Expression, purification and characterization of recombinant interleukin-21

Journal of Immunological Methods

Volumn 362, Issue 1-2, 2010, Pages 185-189

  Lee, Carol M Y ^a   McGuire, Helen ^a   Basten, Antony ^a,b   King, Cecile ^a,b   Christ, Daniel ^a,b  

^a GARVAN INSTITUTE OF MEDICAL RESEARCH   (Australia)

^b UNIVERSITY OF NEW SOUTH WALES   (Australia)

Author keywords

Interleukin 21; Phage display; Protein expression; Protein purification

Indexed keywords

CYTOKINE ANTIBODY; ENDOTOXIN; MONOCLONAL ANTIBODY; RECOMBINANT CYTOKINE; RECOMBINANT INTERLEUKIN 21; UNCLASSIFIED DRUG;

AFFINITY CHROMATOGRAPHY; ARTICLE; CELL INCLUSION; CELL PROLIFERATION; CONTROLLED STUDY; ESCHERICHIA COLI; GEL FILTRATION; HUMAN; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION;

ANIMALS; ANTIBODIES, MONOCLONAL; CELL LINE; CELL PROLIFERATION; CHROMATOGRAPHY, LIQUID; ESCHERICHIA COLI; GENE EXPRESSION; HUMANS; INTERLEUKINS; MICE; PRECURSOR CELLS, B-LYMPHOID; PROTEIN FOLDING; RECOMBINANT PROTEINS;

MURINAE;

EID: 77958473355     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jim.2010.08.008     Document Type: Article

References (19)

1. Asano R., Kudo T., Makabe K., Tsumoto K., Kumagai I. Antitumor activity of interleukin-21 prepared by novel refolding procedure from inclusion bodies expressed in Escherichia coli. FEBS Lett. 2002, 528:70.
2. Asano K., Ikegami H., Fujisawa T., Kawabata Y., Noso S., Hiromine Y., Ogihara T. The gene for human IL-21 and genetic susceptibility to type 1 diabetes in the Japanese. Ann. NY Acad. Sci. 2006, 1079:47.
3. Bondensgaard K., Breinholt J., Madsen D., Omkvist D.H., Kang L., Worsaae A., Becker P., Schiodt C.B., Hjorth S.A. The existence of multiple conformers of interleukin-21 directs engineering of a superpotent analogue. J. Biol. Chem. 2007, 282:23326.
4. Christ D., Famm K., Winter G. Tapping diversity lost in transformations-in vitro amplification of ligation reactions. Nucleic Acids Res. 2006, 34:e108.
5. Cole C., Barber J.D., Barton G.J. The Jpred 3 secondary structure prediction server. Nucleic Acids Res. 2008, 36:W197.
6. Fairall L., Chapman L., Moss H., de Lange T., Rhodes D. Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2. Mol. Cell 2001, 8:351.
7. Festen E.A., Goyette P., Scott R., Annese V., Zhernakova A., Lian J., Lefebvre C., Brant S.R., Cho J.H., Silverberg M.S., Taylor K.D., de Jong D.J., Stokkers P.C., McGovern D., Palmieri O., Achkar J.P., Xavier R.J., Daly M.J., Duerr R.H., Wijmenga C., Weersma R.K., Rioux J.D. Genetic variants in the region harbouring IL2/IL21 associated with ulcerative colitis. Gut 2009, 58:799.
8. Holt L.J., Bussow K., Walter G., Tomlinson I.M. By-passing selection: direct screening for antibody-antigen interactions using protein arrays. Nucleic Acids Res. 2000, 28:E72.
9. Kristensen P., Winter G. Proteolytic selection for protein folding using filamentous bacteriophages. Fold. Des. 1998, 3:321.
10. Lee C.M., Iorno N., Sierro F., Christ D. Selection of human antibody fragments by phage display. Nat. Protoc. 2007, 2:3001.
11. Liu Y., Helms C., Liao W., Zaba L.C., Duan S., Gardner J., Wise C., Miner A., Malloy M.J., Pullinger C.R., Kane J.P., Saccone S., Worthington J., Bruce I., Kwok P.Y., Menter A., Krueger J., Barton A., Saccone N.L., Bowcock A.M. A genome-wide association study of psoriasis and psoriatic arthritis identifies new disease loci. PLoS Genet. 2008, 4:e1000041.
12. Marks J.D., Hoogenboom H.R., Bonnert T.P., McCafferty J., Griffiths A.D., Winter G. By-passing immunization. Human antibodies from V-gene libraries displayed on phage. J. Mol. Biol. 1991, 222:581.
13. Ozaki K., Kikly K., Michalovich D., Young P.R., Leonard W.J. Cloning of a type I cytokine receptor most related to the IL-2 receptor beta chain. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:11439.
14. Parrish-Novak J., Dillon S.R., Nelson A., Hammond A., Sprecher C., Gross J.A., Johnston J., Madden K., Xu W., West J., Schrader S., Burkhead S., Heipel M., Brandt C., Kuijper J.L., Kramer J., Conklin D., Presnell S.R., Berry J., Shiota F., Bort S., Hambly K., Mudri S., Clegg C., Moore M., Grant F.J., Lofton-Day C., Gilbert T., Rayond F., Ching A., Yao L., Smith D., Webster P., Whitmore T., Maurer M., Kaushansky K., Holly R.D., Foster D. Interleukin 21 and its receptor are involved in NK cell expansion and regulation of lymphocyte function. Nature 2000, 408:57.
15. Tang W., Chen G., Gu Q., Pan J., Wu W. Expression, purification and identification of recombinant mouse interleukin 21 protein in E. coli. Cell. Mol. Immunol. 2006, 3:311.
16. van Heel D.A., Franke L., Hunt K.A., Gwilliam R., Zhernakova A., Inouye M., Wapenaar M.C., Barnardo M.C., Bethel G., Holmes G.K., Feighery C., Jewell D., Kelleher D., Kumar P., Travis S., Walters J.R., Sanders D.S., Howdle P., Swift J., Playford R.J., McLaren W.M., Mearin M.L., Mulder C.J., McManus R., McGinnis R., Cardon L.R., Deloukas P., Wijmenga C. A genome-wide association study for celiac disease identifies risk variants in the region harboring IL2 and IL21. Nat. Genet. 2007, 39:827.
17. Vogelzang A., King C. The modulatory capacity of interleukin-21 in the pathogenesis of autoimmune disease. Front. Biosci. 2008, 13:5304.
18. Vogelzang A., McGuire H.M., Yu D., Sprent J., Mackay C.R., King C. A fundamental role for interleukin-21 in the generation of T follicular helper cells. Immunity 2008, 29:127.
19. Yu D., Tan A.H., Hu X., Athanasopoulos V., Simpson N., Silva D.G., Hutloff A., Giles K.M., Leedman P.J., Lam K.P., Goodnow C.C., Vinuesa C.G. Roquin represses autoimmunity by limiting inducible T-cell co-stimulator messenger RNA. Nature 2007, 450:299.