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dc.contributor.authorYuan, Y.
dc.contributor.authorWan, L.
dc.contributor.authorChen, Younan
dc.contributor.authorShi, M.
dc.contributor.authorWang, C.
dc.contributor.authorZhao, J.
dc.contributor.authorLu, X.
dc.contributor.authorWang, H.
dc.contributor.authorLu, Y.
dc.contributor.authorCheng, J.
dc.date.accessioned2017-01-30T15:10:18Z
dc.date.available2017-01-30T15:10:18Z
dc.date.created2015-10-29T04:10:13Z
dc.date.issued2013
dc.identifier.citationYuan, Y. and Wan, L. and Chen, Y. and Shi, M. and Wang, C. and Zhao, J. and Lu, X. et al. 2013. Production and characterization of human soluble CD83 fused with the fragment crystallizable region of human IgG1 in Pichia pastoris. Applied Microbiology and Biotechnology. 97 (21): pp. 9409-9417.
dc.identifier.urihttp://hdl.handle.net/20.500.11937/43816
dc.identifier.doi10.1007/s00253-013-4732-1
dc.description.abstract

The cell surface protein CD83 belongs to the immunoglobulin superfamily and is highly expressed on mature dendritic cells. The soluble form of CD83, sCD83, is a potential immune suppressor. In a previous study, recombinant soluble CD83 was expressed in Escherichia coli, resulting in a lack of functional glycosylation. Although eukaryotic cell systems for producing sCD83 offer the advantages of protein processing, folding, and posttranslational modification, these systems are complicated, expensive, and produce low levels of protein. To obtain more efficient expression of sCD83, we expressed human sCD83 fused with fragment crystallizable region of human IgG1 (hIgG1 Fc) in Pichia pastoris. Under the optimal conditions (time of induction, 48 h; inoculum density (OD 600), 80; concentration of methanol, 3.0 %; pH 7.0-8.0; concentration of casamino acid, 5.0 %), the purified human sCD83-hIgG1 Fc (hsCD83-Ig) fusion protein existed as dimers at 25-30 mg/L culture. Treatment with PNGase F showed that purified hsCD83-Ig was modified by N-linked glycosylation. Moreover, the hsCD83-Ig expressed in the P. pastoris system could suppress lymphocyte proliferation in ConA-stimulated and one-way mixed lymphocyte reaction systems. Thus, hsCD83-Ig expressed in P. pastoris is functional and may be used in experimental therapies for graft rejection, graft-versus-host disease, and autoimmune diseases. © 2013 Springer-Verlag Berlin Heidelberg.

dc.titleProduction and characterization of human soluble CD83 fused with the fragment crystallizable region of human IgG1 in Pichia pastoris
dc.typeJournal Article
dcterms.source.volume97
dcterms.source.number21
dcterms.source.startPage9409
dcterms.source.endPage9417
dcterms.source.issn0175-7598
dcterms.source.titleApplied Microbiology and Biotechnology
curtin.departmentSchool of Biomedical Sciences
curtin.accessStatusFulltext not available


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