Differential N-Glycan modifications of human alpha 1-acid glycoprotein (α1AGP) produced in different silkworm strains using the baculovirus expression system

Daisuke Morokuma, Hiroaki Mon, Yutaka Banno, Takahiro Kusakabe, Man Lee

研究成果: ジャーナルへの寄稿記事

抄録

N-glycosylation plays an important role in various biological activities and in the structural stability of serum glycoproteins. The baculovirus expression system (BES) is widely used to produce recombinant proteins but in some case it is not suitable for medical use because of the differences in N-linked glycans between insects and mammals. We reported that human serum protein alpha 1-acid protein (α1AGP) is effectively used as a model protein for evaluating the validity of engineering the insect-type N-glycosylation pathway. Using this protein, the productivity and N-linked glycan structures were compared among the 37 different silkworm strains. Interestingly, there was no difference in N-linked glycan structure among the silkworm strains, but there was difference in the degree of N-glycosylation.

元の言語英語
ページ(範囲)49-53
ページ数5
ジャーナルJournal of Insect Biotechnology and Sericology
84
発行部数2
DOI
出版物ステータス出版済み - 11 11 2015

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Orosomucoid
Glycoproteins
Bombyx
Baculoviridae
glycosylation
silkworms
Glycosylation
Polysaccharides
glycoproteins
polysaccharides
Proteins
Insects
Acids
acids
insects
proteins
Recombinant Proteins
recombinant proteins
Recombinant proteins
blood proteins

All Science Journal Classification (ASJC) codes

  • Insect Science
  • Business, Management and Accounting(all)
  • Industrial and Manufacturing Engineering
  • Agricultural and Biological Sciences(all)
  • Biotechnology
  • Applied Microbiology and Biotechnology

これを引用

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abstract = "N-glycosylation plays an important role in various biological activities and in the structural stability of serum glycoproteins. The baculovirus expression system (BES) is widely used to produce recombinant proteins but in some case it is not suitable for medical use because of the differences in N-linked glycans between insects and mammals. We reported that human serum protein alpha 1-acid protein (α1AGP) is effectively used as a model protein for evaluating the validity of engineering the insect-type N-glycosylation pathway. Using this protein, the productivity and N-linked glycan structures were compared among the 37 different silkworm strains. Interestingly, there was no difference in N-linked glycan structure among the silkworm strains, but there was difference in the degree of N-glycosylation.",
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AU - Kusakabe, Takahiro

AU - Lee, Man

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