Scientia Agricultura Sinica ›› 2005, Vol. 38 ›› Issue (05): 1034-1039 .doi: 10.3864/j.issn.0578-1752.at-2004-2889

• ANIMAL SCIENCE·VETERINARY SCIENCERE·SOURCE INSECT • Previous Articles     Next Articles

In vitro Expression and Bioactivity of Chicken Interleukin-2

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  1. 浙江大学动物预防医学研究所病毒与免疫研究室
  • Received:2004-10-28 Revised:1900-01-01 Online:2005-05-10 Published:2005-05-10

Abstract: In this study, the recombinant chicken interleukin-2 (rchIL-2) was successfully produced in the pBAD/His B expression system induced by L-(+)-arabinose. By SDS-PAGE analysis, the observed molecular weight of rchIL-2 fusion protein without the signal peptide was 18 kD. Monoclonal and polyclonal antibodies specific for rchIL-2 were produced. These antibodies were used to develop a mAb-based antigen capture ELISA (AC-ELISA). Based on the constructed AC-ELISA, in vitro kinetics of endogenous chicken IL-2 production were detected. The soluble rchIL-2 protein purified under native conditions was shown to activate the proliferation of chicken lymphocytes stimulated by Con A for 24 h in a dose-dependent manner. This activity cannot be neutralized by mAbs to chIL-2, but can be neutralized by anti-chIL-2 polyclonal antibody. These results demonstrated that the E.coli-derived rchIL-2 and polyclonal antibody to chIL-2 have bioactivity.

Key words: Chicken, Interleukin-2, Bioactivity, Monoclonal antibody, Polyclonal antibody, Ag capture ELISA

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