論文 - 詳細
| RRC ID | 66073 |
|---|---|
| 著者 | Takashima S, Kurogochi M, Tsukimura W, Mori M, Osumi K, Sugawara SI, Amano J, Mizuno M, Takada Y, Matsuda A. |
| タイトル | Preparation and biological activities of anti-HER2 monoclonal antibodies with multibranched complex-type N-glycans. |
| ジャーナル | Glycobiology |
| Abstract |
Immunoglobulin G (IgG) has a conserved N-glycosylation site at Asn297 in the fragment crystallizable (Fc) region. Previous studies have shown that N-glycosylation of this site is a critical mediator of the antibody's effector functions, such as antibody-dependent cellular cytotoxicity. While the N-glycan structures attached to the IgG-Fc region are generally heterogenous, IgGs engineered to be homogenously glycosylated with functional N-glycans may improve the efficacy of antibodies. The major glycoforms of the N-glycans on the IgG-Fc region are bi-antennary complex-type N-glycans, while multi-branched complex-type N-glycans are not typically found. However, IgGs with tri-antennary complex-type N-glycans have been generated using the N-glycan remodeling technique, suggesting that more branched N-glycans might be artificially attached. At present, little is known about the properties of these IgGs. In this study, IgGs with multi-branched N-glycans on the Fc region were prepared by using a combination of the glycosynthase/oxazoline substrate-based N-glycan remodeling technique and successive reactions with glycosyltransferases. Among the IgGs produced by these methods, the largest N-glycan attached was a bisecting N-acetylglucosamine (GlcNAc) containing a sialylated penta-antennary structure. Concerning the Fc-mediated effector functions, the majority of IgGs with tri- and tetra-antennary N-glycans on their Fc region showed properties similar to IgGs with ordinary bi-antennary N-glycans. |
| 巻・号 | 31(10) |
| ページ | 1401-1414 |
| 公開日 | 2021-11-18 |
| DOI | 10.1093/glycob/cwab064 |
| PII | 6311236 |
| PMID | 34192331 |
| MeSH | Acetylglucosamine / immunology Humans Immunoglobulin Fc Fragments / immunology* Immunoglobulin G / immunology* Polysaccharides / immunology* Receptor, ErbB-2 / immunology* |
| IF | 4.06 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 各媒体での言及数の合計 | 0 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| ヒト・動物細胞 | 293(RCB1637) |