| RRC ID |
57033
|
| Author |
Morokuma D., Hino M., Tsuchioka M., Masuda A., Mon H., Fujiyama K., Kajiura H., Kusakabe T. and Lee J.M.
|
| Title |
A truncated form of human alpha 1-acid glycoprotein is useful as a molecular tool for insect glycobiology.
|
| Journal |
Int. J. Indust. Entomol.
|
| Abstract |
N -glycosylation is an important posttranslational modification that results in a variety of biological activities, structural stability, and protein-protein interactions. There are still many mysteries in the structure and function of N-glycans, and detailed elucidation is necessary. Baculovirus expression system (BES) is widely used to produce recombinant glycoproteins, but it is not suitable for clinical use due to differences in N-glycan structure between insects and mammals. It is necessary to develop adequate model glycoproteins for analysis to efficiently alter the insect-type N-glycosylation pathway to human type. The previous research shows the recombinant alpha 1-acid glycoprotein (a1AGP) secreted from silkworm cultured cells or larvae is highly glycosylated and expected to be an excellent research candidate for the glycoprotein analysis expressed by BES. Therefore, we improved the a1AGP to be a better model for studying glycosylation. The modified a1AGP (a1AGPΔ) recombinant protein was successfully expressed and purified by using BES, however, the expression level in silkworm cultured cells and larvae were lower than that of the a1AGP. Subsequently, we confirmed the detailed profile of N-glycan on the a1AGPΔ by LS/MS analysis the N-glycan structure at each glycosylation site. These results indicated that the recombinant a1AGPΔ could be usable as a better model glycoprotein of N-glycosylation research in BES.
|
| Volume |
36(1)
|
| Pages |
15-24
|
| Published |
2018-3-31
|
| DOI |
10.7852/ijie.2018.36.1.15
|
| Resource |
| Silkworms |
n17 |
