JP2003192699A - トランスジェニック動物からの抗体の生産 - Google Patents
トランスジェニック動物からの抗体の生産Info
- Publication number
- JP2003192699A JP2003192699A JP2002314611A JP2002314611A JP2003192699A JP 2003192699 A JP2003192699 A JP 2003192699A JP 2002314611 A JP2002314611 A JP 2002314611A JP 2002314611 A JP2002314611 A JP 2002314611A JP 2003192699 A JP2003192699 A JP 2003192699A
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- JP
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- Prior art keywords
- immunoglobulin
- animal
- human
- dna
- cells
- 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.)
- Granted
Links
- 241001465754 Metazoa Species 0.000 title claims abstract description 50
- 230000009261 transgenic effect Effects 0.000 title claims abstract description 29
- 238000004519 manufacturing process Methods 0.000 title description 6
- 108060003951 Immunoglobulin Proteins 0.000 claims abstract description 53
- 102000018358 immunoglobulin Human genes 0.000 claims abstract description 53
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 44
- 239000000427 antigen Substances 0.000 claims abstract description 17
- 108091007433 antigens Proteins 0.000 claims abstract description 17
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- 241000251539 Vertebrata <Metazoa> Species 0.000 claims 1
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- 108091029865 Exogenous DNA Proteins 0.000 abstract description 2
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- 210000004080 milk Anatomy 0.000 description 10
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- 238000002105 Southern blotting Methods 0.000 description 4
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- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
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- 210000000628 antibody-producing cell Anatomy 0.000 description 2
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- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- 101150084750 1 gene Proteins 0.000 description 1
- NHBKXEKEPDILRR-UHFFFAOYSA-N 2,3-bis(butanoylsulfanyl)propyl butanoate Chemical compound CCCC(=O)OCC(SC(=O)CCC)CSC(=O)CCC NHBKXEKEPDILRR-UHFFFAOYSA-N 0.000 description 1
- 102100033040 Carbonic anhydrase 12 Human genes 0.000 description 1
- 102100032566 Carbonic anhydrase-related protein 10 Human genes 0.000 description 1
- 241000701959 Escherichia virus Lambda Species 0.000 description 1
- 238000012413 Fluorescence activated cell sorting analysis Methods 0.000 description 1
- 108091092584 GDNA Proteins 0.000 description 1
- 101000867855 Homo sapiens Carbonic anhydrase 12 Proteins 0.000 description 1
- 101000867836 Homo sapiens Carbonic anhydrase-related protein 10 Proteins 0.000 description 1
- 101000799461 Homo sapiens Thrombopoietin Proteins 0.000 description 1
- 206010061598 Immunodeficiency Diseases 0.000 description 1
- 208000029462 Immunodeficiency disease Diseases 0.000 description 1
- 102000009786 Immunoglobulin Constant Regions Human genes 0.000 description 1
- 108010009817 Immunoglobulin Constant Regions Proteins 0.000 description 1
- 108091092195 Intron Proteins 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- 102000014171 Milk Proteins Human genes 0.000 description 1
- 108010011756 Milk Proteins Proteins 0.000 description 1
- 101100370002 Mus musculus Tnfsf14 gene Proteins 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
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- 229940098773 bovine serum albumin Drugs 0.000 description 1
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- 238000003776 cleavage reaction Methods 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 1
- 101150118163 h gene Proteins 0.000 description 1
- 230000035931 haemagglutination Effects 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 102000053400 human TPO Human genes 0.000 description 1
- 230000007813 immunodeficiency Effects 0.000 description 1
- 238000001114 immunoprecipitation Methods 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 235000021239 milk protein Nutrition 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/85—Vectors or expression systems specially adapted for eukaryotic hosts for animal cells
- C12N15/8509—Vectors or expression systems specially adapted for eukaryotic hosts for animal cells for producing genetically modified animals, e.g. transgenic
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K67/00—Rearing or breeding animals, not otherwise provided for; New or modified breeds of animals
- A01K67/027—New or modified breeds of vertebrates
- A01K67/0275—Genetically modified vertebrates, e.g. transgenic
- A01K67/0278—Knock-in vertebrates, e.g. humanised vertebrates
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/46—Hybrid immunoglobulins
- C07K16/461—Igs containing Ig-regions, -domains or -residues form different species
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2207/00—Modified animals
- A01K2207/15—Humanized animals
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2217/00—Genetically modified animals
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2217/00—Genetically modified animals
- A01K2217/05—Animals comprising random inserted nucleic acids (transgenic)
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2227/00—Animals characterised by species
- A01K2227/10—Mammal
- A01K2227/105—Murine
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2267/00—Animals characterised by purpose
- A01K2267/01—Animal expressing industrially exogenous proteins
-
- 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
- C07K2319/00—Fusion polypeptide
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- Biotechnology (AREA)
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- Biophysics (AREA)
- Immunology (AREA)
- Biomedical Technology (AREA)
- Environmental Sciences (AREA)
- Veterinary Medicine (AREA)
- Microbiology (AREA)
- Animal Behavior & Ethology (AREA)
- Animal Husbandry (AREA)
- Biodiversity & Conservation Biology (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
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- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Abstract
益な免疫グロブリンを、ヒト以外のトランスジェニック
動物を用いて生産する。 【解決手段】 ヒト由来免疫グロブリンのH鎖領域をコ
ードする遺伝子セグメントを含み、ヒト由来の免疫グロ
ブリンの少なくとも一部をコードする外来DNAを、ヒ
ト以外の動物の生殖系列内に導入することにより、ヒト
以外のトランスジェニック動物を生産し、それにより、
このトランスジェニック動物を特定の抗原で攻撃するこ
とに続いて、この再配列または変異されたDNAにコー
ドされたこの特定の抗原に対するこの免疫グロブリンを
この動物の細胞内または体液内において発現させるステ
ップと、この動物の細胞または適当な体液から免疫グロ
ブリンを得るステップと、を備える、特定の抗原に対す
る免疫グロブリンを生産する方法。
Description
ン)の生産に関するものである。
源の免疫グロブリンの少なくとも一部をコードするかま
たは免疫グロブリンのレパートリーをコードするために
再配列し得る遺伝物質をその生殖系列に挿入されたトラ
ンスジェニック動物の細胞または体液から免疫グロブリ
ンを得ることを含む、免疫グロブリンを生産する方法が
提供される。
物源から誘導される免疫グロブリンを意味する。たとえ
ばトランスジェニック動物がマウスの場合、挿入される
遺伝物質は、たとえばヒトのようなマウス以外の起源の
ものである。
れてもよく、または人工合成により生産されてもよい。
材料は、知られた免疫グロブリンの少なくとも一部をコ
ードしてもよく、または改変された免疫グロブリンの少
なくとも一部をコードするよう修飾されてもよい。これ
らのプロセスのための適当な技術はよく知られている。
動物において発現することができ、少なくとも一部は挿
入された材料から誘導される免疫グロブリンの生産をも
たらす。遺伝物質はトランスジェニック動物において再
配列され、それにより、たとえ挿入された遺伝物質が生
殖系列において間違った位置にまたは間違った形態構造
で組込まれたとしても、挿入された遺伝物質からの一つ
の部分または複数の部分で免疫グロブリンのレパートリ
ーが生産され得ることが見出された。挿入された物質の
性質によって、動物は、たとえば混合されたマウス/ヒ
ト起源のキメラの免疫グロブリンを生産し得、そこでは
外来起源の遺伝物質は免疫グロブリンの一部だけをコー
ドする。あるいは動物は、たとえばまったくヒト起源
の、完全に外来の免疫グロブリンを生産し得、そこでは
外来起源の遺伝物質は、免疫グロブリン全体をコードす
る。ヒトでの使用に適する可能性のある治療上有益な免
疫グロブリンは、こうしてこの発明の使用によって生産
できる。
てトランスジェニック動物から生産されてもよい。その
代わりに、たとえば骨髄腫細胞と動物からの脾臓細胞を
融合しかつ所望の抗体を生産するものを選択するために
結果として生じたハイブリドーマをふるい分けることに
よって、モノクローナル抗体がトランスジェニック動物
から生産されてもよい。このようなプロセスのための適
当な技術は当業者によく知られている。
血清のような体液または乳汁、初乳もしくは唾液のよう
な動物の外部分泌物において所望の抗体が産出されるよ
うに動物に組込まれてもよい。たとえば、外来起源の免
疫グロブリンの少なくとも一部をコードする遺伝物質を
乳タンパク質をコードする哺乳動物の遺伝子にインビト
ロで挿入し、かつそれから、たとえば注入によって、そ
の遺伝子を哺乳動物の受精卵に導入することによって、
その卵は、少なくとも一部は挿入された遺伝物質から誘
導される免疫グロブリンを含む乳汁を生産する成熟した
雌の哺乳動物に発育することができる。次いで所望の抗
体が乳汁から採収できる。このようなプロセスを実施す
るための適当な技術は当業者に知られている。
によって生成された免疫グロブリン生産細胞を動物から
除去した後、対象の免疫グロブリンを生産する細胞をイ
ンビトロで選択することを含む。次いで免疫グロブリン
は知られた態様において選択された細胞からインビトロ
で生産できる。
入される免疫原に応答してキメラのまたは外来の免疫グ
ロブリン(挿入された遺伝物質から誘導される)を生産
できるということが発見された。したがって、免疫グロ
ブリンの種特異的な全領域を実質的にコードする外来
の、たとえばヒトの遺伝物質を導入することによって、
動物に導入される任意の抗原に対して外来の免疫グロブ
リンを生産するよう動物を刺激することが可能になり得
る。こうしてトランスジェニック動物は、広範囲の抗原
に対するヒトの免疫グロブリンの非常に有益で、便利で
かつ価値のある源を提供することができるであろう。
まく再配列させるために近接ゲノムに組込まれるという
ことが重要であるかもしれない。そこで、挿入される遺
伝物質はプラスミドおよびコスミドのような原核生物の
ベクタにクローン化されたDNAの形態とすることがで
きる。複数のプラスミドまたはコスミドもまた使用され
てもよく、しかしこれらがゲノム上に近接して組込まれ
ることがおそらく必要である。酵母の人工染色体ベクタ
を使用することによって(1987年、バーク(Burk
e)、DT、カール(Carle)、GFおよびオルソン(Olso
n)、MVの「人工染色体ベクタによる酵母への外因性D
NAの大きなセグメントのクローニング」(Cloning of
large segments of exogenous DNA into yeast by mean
s of artifical chromosome vectors)サイエンス(Scien
ce) 、236号、806頁ないし812頁を参照)、ま
たは染色体断片の導入によって(リッチャー(Richer)
、JおよびLo、CW、1989年「全裂ヒト染色体
断片の注入によるヒトDNAのマウス卵への導入」(Int
roduction of human DNA into mouse eggs by injectio
n of dissected human chromo some fragments) サイエ
ンス(Science)245号、175頁ないし177頁を参
照)、より大きいDNA断片を挿入することもまた可能
であると判明し得る。
たは胚幹細胞への注入または他の方法による従来の態様
で宿主に導入することができる。
する遺伝物質を持たない宿主動物を使用することが便利
となり得、それにより得られるトランスジェニック動物
は、免疫グロブリンを生産するとき、挿入された外来の
遺伝物質だけを使用するであろう。これは、関連する遺
伝物質を欠く自然に発生した突然変位体宿主を使用する
ことによって、または関連する遺伝物質が取り除かれた
宿主を最後に作るために、突然変位体をたとえば細胞系
において人工的に作ることによってのどちらかで達成さ
れ得る。
ドする遺伝物質を持つ場合、トランスジェニック動物
は、本来生じる遺伝物質および挿入された遺伝物質を持
つであろうし、かつ本来生じる遺伝物質、挿入された遺
伝物質および遺伝物質の両方の型の混合物から誘導され
る免疫グロブリンを生産するであろう。この場合におい
て、所望の免疫グロブリンは、トランスジェニック動物
から誘導されるハイブリドーマをふるい分けることによ
って、たとえば示差的染色体喪失または抗体遺伝子発現
の対立遺伝子排除の現象を活用することによって得るこ
とができる。
にヒト以外の哺乳動物のトランスジェニック動物を生産
し、その動物は、その生殖系列に外来起源の免疫グロブ
リンの少なくとも一部をコードするか、または免疫グロ
ブリンのレパートリーをコードするために再配列できる
遺伝物質を挿入されたものである。
発明に従うトランスジェニック動物から生産されたまた
はこの発明の方法によって生産された免疫グロブリンも
含む。
ブリンVH遺伝子、Dセグメントのいくつか、およびす
べてのJHおよびCmu遺伝子セグメントを含み、その
生殖系列に導入されたDNAセグメントを持つトランス
ジェニックマウスの系統が確立された。VH遺伝子の1
つ、すべてのJHセグメントおよびIgM抗体の分泌さ
れるH鎖定常領域をコードするエキソンは、ヒト起源で
あり、残りの物質はマウス起源であった。遺伝子セグメ
ントは、トランスジェニックマウスのリンパ組織におい
て生産的VH−D−JH結合を受け、血清において結果
として生じるヒト/マウスキメラのIgM抗体の合成を
伴う。
スジェニックマウスからの脾臓細胞との間での融合によ
りハイブリドーマが確立された。ハイブリッドの多くは
ヒトキメラのIgMモノクローナル抗体を分泌する。し
たがって、トランスジェニックマウスのこれらの系統
は、キメラのヒト抗血清またはモノクローナル抗体の生
産のために使用できる。
作に続いて、導入された抗原に対してキメラの抗体を生
産する応答をし、したがってこのアプローチはヒトのお
よび異種の抗原に対して向けられる通常のヒトのまたは
キメラのヒト抗体のレパートリーを生産するためにも有
益であることが判明するはずであり、なぜならトランス
ジェニックマウスはヒト抗原の決定基に対して寛容でな
いであろうからである。
よびCmu配列を独占的に持つトランスジェニックマウ
スが、受精マウス卵にヒトVH遺伝子、Dセグメント、
JセグメントおよびCmu定常領域を含むコスミドを注
入することによって生産された。得られたマウスは、マ
ウスIgMが約200ug/mlで存在する状態で、そ
の血清においてヒトmu鎖を含む抗体を10〜100u
g/mlの間で生産した。
の例において例示として説明される。
マウス卵に注入された。この図において、ヒト配列は塗
りつぶされた棒によって表わされ、マウス配列は塗りつ
ぶされていない棒によって表わされ、ベクタは交差する
斜線が引かれた棒によって表わされ、かつD要素は斜線
が引かれた棒によって表わされる。制限エンドヌクレア
ーゼ開裂部位は以下のように、BglIIがBgに、P
vulがPに、EcoRIがRに、KpnlがKに、B
amHIがBに、XbaIがXに、HindIIIがH
に略されている。
とおりである。ベクタ 充填されたNarI部位にクローン化されたB
glIIリンカを含むpUC12誘導体のEcoRI部
位とBglII部位との間に全「ミニIgH遺伝子座」
がクローン化された。
のVH遺伝子がある。VH26は、ヒト起源のものであ
りかつファージラムダVH26からBglII−Eco
RI0.85Kb断片として得られた(1980年、マ
ティセンズ・アンド・ラビッツ(Matthyssens & Rabbitt
s)PNAS、77巻、6561頁ないし6565頁)。
VH−186.2は、C57BL/6マウスからの生殖
系列VH遺伝子であり、かつ2.5KbのSacI−K
pnI断片として得られた(ボースウェル(Bothwell)
、パスキンド(Paskind) 、リース(Reth)、イマニシ−
カリ(Imanishi-Kari)、ラジェウスキ(Rajewsky)および
バルチモア(Baltimore) 1981年、セル(Cell)、24
巻、625頁ないし637頁)。
52要素は、221 nt XhoI−SacI断片と
して得られた。M13tg131のSacI部位とSa
lI部位との間でのクローン化に続き、オリゴヌクレオ
チド 5′−GCGTCACCGTGGTAGCTGCTAC
CGTAGTAATAAACACTGTGGTCC、ま
たは5′−GCGTCACCGTGGTCGTAACC
ATAGTAGACACTGTGGTGC のどちらかでの位置指定突然変異誘発が、マウスSP2
およびFL16系統群のものにそれぞれ関連するD要素
をもつM13tg131クローンをつくるために使用さ
れた。これらのD系統群はマウスおよびヒトの両方にお
いて見出される。別のD要素−ヒトD−Q52−はヒト
JHクラスタ(以下を参照)内において含まれた。
グメント、3つの擬似JHおよびヒトD−Q52要素を
含む、ヒトDNAからの3.5Kb BglII断片が
使用された(ラベッチ(Ravetch) 他、1981年、セル
(Cell)、27巻、583頁ないし591頁)IgHエンハンサ ヒトIgHエンハンサの部分は、J
Hクラスタを含むBglII断片内に含まれる。マウス
エンハンサの完全な複製物は1Kb XbaI断片内に
含まれる。
トDNAの7.5Kb Xbal断片がmuS(スイッ
チ)領域およびmuH鎖定常領域のエキソン1〜4を含
む。mu膜エキソンおよびCmu4エキソンとCmuM
l膜エキソンとの間のイントロンの塊が、マウスmuC
H遺伝子の2.5Kb HindIII−SphI断片
によって与えられ、そこにおいてSphI部位はリンカ
の使用によってBglII部位に変換された。
スゲルにおける電気泳動の後精製されかつ既に説明され
ているようにC57BL/6J×CBA/Caマウスの
受精卵の雄性前核の中に注入された(レイク(Reik)他、
1987年、ヨーロピアン・ジャーナル・オブ・イムノ
ロジー(Eur.J.Immunol.)17巻、465頁ないし469
頁)。尾部DNAのサザンブロット分析が、生まれた3
2匹のマウスのうち12匹がミニ遺伝子座を持っていた
ことを明らかにした。最終的な研究は、それらすべてが
ミニ遺伝子座の少数の複製物(2ないし5)を持つ3匹
の基礎となるマウス−HIg17、19および29の子
孫において行なわれた。
性を含む抗体の存在についてELISAにより検査され
た。免疫感作されていないトランスジェニックマウス
は、それらの血清において10〜100ug/mlの間
でキメラのヒトIgMを含むことが判明した。末梢血に
おけるリンパ球の蛍光抗体分析もまた、ビオチニル化さ
れた種特異的な抗ヒトIgM抗体およびフルオレセイン
結合されたストレプトアビジンによる細胞染色の存在を
明らかにした。
ドーマ トランスジェニックマウスは、ヒト赤血球細胞またはヒ
ツジ赤血球細胞のどちらかで腹膜内で免疫処置された。
脾臓が免疫感作の後様々な時期に取り除かれ、HAT培
地において選択されたハイブリッドおよびNSO骨髄腫
を用いて融合が行なわれた。これらのハイブリッドの多
くはELISAアッセイによって明らかにされるとおり
キメラのヒトIgMを作った。
からの組織からのDNAのサザンブロット分析は、トラ
ンスジェニックマウスのリンパ組織におけるミニIg遺
伝子座内において高頻度のDNA再配列があることを明
らかにした。
組織またはハイブリドーマからのDNAは、EcoRI
で消化され、かつミニ遺伝子座におけるヒトJ6要素と
マウスIgHエンハンサとの間の領域に対してハイブリ
ッド形成するヒトIgHエンハンサプローブ(BalI
−BglII断片)とハイブリッド形成された。DNA
のサザンブロット分析の結果は図2に示される。標識断
片のKbによるサイズが図に与えられている。
またはNSO融合のパートナーからの細胞質RNA(5
ug)が、ヒトCmu、ヒトVH26またはマウスVH
186プローブでプローブされた。細胞質RNAのノー
ザンブロット分析の結果は図3に示され、それは、ハイ
ブリドーマがVH26、VH186V遺伝子のどちらか
または両方に対すると同様にヒトmuに対するプローブ
とハイブリッド形成するmRNAを含んでいたことを明
らかにしている。こうしてヒトVH26およびマウスV
H186の両方は再配列できかつ従ってキメラのヒトI
gM抗体を分泌する細胞系を造ることができる。
ドーマによる抗体分泌 クローン化されたハイブリドーマ細胞系によるタンパク
質生産は、L−[3 5S]メチオニンによる生合成標識
の使用およびその後の抗ヒトmu抗血清での精製により
分析された。特に、細胞は、L−[3 5 S]メチオニン
および免疫沈降により培養上澄みから精製されたIgM
抗体ならびに抗ヒトmu抗血清を含む培地にてひと晩イ
ンキュベートされた。トランスジェニックハイブリドー
マ35.5および24aの上澄みからの精製は、図4に
おいて「+」によって示されるように非放射性の、精製
されたマウスモノクローナルIgM抗体(B1−8)の
大過剰(50ug)の存在下で達成された。マウスIg
M分泌細胞系を使用して見られるように、抗ヒトmu抗
血清はマウスmuと交差反応するが、この交差反応は非
放射性のマウスB1−8IgM抗体によって競争され得
る−図4の左の4つのレーンを参照。
を分泌するこれらのトランスジェニックマウスからのハ
イブリドーマを確立することが可能であることを示す。
生産するトランスジェニック動物をつくることができ
る。例示として、この例は、抗原特異的キメラのヒトI
gA2抗体のH鎖およびL鎖をコードする遺伝子をそれ
らの生殖系列に組込まれて保有するトランスジェニック
マウスに関するものである。
み物を保有する9つのトランスジェニックマウス系統が
確立された。図5において、太く塗られた線はマウスI
gDNAを示し、斜線が引かれた部分はヒトDNAを、
空白の部分はマウスIgHおよびSV40エンハンサ
を、かつ細く塗られた線はpSV2gptベクタを示
す。制限部位の略語は図1と同様である。プラスミド
は、既に説明されているpSV−VNPHα2の誘導体
であり(ブルゲマン(Bruggemann)他、J.Exp.Med 、19
87年、166巻、1351頁ないし1361頁)かつ
マウスHOPC2020形質細胞腫の再配列されたラム
ダ1遺伝子を含む7.4kb EcoRI断片を含んで
いる(バーナード(Bernard) 他、1978年、セル(Cel
l)15巻、1133頁ないし1140頁)。プラスミド
DNAは、ベクタにおけるPvuI部位において線状に
され、既に説明されているようにトランスジェニックマ
ウスが誘導された(レイク(Reik)他、Eur. F. Immunol
、1987年、17巻、465頁ないし469頁)。
は、ハプテン4−ヒドロキシ−3−ニトロフェンアセチ
ル(NP)に対して特異性を有する。トランスジェニッ
ク抗体の発現は、プラスチックプレートに結合されたN
Pウシ血清アルブミンを使用しかつビオチニル化された
抗ヒトアルファ抗血清で展開するELISAアッセイに
よって測定された。Ig全体は、抗マウスIg被覆され
たプラスチックを使用しかつビオチニル化された抗マウ
スカッパ抗血清で展開して測定された。キメラの抗NP
IgA2の濃度は、7匹のトランスジェニックマウスお
よび1匹の対照マウスからの初乳、血清および乳汁にお
いて測定され、その結果は表1に示される。初乳は出産
から24時間以内にホルモン注射に続いて母親からとら
れ、かつ乳汁は同腹子が生後13〜15日目であったと
き母親からとられ、血清は乳汁と同じときに得られた。
動物は、特定の抗体の生産のために使用することがで
き、そして特定の有用な抗体が混ざった乳汁を生ずる動
物の繁殖が可能になるとともに、乳汁、初乳、血清、唾
液等からの大規模な生産が可能になるということが明ら
かである。トランスジェニック抗体の濃度は乳汁におい
てよりも初乳においての方がより高いということもまた
明らかである。さらに、トランスジーンの存在は、大量
の内因性の抗体を作るという動物の能力に影響を及ぼさ
ない。動物は著しく免疫不全または不健康な状態の徴候
を示さない。
u鎖を使用して抗原特異的ハイブリドーマが生産され
た。例1に記載されるトランスジェニックマウスが、抗
原結合部位に対するH鎖の寄与がトランスジェニックヒ
トH鎖ミニ遺伝子座によってもたらされる抗原特異的抗
体を生産するために使用できることを示すために、該ト
ランスジェニックマウスは107 のヒツジ赤血球(SR
C)で免疫処置された。脾臓細胞が6日後NSO形質細
胞腫と融合された(ケーラー(Kohler)およびミルスタイ
ン(Milstein)、ネイチャ(Nature)、256号、495頁
ないし497頁、1975年)。細胞は、予期される播
種頻度がウェルあたり1ハイブリドーマであるように9
6−ウェルコスタープレートで培養された。ヒトmu陽
性ハイブリッドが、ビオチニル化された抗ヒトIgMを
使用しELISAにおいて検出された。抗原特異的ハイ
ブリッドは、ヒツジ赤血球を使用し赤血球凝集において
同定された。ELISAによって決定されたように、ヒ
ツジ赤血球に特異的な抗体を含み、かつヒトmuを含
み、しかしマウスmuまたはマウスガンマH鎖のどちら
も含まないウェルが選ばれた。
れる抗体が本当にヒトmu/マウスL鎖抗SRC免疫グ
ロブリンであることを示すために、蛍光活性化セルソー
タ(FACS)における分析が使用された。FACS分
析のために、107 のヒツジ赤血球が30分間20ul
培養上清とともにインキュベートされ、リン酸塩緩衝生
理食塩水で一度洗われ、さらにビオチニル化された抗ヒ
トmuH鎖抗血清、ビオチニル化された抗マウスmu抗
血清またはビオチニル化された抗マウスカッパL鎖抗血
清のどれかとともにインキュベートされた。30分後細
胞は、前のように洗われ、かつFITC結合されたスト
レプトアビジンとともにインキュベートされた。細胞は
30分後に洗われ、ゆるやかな破壊の後、分析のための
用意ができた。
Mを生産する3つの異なったハイブリッドに対する結果
が図6、図7および図8のFACSヒストグラムにそれ
ぞれ示されている。
Dは異なった染色を表示する。図6A、図7A、図8A
は、ヒツジ赤血球だけ、抗体とともにインキュベートさ
れたヒツジ赤血球、またはフルオレセイン化された(F
ITC)第2の抗体(抗ヒトmu抗マウスmu、抗マウ
スカッパのどれか)とともにインキュベートされたヒツ
ジ赤血球を使用した陰性のコントロールに対する結果で
ある。図6B、図7B、図8Bは、ハイブリッド培養上
清およびフルオレセイン化された(FITC)抗ヒトm
uとともにインキュベートされたヒツジ赤血球を使用し
た結果である。図6C、図7C、図8Cは、トランスジ
ェニックハイブリッドからの培養上清およびフルオレセ
イン化された(FITC)抗マウスmuとともにインキ
ュベートされたヒツジ赤血球を使用した結果である。図
6Dは、ハイブリッド培養上清およびフルオレセイン化
された(FITC)抗マウスカッパとともにインキュベ
ートされたヒツジ赤血球を使用した結果である。
光強度が細胞数に対してプロットされる。図7において
は、細胞の固定数の蛍光強度が散点に対してプロットさ
れ、各点は細胞を表わす。
蛍光)は、ヒトmuH鎖およびマウスカッパL鎖を含む
抗体に対してのみ見ることができるが、マウスmuH鎖
またはマウスガンマH鎖を含む抗体に対しては見ること
ができない(図示せず)ポジティブ染色を示している。
スジェニックマウスから誘導されるハイブリドーマから
のおよび組織からのDNAのサザンブロット分析を表わ
す図である。
ーマからの細胞質RNAのノーザンブロット分析を表わ
す図である。
イブリドーマの2つによって分泌された免疫グロブリン
の分析を表わす図である。
す図である。
の蛍光強度を示す一連のFACSヒストグラムを表わす
図である。
蛍光強度を示す一連のFACSプロファイルであり、各
点は細胞を表わす図である。
トグラムを表わす図である。
Claims (11)
- 【請求項1】 ヒト由来免疫グロブリンのH鎖領域をコ
ードする遺伝子セグメントを含み、ヒト由来の免疫グロ
ブリンの少なくとも一部をコードする外来DNAを、ヒ
ト以外の動物の生殖系列内に導入することにより、ヒト
以外のトランスジェニック動物を生産し、 それにより、前記外来起源のDNAを、免疫グロブリ
ン、免疫グロブリンの断片、あるいはキメラの免疫グロ
ブリン分子をコードする多様な再配列した遺伝子を生産
するように、前記トランスジェニック動物のリンパ組織
内において再配列または変異させ、 それにより、前記トランスジェニック動物を特定の抗原
で攻撃することに続いて、前記再配列または変異された
DNAにコードされた前記特定の抗原に対する前記免疫
グロブリンを、前記動物の細胞内または体液内において
発現させるステップと、 前記動物の細胞または適当な体液から免疫グロブリンを
得るステップと、を備える、特定の抗原に対する免疫グ
ロブリンを生産する方法。 - 【請求項2】 前記免疫グロブリンを含むポリクローナ
ル抗体が前記動物から得られる、請求項1に記載の方
法。 - 【請求項3】 前記免疫グロブリンを含むモノクローナ
ル抗体が前記動物から得られる細胞を用いて生産され
る、請求項1に記載の方法。 - 【請求項4】 前記免疫グロブリンは前記動物の体液内
または分泌液内において生産される、請求項1に記載の
方法。 - 【請求項5】 前記免疫グロブリンは前記動物から得ら
れる細胞からインビトロで生産される、請求項1に記載
の方法。 - 【請求項6】 前記導入されたDNAは免疫グロブリン
の種特異的な全領域を実質的にコードする、請求項1〜
5のいずれかに記載の方法。 - 【請求項7】 前記トランスジェニック動物はマウスで
ある、請求項1〜6のいずれかに記載の方法。 - 【請求項8】 前記導入されたDNAは単数のプラスミ
ドまたはコスミド、複数のプラスミドまたはコスミド、
酵母人工染色体、あるいは脊椎動物の染色体またはDN
Aの断片を構成要素として含む、請求項1〜7のいずれ
かに記載の方法。 - 【請求項9】 前記DNAは受精卵または胚性幹細胞に
注射または他の方法により導入される、請求項1〜8の
いずれかに記載の方法。 - 【請求項10】 前記動物は免疫グロブリンの定常領域
をコードする遺伝物質を最初は保有していない、請求項
1〜9のいずれかに記載の方法。 - 【請求項11】 請求項1〜10のいずれかに記載の方
法により得ることのできる、外来起源の免疫グロブリ
ン。
Applications Claiming Priority (2)
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GB8823869.6 | 1988-10-12 | ||
GB888823869A GB8823869D0 (en) | 1988-10-12 | 1988-10-12 | Production of antibodies |
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JP51081289A Division JP3484442B2 (ja) | 1988-10-12 | 1989-10-12 | トランスジェニック動物からの抗体の生産 |
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JP2003192699A true JP2003192699A (ja) | 2003-07-09 |
JP2003192699A5 JP2003192699A5 (ja) | 2004-07-15 |
JP3871997B2 JP3871997B2 (ja) | 2007-01-24 |
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JP51081289A Expired - Lifetime JP3484442B2 (ja) | 1988-10-12 | 1989-10-12 | トランスジェニック動物からの抗体の生産 |
JP2002314611A Expired - Lifetime JP3871997B2 (ja) | 1988-10-12 | 2002-10-29 | トランスジェニック動物からの抗体の生産 |
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JP51081289A Expired - Lifetime JP3484442B2 (ja) | 1988-10-12 | 1989-10-12 | トランスジェニック動物からの抗体の生産 |
Country Status (9)
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US (1) | US5545807A (ja) |
EP (1) | EP0438474B1 (ja) |
JP (2) | JP3484442B2 (ja) |
KR (1) | KR0164608B1 (ja) |
AT (1) | ATE138104T1 (ja) |
AU (1) | AU4417389A (ja) |
DE (1) | DE68926508T2 (ja) |
GB (1) | GB8823869D0 (ja) |
WO (1) | WO1990004036A1 (ja) |
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ATE141646T1 (de) * | 1986-04-09 | 1996-09-15 | Genzyme Corp | Genetisch transformierte tiere, die ein gewünschtes protein in milch absondern |
GB8615942D0 (en) * | 1986-06-30 | 1986-08-06 | Animal & Food Research Council | Peptide production |
WO1988001648A1 (en) * | 1986-08-28 | 1988-03-10 | Immunex Corporation | Expression of heterologous proteins by transgenic lactating mammals |
EP0273085A1 (en) * | 1986-12-29 | 1988-07-06 | IntraCel Corporation | A method for internalizing nucleic acids into eukaryotic cells |
US4873316A (en) * | 1987-06-23 | 1989-10-10 | Biogen, Inc. | Isolation of exogenous recombinant proteins from the milk of transgenic mammals |
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1988
- 1988-10-12 GB GB888823869A patent/GB8823869D0/en active Pending
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1989
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- 1989-10-12 KR KR1019900701247A patent/KR0164608B1/ko not_active IP Right Cessation
- 1989-10-12 DE DE68926508T patent/DE68926508T2/de not_active Expired - Lifetime
- 1989-10-12 JP JP51081289A patent/JP3484442B2/ja not_active Expired - Lifetime
- 1989-10-12 AT AT89911584T patent/ATE138104T1/de not_active IP Right Cessation
- 1989-10-12 WO PCT/GB1989/001207 patent/WO1990004036A1/en active IP Right Grant
- 1989-10-12 AU AU44173/89A patent/AU4417389A/en not_active Abandoned
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WO1990004036A1 (en) | 1990-04-19 |
ATE138104T1 (de) | 1996-06-15 |
JP3484442B2 (ja) | 2004-01-06 |
GB8823869D0 (en) | 1988-11-16 |
EP0438474B1 (en) | 1996-05-15 |
DE68926508D1 (de) | 1996-06-20 |
KR0164608B1 (ko) | 1999-01-15 |
US5545807A (en) | 1996-08-13 |
JPH04500911A (ja) | 1992-02-20 |
JP3871997B2 (ja) | 2007-01-24 |
AU4417389A (en) | 1990-05-01 |
KR900702049A (ko) | 1990-12-05 |
EP0438474A1 (en) | 1991-07-31 |
DE68926508T2 (de) | 1996-10-31 |
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