Expression of Chicken Interleukin-2 in Insect Cells

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Min-Jie Cao^*, Guo-Ping Wu, Chuan Guo, and Wen-Jin Su

College of Biological Engineering, Jimei University, Jimei, Xiamen, China, 361021; fax: +86-592-6180-470; E-mail: caomj@suntar.com; mjcao@jmu.edu.cn

^* To whom correspondence should be addressed.

Received November 22, 2004

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Full-length chicken interleukin-2 (ChIL-2) protein was successfully expressed using the recombinant baculovirus/Sf9 insect cell system. The expressed protein was soluble and reached approximately 12 µg/ml. Similarly to native ChIL-2, baculovirus expressed ChIL-2 revealed two main bands corresponding to molecular masses of 22 and 20 kD as detected by SDS-PAGE and Western blot. Treatment of the expressed protein with N-endoglycosidase F for 2 h caused the complete disappearance of the 22 kD band, while the 20 kD band (which is close to the molecular weight predicted from the cloned cDNA sequence) remained unchanged. Together with results on native ChIL-2, it can be concluded that ChIL-2 is an N-glycosylated protein.

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KEY WORDS: chicken, glycosylation, interleukin-2, monoclonal antibody

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