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

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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.

Original languageEnglish
Pages (from-to)49-53
Number of pages5
JournalJournal of Insect Biotechnology and Sericology
Volume84
Issue number2
DOIs
Publication statusPublished - Nov 11 2015

All Science Journal Classification (ASJC) codes

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

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