JP2009532477A5 - - Google Patents
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- JP2009532477A5 JP2009532477A5 JP2009504279A JP2009504279A JP2009532477A5 JP 2009532477 A5 JP2009532477 A5 JP 2009532477A5 JP 2009504279 A JP2009504279 A JP 2009504279A JP 2009504279 A JP2009504279 A JP 2009504279A JP 2009532477 A5 JP2009532477 A5 JP 2009532477A5
- Authority
- JP
- Japan
- Prior art keywords
- polypeptide
- region
- sialic acid
- polypeptides
- unpurified
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
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- 229920001184 polypeptide Polymers 0.000 claims 36
- SQVRNKJHWKZAKO-OQPLDHBCSA-N sialic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)OC1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-OQPLDHBCSA-N 0.000 claims 14
- 239000000203 mixture Substances 0.000 claims 5
- 102000003838 Sialyltransferases Human genes 0.000 claims 4
- 108090000141 Sialyltransferases Proteins 0.000 claims 4
- 230000003110 anti-inflammatory Effects 0.000 claims 4
- 108090001123 antibodies Proteins 0.000 claims 3
- 102000004965 antibodies Human genes 0.000 claims 3
- 102000004190 Enzymes Human genes 0.000 claims 2
- 108090000790 Enzymes Proteins 0.000 claims 2
- 101710015954 HVA1 Proteins 0.000 claims 2
- 108090001095 Immunoglobulin G Proteins 0.000 claims 2
- 102000004851 Immunoglobulin G Human genes 0.000 claims 2
- 101700065814 LEA2 Proteins 0.000 claims 2
- 101700021338 LEC Proteins 0.000 claims 2
- 101700077545 LECC Proteins 0.000 claims 2
- 101700028499 LECG Proteins 0.000 claims 2
- 101700063913 LECT Proteins 0.000 claims 2
- 229920001850 Nucleic acid sequence Polymers 0.000 claims 2
- 101710034340 Os04g0173800 Proteins 0.000 claims 2
- 238000001042 affinity chromatography Methods 0.000 claims 2
- 238000005571 anion exchange chromatography Methods 0.000 claims 2
- 230000003013 cytotoxicity Effects 0.000 claims 2
- 231100000135 cytotoxicity Toxicity 0.000 claims 2
- 238000004128 high performance liquid chromatography Methods 0.000 claims 2
- 101700036391 lecA Proteins 0.000 claims 2
- 239000002523 lectin Substances 0.000 claims 2
- 101700001016 mbhA Proteins 0.000 claims 2
- 150000007523 nucleic acids Chemical group 0.000 claims 2
- 108010030046 Intravenous Immunoglobulins Proteins 0.000 claims 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 claims 1
- 150000001720 carbohydrates Chemical class 0.000 claims 1
- 239000000969 carrier Substances 0.000 claims 1
- 238000006243 chemical reaction Methods 0.000 claims 1
- 239000003085 diluting agent Substances 0.000 claims 1
- 230000000694 effects Effects 0.000 claims 1
- 238000009472 formulation Methods 0.000 claims 1
- 230000002538 fungal Effects 0.000 claims 1
- 230000003899 glycosylation Effects 0.000 claims 1
- 238000006206 glycosylation reaction Methods 0.000 claims 1
- 238000000338 in vitro Methods 0.000 claims 1
- 238000004519 manufacturing process Methods 0.000 claims 1
- 238000000034 method Methods 0.000 claims 1
- 102000004169 proteins and genes Human genes 0.000 claims 1
- 108090000623 proteins and genes Proteins 0.000 claims 1
- 239000000126 substance Substances 0.000 claims 1
Claims (24)
- 少なくとも一つのＩｇＧＦｃ領域を含む精製または修飾されたポリペプチドであり、未精製または未修飾のポリペプチドと比較して、より高い抗炎症活性、より高いシアル酸含有量、およびより低い細胞毒性を有する、ポリペプチド。
- ヒトＩｇＧ１、ＩｇＧ２、ＩｇＧ３またはＩｇＧ４ Ｆｃ領域を含む、請求項１に記載のポリペプチド。
- 未精製または未修飾のポリペプチドと比較して、α−（２，６）シアル酸含有量がより高い、請求項１または２に記載のポリペプチド。
- インビトロでの抗炎症性活性が増加している、請求項１〜３のいずれか１項に記載のポリペプチド。
- インビボでの抗炎症性活性が増加している、請求項１〜４のいずれか１項に記載のポリペプチド。
- 天然に存在する抗体源由来である、請求項１〜５のいずれか１項に記載のポリペプチド。
- 組み換え抗体源由来である、請求項１〜５のいずれか１項に記載のポリペプチド。
- 未修飾または未精製のポリペプチドと比較してシアル酸含有割合が高く、前記未修飾または未精製のポリペプチドがＩＶＩＧを含む、請求項１〜７のいずれか１項に記載のポリペプチド。
- タンパク質シアル化活性が高い細胞株由来である、請求項１〜８のいずれか１項に記載のポリペプチド。
- シアル酸転移酵素を用いた処理により修飾された、請求項１〜９のいずれか１項に記載のポリペプチド。
- 前記シアル酸転移酵素がα−（２，６）シアリルトランスフェラーゼである、請求項１０に記載のポリペプチド。
- 精製されている、請求項１〜１１のいずれか１項に記載のポリペプチド。
- 適切なキャリアーまたは希釈剤と組み合わせて請求項１〜１２のいずれか１項に記載のポリペプチドを含む製剤。
- 少なくとも一つのＦｃ領域を含む精製または修飾されたポリペプチドの製造方法であって、前記ポリペプチドが未精製または未修飾のポリペプチドより高い抗炎症活性、高いシアル酸含有量、および低い細胞毒性を有し、
少なくとも一つのＦｃ領域を含むポリペプチドの未精製または未修飾の源を提供し、ここで、前記少なくとも一つのＦｃ領域を含むポリペプチドの未精製または未修飾の源は、シアル酸を有する少なくとも一つのＦｃ領域を含むポリペプチドの複数およびシアル酸を欠く少なくとも一つのＦｃ領域を有するポリペプチドの複数を含み；そして
シアル酸を欠く少なくとも一つのＦｃ領域を含むポリペプチドの複数に対する、シアル
酸を含む少なくとも一つのＦｃ領域を含むポリペプチドの複数の比率を増加させる、
ことを含む、方法。 - 前記少なくとも一つのＦｃ領域を含むポリペプチドの源がヒトＩｇＧ抗体を含む、請求項１４に記載の方法。
- 前記少なくとも一つのＦｃ領域を含むポリペプチドの源が、発現系で核酸配列を含むベクターを発現させることにより提供され、ここで前記核酸配列がＩｇＧ抗体に翻訳される、請求項１４または１５に記載の方法。
- 前記発現系が、菌の、植物の、脊椎動物のおよび無脊椎動物の発現系、およびこれらの組み合わせからなる群から選択されるＮ−結合グリコシル化ができる修飾されたホスト発現系を含む、請求項１６に記載の方法。
- シアル酸を欠く少なくとも一つのＦｃ領域を含むポリペプチドの複数に対する、シアル酸を含む少なくとも一つのＦｃ領域を含むポリペプチドの複数の比率を増加させる段階が、シアル酸を欠く少なくとも一つのＦｃ領域を含むポリペプチドの除去を通じて達成される、請求項１４〜１７のいずれか１項に記載の方法。
- 前記除去が物理的または化学的方法により達成される、請求項１８に記載の方法。
- 前記除去が、ＨＰＬＣ、レクチンアフィニティクロマトグラフィー、高ｐＨアニオン交換クロマトグラフィー、およびこれらの組み合わせからなる群から選ばれる方法によって達成される、請求項１８または１９に記載の方法。
- シアル酸を欠く少なくとも一つのＦｃ領域を含むポリペプチドの複数に対する、シアル酸を含む少なくとも一つのＦｃ領域を含むポリペプチドの複数の比率を増加させる段階が、前記少なくとも一つのＦｃ領域を含むポリペプチドの未精製源の濃縮を通じて達成される、請求項１４〜２０のいずれか１項に記載の方法。
- 前記濃縮が、ＨＰＬＣ、レクチンアフィニティクロマトグラフィー、高ｐＨアニオン交換クロマトグラフィー、およびこれらの組み合わせからなる群から選ばれる方法によって達成される、請求項２１に記載の方法。
- 前記シアル化が、少なくとも一つのＦｃ領域を含むポリペプチドに付加された糖質に対
して、シアル酸を付加する酵素を用いた化学反応によって達成される、請求項２１または２２に記載の方法。 - 前記酵素がα−（２，６）シアリルトランスフェラーゼである、請求項２３に記載の方法。
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US78938406P | 2006-04-05 | 2006-04-05 | |
| US60/789,384 | 2006-04-05 | ||
| PCT/US2007/008396 WO2007117505A2 (en) | 2006-04-05 | 2007-04-03 | Polypeptides with enhanced anti-inflammatory and decreased cytotoxic properties and relating methods |
Related Child Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2014182741A Division JP2015038086A (ja) | 2006-04-05 | 2014-09-08 | 抗炎症特性が増強され、細胞毒性特性が減少したポリペプチドおよび関連する方法 |
| JP2016114709A Division JP6322849B2 (ja) | 2006-04-05 | 2016-06-08 | 抗炎症特性が増強され、細胞毒性特性が減少したポリペプチドおよび関連する方法 |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2009532477A JP2009532477A (ja) | 2009-09-10 |
| JP2009532477A5 true JP2009532477A5 (ja) | 2010-05-13 |
| JP6084761B2 JP6084761B2 (ja) | 2017-02-22 |
Family
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Family Applications (6)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2009504279A Active JP6084761B2 (ja) | 2006-04-05 | 2007-04-03 | 抗炎症特性が増強され、細胞毒性特性が減少したポリペプチドおよび関連する方法 |
| JP2014182741A Pending JP2015038086A (ja) | 2006-04-05 | 2014-09-08 | 抗炎症特性が増強され、細胞毒性特性が減少したポリペプチドおよび関連する方法 |
| JP2016114709A Active JP6322849B2 (ja) | 2006-04-05 | 2016-06-08 | 抗炎症特性が増強され、細胞毒性特性が減少したポリペプチドおよび関連する方法 |
| JP2018053298A Active JP6686058B2 (ja) | 2006-04-05 | 2018-03-20 | 抗炎症特性が増強され、細胞毒性特性が減少したポリペプチドおよび関連する方法 |
| JP2020065891A Active JP6989979B2 (ja) | 2006-04-05 | 2020-04-01 | 抗炎症特性が増強され、細胞毒性特性が減少したポリペプチドおよび関連する方法 |
| JP2021192123A Active JP7357382B2 (ja) | 2006-04-05 | 2021-11-26 | 抗炎症特性が増強され、細胞毒性特性が減少したポリペプチドおよび関連する方法 |
Family Applications After (5)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2014182741A Pending JP2015038086A (ja) | 2006-04-05 | 2014-09-08 | 抗炎症特性が増強され、細胞毒性特性が減少したポリペプチドおよび関連する方法 |
| JP2016114709A Active JP6322849B2 (ja) | 2006-04-05 | 2016-06-08 | 抗炎症特性が増強され、細胞毒性特性が減少したポリペプチドおよび関連する方法 |
| JP2018053298A Active JP6686058B2 (ja) | 2006-04-05 | 2018-03-20 | 抗炎症特性が増強され、細胞毒性特性が減少したポリペプチドおよび関連する方法 |
| JP2020065891A Active JP6989979B2 (ja) | 2006-04-05 | 2020-04-01 | 抗炎症特性が増強され、細胞毒性特性が減少したポリペプチドおよび関連する方法 |
| JP2021192123A Active JP7357382B2 (ja) | 2006-04-05 | 2021-11-26 | 抗炎症特性が増強され、細胞毒性特性が減少したポリペプチドおよび関連する方法 |
Country Status (13)
| Country | Link |
|---|---|
| US (14) | US10167332B2 (ja) |
| EP (3) | EP2010566B2 (ja) |
| JP (6) | JP6084761B2 (ja) |
| CN (1) | CN101432301B (ja) |
| AU (1) | AU2007235413B2 (ja) |
| CA (1) | CA2647524C (ja) |
| EA (1) | EA022780B1 (ja) |
| HK (1) | HK1124074A1 (ja) |
| IL (1) | IL194526A (ja) |
| MX (1) | MX2008012843A (ja) |
| NZ (1) | NZ572379A (ja) |
| WO (1) | WO2007117505A2 (ja) |
| ZA (1) | ZA200808900B (ja) |
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