JPH06510904A - 少なくとも遊離のチオールとして存在するシステインを有する抗体フラグメントの大腸菌での発現、2官能性F(ab’)↓2抗体の産生のための使用 - Google Patents
少なくとも遊離のチオールとして存在するシステインを有する抗体フラグメントの大腸菌での発現、2官能性F(ab’)↓2抗体の産生のための使用Info
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- JPH06510904A JPH06510904A JP5506295A JP50629593A JPH06510904A JP H06510904 A JPH06510904 A JP H06510904A JP 5506295 A JP5506295 A JP 5506295A JP 50629593 A JP50629593 A JP 50629593A JP H06510904 A JPH06510904 A JP H06510904A
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- fab
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/06—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies from serum
- C07K16/065—Purification, fragmentation
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- 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
- C07K16/32—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against translation products of oncogenes
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/46—Hybrid immunoglobulins
- C07K16/468—Immunoglobulins having two or more different antigen binding sites, e.g. multifunctional antibodies
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- 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
-
- 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
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
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- 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
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
- C07K2317/732—Antibody-dependent cellular cytotoxicity [ADCC]
-
- 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
- C07K2317/77—Internalization into the cell
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/034—Fusion polypeptide containing a localisation/targetting motif containing a motif for targeting to the periplasmic space of Gram negative bacteria as a soluble protein, i.e. signal sequence should be cleaved
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/972—Modified antibody, e.g. hybrid, bifunctional
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- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Immunology (AREA)
- General Health & Medical Sciences (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Life Sciences & Earth Sciences (AREA)
- Oncology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
Abstract
Description
Claims (24)
- 1.免疫グロブリンH鎖Fv領域および免疫グロブリンL鎖Fv領域を含有する Fvポリペプチドを組換え徴生物細胞培養液のペリプラズム中に発現および分泌 し、その際、該L鎖およびH鎖はまた不対システイン残基を遊離チオールとして 含み、ついで該システイン残基を遊離チオールとして実質的に維持する条件下で 該ポリペプチドを回収することからなる方法。
- 2.少なくとも一つのヒンジ領域システインを遊離チオールとして有するFab ′抗体ポリペプチド(Fab′−SH)の製造法であって、(a)Fab′を含 む免疫グロブリンプレ配列をコードする核酸(徴生物宿主細胞によって認識され る制御配列に機能的に連結されている)を含むベクターで形質転換した該宿主細 胞中で、宿主細胞のペリプラズム腔ヘのFab′の分泌およびFab′−SHの 生成に適した条件下にて該核酸を発現させ;ついで(b)該宿主細胞からFab ′−SHを回収することを特徴とする方法。
- 3.工程bの間に該Fab′−SHを還元条件に暴露しない請求項2に記載の方 法。
- 4.該Fab′−SHがヒンジ領域システインを一つだけ有する請求項2に記載 の方法。
- 5.該Fab′−SHの回収を、ヒンジシステインチオールをプロトン化形態に 維持するのに適した条件下で行う請求項4に記載の方法。
- 6.形質転換細胞を培養する間に金属イオンキレート試薬を存在させる請求項2 に記載の方法。
- 7.該Fab′−SHの回収の間に金属イオンキレート試薬を存在させる請求項 2に記載の方法。
- 8.該Fab′−SHの回収の間にプロテアーゼインヒビターを存在させる請求 項2に記載の方法。
- 9.形質転換細胞を培養する間にプロテアーゼインヒビターを存在させる請求項 8に記載の方法。
- 10.該Fab′−SHの回収を、宿主細胞を凍結−解凍し、ついでリゾチーム の存在下で浸透ショックに供することにより行う請求項2に記載の方法。
- 11.Fab′がC末端アミノ酸配列CysAlaAlaを有する請求項2に記 載の方法。
- 12.該微生物宿主が大腸菌である請求項2に記載の方法。
- 13.F(ab′)2からなるポリペプチドの調製法であって、(a)第一Fa b′を含む免疫グロブリンプレ配列をコードする核酸(微生物宿主細胞によって 認識される制御配列に機能的に連結されている)を含むベクターで形質転換した 該宿主細胞中で、宿主細胞のペリプラズム腔ヘの該第一Fab′の分泌およびF ab′−SHの生成に適した条件下にて該核酸を発現させ(該第−Fab′は第 一のエピトープに結合し得る);(b)第二Fab′を含む免疫グロブリンプレ 配列をコードする核酸(微生物宿主細胞によって認識される制御配列に機能的に 連結されている)を含むベクターで形質転換した該宿主細胞中で、宿主細胞のペ リプラズム腔ヘの該第二Fab′の分泌およびFab′−SHの生成に適した条 件下にて該核酸を発現させ(該第二Fab′は第二のエピトープに結合し得る) ;(c)該第一Fab′−SHおよび第二Fab′−SHを該宿主細胞から回収 し;ついで (d)該第一Fab′−SHおよび第二Fab′−SHのシステインの遊離チオ ール間で共有結合を形成して2価F(ab′)2を形成させることを特徴とする 方法。
- 14.該共有結合がジスルフィド結合である請求項12に記載の方法。
- 15.該第一Fab′−SHと第二Fab′−SHとの間の結合形成が下記工程 からなる請求項13に記載の方法。 (a)第一Fab′−SHを(i)5,5′−ジチオビス(2−ニトロ安息香酸 )(DTNB)と反応させてチオニトロベンゾエート誘導体Fab′−TNBを 生成させるか、または(ii)2官能性マレイミドと反応させ;(b)該Fab ′−TNBまたはマレイミド化Fab′を第二Fab′−SHに直接カップリン グしてF(ab′)2を生成させ;ついで(c)該F(ab′)2を回収する。
- 16.2つのFab′によって結合されるエピトープが同じ抗原上に位置する請 求項12に記載の方法。
- 17.2つのFab′によって結合されるエピトープが異なる抗原上に位置する 請求項12に記載の方法。
- 18.各Fab′が約1g/1を越えるレベルで培地中に存在する請求項12に 記載の方法。
- 19.各Fab′が、非ヒト免疫グロブリンからの相補性決定領域アミノ酸配列 およびヒト免疫グロブリンからの他のアミノ酸配列からなる請求項12に記載の 方法。
- 20.該アミノ酸配列がIgGから得られたものである請求項12に記載の方法 。
- 21.(a)天然のFv領域に認められるジスルフィド結合を除いて、誘導体化 されたスルフヒドリル基を有するシステイン残基を含有するF(ab′)2Fv 領域を本質的に含有せず、 (b)ヒンジ領域の鎖内ジスルフィド結合を有するF(ab′)2を全く含有せ ず、(c)混入する亜ヒ酸塩を全く含有せず、および(d)H鎖のC末端アミノ 酸残基に関して全く均一であるF(ab′)2を含む組成物。
- 22.免疫グロブリンポリペプチドの高収率製造法であって、免疫グロブリンポ リペプチドをコードする核酸で形質転換した宿主細胞を誘導プロモーター/オペ レーター系の転写制御下で培養し、それによって細胞培養液中の誘導後ポリペプ チドレベルが細胞培養液1リットル当たり約1グラム以上のポリペプチドとなる に充分、該ポリペプチドの発現を誘導前に抑制することを特徴とする方法。
- 23.該Fab′−SHが2以上のヒンジ領域システインを有する請求項2に記 載の方法。
- 24.該Fab′のL鎖とH鎖が共有結合により結合していない請求項2に記載 の方法。
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US76229291A | 1991-09-19 | 1991-09-19 | |
US07/762,292 | 1991-09-19 | ||
PCT/US1992/007986 WO1993006217A1 (en) | 1991-09-19 | 1992-09-18 | EXPRESSION IN E. COLI OF ANTIBODY FRAGMENTS HAVING AT LEAST A CYSTEINE PRESENT AS A FREE THIOL, USE FOR THE PRODUCTION OF BIFUNCTIONAL F(ab')2 ANTIBODIES |
Related Child Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2003389257A Division JP2004041240A (ja) | 1991-09-19 | 2003-11-19 | 少なくとも遊離のチオールとして存在するシステインを有する抗体フラグメントの大腸菌での発現、2官能性F(ab’)2抗体の産生のための使用 |
JP2005253013A Division JP2006001943A (ja) | 1991-09-19 | 2005-09-01 | 少なくとも遊離のチオールとして存在するシステインを有する抗体フラグメントの大腸菌での発現、2官能性F(ab’)2抗体の産生のための使用 |
Publications (2)
Publication Number | Publication Date |
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JPH06510904A true JPH06510904A (ja) | 1994-12-08 |
JP3951062B2 JP3951062B2 (ja) | 2007-08-01 |
Family
ID=25064638
Family Applications (4)
Application Number | Title | Priority Date | Filing Date |
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JP50629593A Expired - Lifetime JP3951062B2 (ja) | 1991-09-19 | 1992-09-18 | 少なくとも遊離のチオールとして存在するシステインを有する抗体フラグメントの大腸菌での発現、2官能性F(ab’)2抗体の産生のための使用 |
JP2003389257A Pending JP2004041240A (ja) | 1991-09-19 | 2003-11-19 | 少なくとも遊離のチオールとして存在するシステインを有する抗体フラグメントの大腸菌での発現、2官能性F(ab’)2抗体の産生のための使用 |
JP2004256350A Pending JP2004337179A (ja) | 1991-09-19 | 2004-09-02 | 少なくとも遊離のチオールとして存在するシステインを有する抗体フラグメントの大腸菌での発現、2官能性F(ab’)2抗体の産生のための使用 |
JP2005253013A Pending JP2006001943A (ja) | 1991-09-19 | 2005-09-01 | 少なくとも遊離のチオールとして存在するシステインを有する抗体フラグメントの大腸菌での発現、2官能性F(ab’)2抗体の産生のための使用 |
Family Applications After (3)
Application Number | Title | Priority Date | Filing Date |
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JP2003389257A Pending JP2004041240A (ja) | 1991-09-19 | 2003-11-19 | 少なくとも遊離のチオールとして存在するシステインを有する抗体フラグメントの大腸菌での発現、2官能性F(ab’)2抗体の産生のための使用 |
JP2004256350A Pending JP2004337179A (ja) | 1991-09-19 | 2004-09-02 | 少なくとも遊離のチオールとして存在するシステインを有する抗体フラグメントの大腸菌での発現、2官能性F(ab’)2抗体の産生のための使用 |
JP2005253013A Pending JP2006001943A (ja) | 1991-09-19 | 2005-09-01 | 少なくとも遊離のチオールとして存在するシステインを有する抗体フラグメントの大腸菌での発現、2官能性F(ab’)2抗体の産生のための使用 |
Country Status (5)
Country | Link |
---|---|
US (4) | US7018809B1 (ja) |
EP (2) | EP0861893A3 (ja) |
JP (4) | JP3951062B2 (ja) |
CA (1) | CA2116774C (ja) |
WO (1) | WO1993006217A1 (ja) |
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1995
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2004
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2005
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US8618256B2 (en) | 1997-07-14 | 2013-12-31 | Bolder Biotechnology | Cysteine variants of interferon gamma |
US8859497B2 (en) | 1997-07-14 | 2014-10-14 | Bolder Biotechnology, Inc. | Method of treatment using cysteine mutants of beta interferon |
JP2002534119A (ja) * | 1999-01-14 | 2002-10-15 | ボルダー バイオテクノロジー, インコーポレイテッド | 自由システイン残基を有するタンパク質の生産方法 |
JP2014064594A (ja) * | 1999-01-14 | 2014-04-17 | Bolder Biotechnology Inc | 自由システイン残基を有するタンパク質の生産方法 |
US8957023B2 (en) | 1999-01-14 | 2015-02-17 | Bolder Biotechnology Inc. | Methods for making proteins containing free cysteine residues |
US7947655B2 (en) | 1999-01-14 | 2011-05-24 | Bolder Biotechnology, Inc. | Methods for making proteins containing free cysteine residues |
JP2010083898A (ja) * | 1999-04-09 | 2010-04-15 | Intercell Usa Inc | Clostridiumdifficileに対する、組換え毒素A/毒素Bワクチン |
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US5648237A (en) | 1997-07-15 |
EP0861893A2 (en) | 1998-09-02 |
CA2116774C (en) | 2003-11-11 |
WO1993006217A1 (en) | 1993-04-01 |
JP2004337179A (ja) | 2004-12-02 |
JP2004041240A (ja) | 2004-02-12 |
JP2006001943A (ja) | 2006-01-05 |
CA2116774A1 (en) | 1993-04-01 |
JP3951062B2 (ja) | 2007-08-01 |
US7018809B1 (en) | 2006-03-28 |
EP0861893A3 (en) | 1999-11-10 |
US20080124765A1 (en) | 2008-05-29 |
EP0604580A1 (en) | 1994-07-06 |
US20050244929A1 (en) | 2005-11-03 |
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