MX2015012361A - Metodos de fabricacion para controlar el contenido de lisina c-terminal, galactosa y acido sialico en proteinas recombinantes. - Google Patents
Metodos de fabricacion para controlar el contenido de lisina c-terminal, galactosa y acido sialico en proteinas recombinantes.Info
- Publication number
- MX2015012361A MX2015012361A MX2015012361A MX2015012361A MX2015012361A MX 2015012361 A MX2015012361 A MX 2015012361A MX 2015012361 A MX2015012361 A MX 2015012361A MX 2015012361 A MX2015012361 A MX 2015012361A MX 2015012361 A MX2015012361 A MX 2015012361A
- Authority
- MX
- Mexico
- Prior art keywords
- sialic acid
- acid content
- terminal lysine
- galactose
- control
- Prior art date
Links
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 title abstract 2
- 239000004472 Lysine Substances 0.000 title abstract 2
- SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Chemical group CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 0.000 title abstract 2
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 title abstract 2
- 238000004519 manufacturing process Methods 0.000 title abstract 2
- SQVRNKJHWKZAKO-OQPLDHBCSA-N sialic acid Chemical group 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 title abstract 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 title 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 title 1
- WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical group OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 title 1
- 229930182830 galactose Chemical group 0.000 title 1
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 abstract 3
- 239000011701 zinc Substances 0.000 abstract 3
- 229910052725 zinc Inorganic materials 0.000 abstract 3
- 239000001963 growth medium Substances 0.000 abstract 2
- 210000004899 c-terminal region Anatomy 0.000 abstract 1
- 210000004027 cell Anatomy 0.000 abstract 1
- 238000012258 culturing Methods 0.000 abstract 1
- 229960000598 infliximab Drugs 0.000 abstract 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/24—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
- C07K16/241—Tumor Necrosis Factors
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/10—Immunoglobulins specific features characterized by their source of isolation or production
- C07K2317/14—Specific host cells or culture conditions, e.g. components, pH or temperature
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/40—Immunoglobulins specific features characterized by post-translational modification
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/40—Immunoglobulins specific features characterized by post-translational modification
- C07K2317/41—Glycosylation, sialylation, or fucosylation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/52—Constant or Fc region; Isotype
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/54—F(ab')2
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/55—Fab or Fab'
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Biophysics (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Immunology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Peptides Or Proteins (AREA)
- Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Microbiology (AREA)
Abstract
En la presente se proporciona un método para producir un anticuerpo, como un anticuerpo anti-TNFa (por ejemplo, infliximab) que tiene un contenido de lisina en el extremo C terminal de aproximadamente 20% a aproximadamente 70%, y un contendido de ácido siálico de aproximadamente 1% a aproximadamente 20%, que comprende cultivar una célula huésped sensible al zinc transfectada con ADN que codifica el anticuerpo en un medio de cultivo que comprende por lo menos 0.5 µM de zinc; y controlar la concentración de zinc en el medio de cultivo, para producir así el anticuerpo.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201361791094P | 2013-03-15 | 2013-03-15 | |
| PCT/US2014/021574 WO2014149935A1 (en) | 2013-03-15 | 2014-03-07 | Manufacturing methods to control c-terminal lysine, galactose and sialic acid content in recombinant proteins |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| MX2015012361A true MX2015012361A (es) | 2016-04-28 |
| MX366910B MX366910B (es) | 2019-07-30 |
Family
ID=51528780
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| MX2015012361A MX366910B (es) | 2013-03-15 | 2014-03-07 | Metodos de fabricacion para controlar el contenido de lisina c-terminal, galactosa y acido sialico en proteinas recombinantes. |
Country Status (27)
| Country | Link |
|---|---|
| US (3) | US20140273092A1 (es) |
| EP (1) | EP2970980B2 (es) |
| JP (1) | JP2016512029A (es) |
| KR (1) | KR102216003B1 (es) |
| CN (1) | CN105378086B (es) |
| AR (2) | AR095660A1 (es) |
| AU (2) | AU2014237635B2 (es) |
| BR (1) | BR112015022971B1 (es) |
| CA (1) | CA2907140A1 (es) |
| CY (1) | CY1120980T1 (es) |
| DK (1) | DK2970980T3 (es) |
| EA (1) | EA201591807A1 (es) |
| ES (1) | ES2690047T3 (es) |
| HR (1) | HRP20181741T1 (es) |
| IL (1) | IL240689B (es) |
| LT (1) | LT2970980T (es) |
| MX (1) | MX366910B (es) |
| PH (1) | PH12015501837B1 (es) |
| PL (1) | PL2970980T3 (es) |
| PT (1) | PT2970980T (es) |
| RS (1) | RS57791B1 (es) |
| SG (1) | SG11201507577RA (es) |
| SI (1) | SI2970980T1 (es) |
| SM (1) | SMT201800550T1 (es) |
| TW (1) | TWI630216B (es) |
| WO (1) | WO2014149935A1 (es) |
| ZA (1) | ZA201507671B (es) |
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| US9334319B2 (en) | 2012-04-20 | 2016-05-10 | Abbvie Inc. | Low acidic species compositions |
| US9181572B2 (en) | 2012-04-20 | 2015-11-10 | Abbvie, Inc. | Methods to modulate lysine variant distribution |
| US9512214B2 (en) | 2012-09-02 | 2016-12-06 | Abbvie, Inc. | Methods to control protein heterogeneity |
| SG11201507230PA (en) | 2013-03-12 | 2015-10-29 | Abbvie Inc | Human antibodies that bind human tnf-alpha and methods of preparing the same |
| WO2014151878A2 (en) | 2013-03-14 | 2014-09-25 | Abbvie Inc. | Methods for modulating protein glycosylation profiles of recombinant protein therapeutics using monosaccharides and oligosacharides |
| US9017687B1 (en) | 2013-10-18 | 2015-04-28 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same using displacement chromatography |
| JP2016512029A (ja) * | 2013-03-15 | 2016-04-25 | ヤンセン バイオテツク,インコーポレーテツド | 遺伝子組換えタンパク質中のc末端リジン、ガラクトース、及びシアル酸含量を制御する製造方法 |
| JP2016527911A (ja) | 2013-08-20 | 2016-09-15 | レック・ファーマシューティカルズ・ディー・ディーLek Pharmaceuticals D.D. | ポリペプチドのα−アミド化および/またはC末端アミノ酸開裂を制御するための細胞培養用培地およびプロセス |
| WO2015051293A2 (en) | 2013-10-04 | 2015-04-09 | Abbvie, Inc. | Use of metal ions for modulation of protein glycosylation profiles of recombinant proteins |
| US9181337B2 (en) | 2013-10-18 | 2015-11-10 | Abbvie, Inc. | Modulated lysine variant species compositions and methods for producing and using the same |
| US9085618B2 (en) | 2013-10-18 | 2015-07-21 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same |
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| EP3370768B9 (en) | 2015-11-03 | 2022-03-16 | Janssen Biotech, Inc. | Antibodies specifically binding pd-1 and their uses |
| CN108350416A (zh) * | 2015-11-09 | 2018-07-31 | 百时美施贵宝公司 | 操纵在cho细胞中产生的多肽的品质属性的方法 |
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| JP7235733B2 (ja) | 2017-06-05 | 2023-03-08 | ヤンセン バイオテツク,インコーポレーテツド | Pd-1に特異的に結合する抗体、及び使用方法 |
| WO2019077628A1 (en) * | 2017-10-16 | 2019-04-25 | Council Of Scientific & Industrial Research | ZINC SUPPLEMENTATION TO DECREASE GALACTOSYLATION OF RECOMBINANT GLYCOPROTEINS |
| US12398209B2 (en) | 2018-01-22 | 2025-08-26 | Janssen Biotech, Inc. | Methods of treating cancers with antagonistic anti-PD-1 antibodies |
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| US9181572B2 (en) * | 2012-04-20 | 2015-11-10 | Abbvie, Inc. | Methods to modulate lysine variant distribution |
| JP2016512029A (ja) * | 2013-03-15 | 2016-04-25 | ヤンセン バイオテツク,インコーポレーテツド | 遺伝子組換えタンパク質中のc末端リジン、ガラクトース、及びシアル酸含量を制御する製造方法 |
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2014
- 2014-03-07 JP JP2016500790A patent/JP2016512029A/ja active Pending
- 2014-03-07 PT PT14768761T patent/PT2970980T/pt unknown
- 2014-03-07 SI SI201430848T patent/SI2970980T1/sl unknown
- 2014-03-07 ES ES14768761.0T patent/ES2690047T3/es active Active
- 2014-03-07 AU AU2014237635A patent/AU2014237635B2/en not_active Ceased
- 2014-03-07 BR BR112015022971-9A patent/BR112015022971B1/pt not_active IP Right Cessation
- 2014-03-07 LT LTEP14768761.0T patent/LT2970980T/lt unknown
- 2014-03-07 MX MX2015012361A patent/MX366910B/es active IP Right Grant
- 2014-03-07 EP EP14768761.0A patent/EP2970980B2/en active Active
- 2014-03-07 SG SG11201507577RA patent/SG11201507577RA/en unknown
- 2014-03-07 HR HRP20181741TT patent/HRP20181741T1/hr unknown
- 2014-03-07 PL PL14768761T patent/PL2970980T3/pl unknown
- 2014-03-07 KR KR1020157029490A patent/KR102216003B1/ko not_active Expired - Fee Related
- 2014-03-07 RS RS20181228A patent/RS57791B1/sr unknown
- 2014-03-07 SM SM20180550T patent/SMT201800550T1/it unknown
- 2014-03-07 EA EA201591807A patent/EA201591807A1/ru unknown
- 2014-03-07 CA CA2907140A patent/CA2907140A1/en active Pending
- 2014-03-07 WO PCT/US2014/021574 patent/WO2014149935A1/en not_active Ceased
- 2014-03-07 CN CN201480015815.5A patent/CN105378086B/zh not_active Expired - Fee Related
- 2014-03-07 DK DK14768761.0T patent/DK2970980T3/en active
- 2014-03-13 US US14/207,915 patent/US20140273092A1/en not_active Abandoned
- 2014-03-13 TW TW103108900A patent/TWI630216B/zh not_active IP Right Cessation
- 2014-03-13 AR ARP140100976A patent/AR095660A1/es not_active Application Discontinuation
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2015
- 2015-08-20 IL IL240689A patent/IL240689B/en unknown
- 2015-08-20 PH PH12015501837A patent/PH12015501837B1/en unknown
- 2015-10-14 ZA ZA2015/07671A patent/ZA201507671B/en unknown
- 2015-12-23 US US14/757,691 patent/US11149085B2/en not_active Expired - Fee Related
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2018
- 2018-11-02 CY CY181101150T patent/CY1120980T1/el unknown
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2020
- 2020-06-11 AU AU2020203864A patent/AU2020203864B2/en not_active Ceased
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2021
- 2021-09-29 US US17/489,744 patent/US20220089712A1/en not_active Abandoned
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2022
- 2022-02-14 AR ARP220100291A patent/AR124871A2/es unknown
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