Human alpha 1-acid glycoprotein as a model protein for glycoanalysis in baculovirus expression vector system

Daisuke Morokuma, Jian Xu, Hiroaki Mon, Kazuma Hirata, Masato Hino, Shoko Kuboe, Mami Yamashita, Takahiro Kusakabe, Jae Man Lee

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Glycosylation is an important post-translational modification that confers various biological activities, structural stability, and inter-molecular interactions to proteins. Baculovirus expression vector system (BEVS) is widely used to produce recombinant glycoproteins, which may not be suitable for clinical use due to differences in the N-linked glycan structure between insects and mammals. It is necessary to develop an appropriate model protein-base platform for glycoanalysis to engineer the insect-type N-glycosylation pathway into human type efficiently. In this study, we employed human plasma protein alpha 1-acid glycoprotein (α1AGP). It was highly secreted from cultured silkworm cells and larvae when using the BEVS and glycosylated with insect type N-linked glycans. Interestingly, when separated on SDS-PAGE, the purified recombinant α1AGP secreted into silkworm haemolymph generated six distinct products from three alternative translates, suggesting that α1AGP has variations for the recognition or choice of glycosylation sites.

元の言語英語
ページ(範囲)303-309
ページ数7
ジャーナルJournal of Asia-Pacific Entomology
18
発行部数2
DOI
出版物ステータス出版済み - 6 1 2015

All Science Journal Classification (ASJC) codes

  • Insect Science

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