Fentabil MA, Haurat MF, Yi W, Woodward R, Wang PG, et al. Extreme substrate promiscuity of the Neisseria oligosaccharyl transferase involved in protein O-glycosylation. J Biol Chem. 2008;283:34596-604.
16. Nguyen VD, Hatahet F, Salo KE, Enlund E, Zhang C, Ruddock LW. Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E. coli. Microb Cell Fact. 2011;10:1.
17. Hatahet F, Ruddock LW. Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation. Antioxid Redox Signal. 2009;11:2807-50.
18. Taus C, Lucini C, Sato T, Furukawa K, Grabherr R, Staudacher E. Expression and characterization of the first snail-derived UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. Glycoconj J. 2013;30:825-33.
19. Ten Hagen KG, Fritz TA, Tabak LA. All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases. Glycobiology. 2003;13:1R-6.
20. Sorensen T, White T, Wandall HH, Kristensen AK, Roepstorff P, Clausen H. UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. Identification and separation of two distinct transferase activities. J Biol Chem. 1995;270:24166-73.
21. Wandall HH, Hassan H, Mirgorodskaya E, Kristensen AK, Roepstorff P, Bennett EP, et al. Substrate specificities of three members of the human UDP-N-acetyl-α-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3. J Biol Chem. 1997;272:23503-14.
22. DeFrees S, Wang ZG, Xing R, Scott AE, Wang J, Zopf D, et al. GlycoPEGylation of recombinant therapeutic proteins produced in Escherichia coli. Glycobiology. 2006;16:833-43.
23. Johnson Jr WC. Protein secondary structure and circular dichroism: a practical guide. Proteins. 1990;7:205-14.
24. Kelly SM, Price NC. The application of circular dichroism to studies of protein folding and unfolding. Biochim Biophys Acta. 1997;1338:161-85.
25. Wu ZL. Phosphatase-coupled universal kinase assay and kinetics for first-order-rate coupling reaction. PLoS One. 2011;6:e23172.
26. Albone EF, Hagen FK, VanWuyckhuyse BC, Tabak LA. Molecular cloning of a rat submandibular gland apomucin. J Biol Chem. 1994;269:16845-52.
27. Pratt MR, Hang HC, Ten Hagen KG, Rarick J, Gerken TA, Tabak LA, et al. Deconvoluting the functions of polypeptide N-α-acetylgalactosaminyltransferase family members by glycopeptide substrate profiling. Chem Biol. 2004;11:1009-16.
28. Faulkner MJ, Veeravalli K, Gon S, Georgiou G, Beckwith J. Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways. Proc Natl Acad Sci U S A. 2008;105:6735-40.
29. Krause M, Ukkonen K, Haataja T, Ruottinen M, Glumoff T, Neubauer A, et al. A novel fed-batch based cultivation method provides high cell-density and improves yield of soluble recombinant proteins in shaken cultures. Microb Cell Fact. 2010;9:11.
30. Panula-Perala J, Siurkus J, Vasala A, Wilmanowski R, Casteleijn MG, Neubauer P. Enzyme controlled glucose auto-delivery for high cell density cultivations in microplates and shake flasks. Microb Cell Fact. 2008;7:31.
31. Ukkonen K, Vasala A, Ojamo H, Neubauer P. High-yield production of biologically active recombinant protein in shake flask culture by combination of enzyme-based glucose delivery and increased oxygen transfer. Microb Cell Fact. 2011;10:107.
32. Horynova M, Takahashi K, Hall S, Renfrow MB, Novak J, Raska M. Production of N-acetylgalactosaminyl-transferase 2 (GalNAc-T2) fused with secretory signal Igκ in insect cells. Protein Expr Purif. 2012;81:175-80.
33. Gomez H, Rojas R, Patel D, Tabak LA, Lluch JM, Masgrau L. A computational and experimental study of O-glycosylation. Catalysis by human UDP-GalNAc polypeptide:GalNAc transferase-T2. Org Biomol Chem. 2014;12:2645-55.
34. Hoglund M. Glycosylated and non-glycosylated recombinant human granulocyte colony-stimulating factor (rhG-CSF)-what is the difference? Med Oncol. 1998;15:229-33.
35. Gascon P. Presently available biosimilars in hematology-oncology: G-CSF. Target Oncol. 2012;7 Suppl 1:S29-34.
36. Oh-eda M, Hasegawa M, Hattori K, Kuboniwa H, Kojima T, Orita T, et al. O-linked sugar chain of human granulocyte colony-stimulating factor protects it against polymerization and denaturation allowing it to retain its biological activity. J Biol Chem. 1990;265:11432-5.
37. Sambrock J, Fritsch EF, Maniatis T. Molecular Cloning: A Laboratory Manual. 2nd ed. New-York: Cold Spring Harbor Laboratory Press; 1989.
38. Krishna Rao DV, Rao JV, Narasu ML, Bhujanga Rao AK. Optimization of the AT-content of codons immediately downstream of the initiation codon and evaluation of culture conditions for high-level expression of recombinant human G-CSF in Escherichia coli. Mol Biotechnol. 2008;38:221-32.