Earticle

초록

영어

Previously, we showed that simple paucimannosidic N-glycan structures in insect Drosophila S2 cells arise mainly because of β -Nacetylglucosaminidase (GlcNAcase) action, which removes terminal N-acetylglucosamine (GlcNAc) residues. In an earlier report, we suppressed GlcNAcase activity and clearly demonstrated that more complex N-glycanswithtwo terminal GlcNAc residues were synthesized.
In the present work, we investigated synergistic effects of Nacetylglucosaminyltransferase II and/or β-1,4-galactosyltransferase co-expressions (by recombinant baculoviral infection) and GlcNAcase suppression (by knock-out screening) on N-glycan patterns. Using HPLC and MALDI-TOF MS analyses, we found that the N-glycosylation pattern of human erythropoietin secreted by engineered S2 cells expressing glycosyltransferase but not GlcNAcase was complete except for sialylation; N-glycan structures had two terminal galactose residues.
Therefore, it will be possible to express complete functional human therapeutic glycoprotein in engineered Drosophila cells by suppressing GlcNAcase and co-expressing additional glycosyltransferases of N-glycosylation pathway.

저자

• Hyung Joon CHA [ Department of chemical Engineering, Pohang University of Science and Technology, Pohang 790-784, Korea. ]
• Kyoung Ro KIM [ Department of chemical Engineering, Pohang University of Science and Technology, Pohang 790-784, Korea. ]
• Yeon Kyu KIM [ Department of chemical Engineering, Pohang University of Science and Technology, Pohang 790-784, Korea. ]
• Dong Gyun KANG [ Department of chemical Engineering, Pohang University of Science and Technology, Pohang 790-784, Korea. ]

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간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576