JP2005524379A - 抗体依存性細胞傷害性の増強を伴う抗体グリコシル化改変体 - Google Patents
抗体依存性細胞傷害性の増強を伴う抗体グリコシル化改変体 Download PDFInfo
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Abstract
Description
(発明の分野)
本発明は、タンパク質のグリコシル化操作の分野に関する。より詳細には、本発明は、改良された処置的特性を有するタンパク質(抗体依存性細胞傷害性の増強を伴う抗体)を生成するためのグリコシル化操作に関する。
糖タンパク質は、ヒト、その他の真核生物およびいくつかの原核生物における多数の不可欠な機能(触媒作用、シグナル伝達、細胞間コミュニケーション、ならびに分子認識および会合)を媒介する。それらは、真核生物において非細胞質ゾルタンパク質の大部分を構成する(Lisら、Eur.J.Biochem.218:1−27(1993))。多数の糖タンパク質が処置目的のために開発されてきており、過去20年の間、天然に存在する分泌糖タンパク質の組換えバージョンが生物工学産業の主要な産物であった。例としては、エリスロポエチン(EPO)、処置用モノクローナル抗体(処置用mAb)、組織プラスミノーゲンアクチベータ(tPA)、インターフェロン−β(IFN−β)、顆粒球−マクロファージコロニー刺激因子(GM−CSF)およびヒト絨毛性ゴナドトロピン(hCG)が挙げられる(Cummingら、Glycobiology 1:115−130(1991))。
テトラサイクリン調節様式で、N−アセチルグルコサミニルトランスフェラーゼIII(GnTIII;EC2.1.4.144)を過剰発現する遺伝子操作されたmAb産生細胞株を用いて、抗−CD20モノクローナル抗体(mAb)IDEC−C2B8(Rituximab)および抗癌mAb chG250の新規のグリコシル化改変体を、本発明者等はここに生成した。GnTIIIは、天然に存在するヒト抗体中に低から中レベルで見出されるが、標準工業細胞株中に産生されるmAbを欠いているバイセクトオリゴ糖の合成に必要とされる。新規のグリコシル化バージョンは、MabtheraTM(欧州で販売されているRixtuximabのバージョン)およびマウスミエローマ由来chG250より生物学的(ADCC)活性が優れていた。例えば、MabtheraTMのような最大ADCC活性に達するために必要とされる量は、最高レベルのバイセクトオリゴ糖を保有する改変体では10分の1であった。chG250に関しては、最高レベルのバイセクトオリゴ糖を保有する改変体は、非修飾コントロールchG250にさらに低いADCC活性を検出するために必要とされるものの125分の1の濃度で有意のADCC活性を媒介した。GnTIII発現およびADCC活性のレベル間に明らかな相関が見出された。
用語は、別に定義しない限り、以下のように当該技術分野で一般的に用いられるように本明細書中で用いられる。
「ヒト免疫エフェクター細胞」は、抗体またはFc融合タンパク質のFc領域と結合し、エフェクター機能を実施する、それらの表面上にFc受容体を提示する白血球の集団である。このような集団としては、末梢血単核球(PBMC)および/またはナチュラルキラー(NK)細胞が挙げられ得るが、これらに限定されない。
1)本アッセイは、抗体の抗原結合領域により認識される標的抗原を発現することが既知である標的細胞を用いる。
i)PBMCを、標準密度遠心分離法を用いて単離し、5×106細胞/mlでRPMI細胞培地中に懸濁する。
本発明は、グリコフォームの抗体または抗体フラグメント、あるいは抗体依存性細胞傷害性の増強を伴う抗体フラグメントを含む融合タンパク質の産生のための宿主細胞系の生成および使用の方法を提供する。標的エピトープの同定、ならびにグリコシル化パターンの変更が望ましい潜在的処置値を有する抗体の生成、ならびにそれらのそれぞれのコード核酸配列の単離は、本発明の範囲内である。
本発明は、変更されたグリコシル化パターンを有するタンパク質の生成のための宿主細胞発現系を提供する。特に本発明は、改良された処置値を有するグリコフォームのタンパク質の生成のための宿主細胞系を提供する。したがって、本発明は、糖タンパク質修飾グリコシルトランスフェラーゼ、すなわちβ(1,4)−N−アセチルグルコサミニルトランスフェラーゼIII(GnTIII)の発現を増強するよう選択または操作された宿主細胞発現系を提供する。特に、このような宿主細胞発現系は、任意に構成的プロモーター系または調節プロモーター系に作動可能に連結されるGnTIIIをコードする組換え核酸分子を含むように操作され得る。あるいは、GnTIIIを天然に産生し、産生するよう誘導され、かつ/または産生するよう選択される宿主細胞発現系が用いられ得る。
当業者に既知である方法を用いて、目的のタンパク質のコード配列、ならびにGnTIIIおよび適切な転写/翻訳制御シグナルのコード配列を含有する発現ベクターを構築し得る。これらの方法としては、組換えDNA法、合成法およびインビボ組換え/遺伝子組換えが挙げられる(例えば、Maniatisら、Molecular Cloning A Laboratory Manual,Cold Spring Harbor Laboratory,N.Y.(1989)およびAusubelら、Current Protocols in Molecular Biology,Greene Pubulishing AssociatesおよびWiley Interscience,N.Y.(1989)に記載された技法を参照)。
コード配列を含有し、生物学的に活性な遺伝子産物を発現する宿主細胞は、少なくとも4つの一般的アプローチにより同定され得る;(a)DNA−DNAハイブリダイゼーションまたはDNA−RNAハイブリダイゼーション;(b)「マーカー」遺伝子機能の存在または非存在;(c)宿主細胞中のそれぞれのmRNA転写体の発現により測定した場合の転写のレベルの評価;および(d)イムノアッセイにより、またはその生物学的活性により測定した場合の遺伝子産物の検出。
(i.抗体依存性細胞傷害性の増強を伴う抗体の生成および使用)
好ましい実施形態において、本発明は、抗体依存性細胞傷害性の増強を伴うグリコフォームの抗体および抗体フラグメントを提供する。
上記のように、本発明は、処置用抗体のADCC活性を増強するための方法に関する。これは、このような抗体のFc領域のグリコシル化パターンを操作することにより、特にそれらのFc領域の保存グリコシル化部位にN結合されるバイセクト複合オリゴ糖およびバイセクトハイブリッドオリゴ糖を保有する抗体分子の割合を最大にすることにより、達成される。この戦略は、処置用抗体によってだけでなく、免疫グロブリンのFc領域と等価である領域を保有する任意の分子により媒介される望ましくない細胞に対するFc媒介性細胞傷害性を増強するために適用され得るが、これは、グリコシル化の操作により導入される変化が、Fc領域のみに、したがってADCCメカニズムに関与するエフェクター細胞の表面のFc受容体とのその相互作用に、影響を及ぼすためである。本明細書に開示された方法が適用され得るFc含有分子としては、(a)Fc領域のN末端に融合されたターゲッティングタンパク質ドメインから作製される可溶性融合タンパク質(ChamovおよびAshkenazi,Trends Biotech.14:52(1996))、および(b)Fc領域のN末端に融合された原形質膜に局在化されるII型膜貫通ドメインから作製される原形質膜固定融合タンパク質(Stabila,P.F.,Nature Biotech.16:1357(1998))が挙げられるが、これらに限定されない。
(IDEC−CEB8産生細胞株のグリコシル化操作により得られる、増強された抗体依存性細胞傷害性を有する、キメラ抗CD20抗体IDEC−C2B8の新規バージョン)
IDEC−C2B8のVHおよびVLのコード領域の合成ならびに哺乳動物発現ベクターの構築。IDEC−C2B8抗体のVHおよびVL領域をコードするcDNAを、PCRを用いて、一段階法で、一組の重複一本鎖オリゴヌクレオチドから構築した(Kobayashi,N.ら、Biotechniques 23:500−503(1997))。国際公開特許出願(国際公開番号WO94/11026)から、IDEC−C2B8 VLおよびVHをコードするオリジナル配列データを得た。構築されたVLおよびVHcDNAフラグメントをpBluescriptIIKS(+)にサブクローニングし、配列決定して、オリジナルアミノ酸残基配列を変更せずに、可変領域および定常領域接合部に導入された独特の制限部位を用いて、それぞれヒト定常軽鎖(Igκ)および重鎖(IgG1)cDNAへの連結により直接結合した(Umana,P.ら、Nat Biotechnol.17:176−180(1999);Reff,M.E.ら、Blood 83:435−445(1994))。各完全長cDNAをpcDNA3.1(+)(Invitrogen,Leek,The Netherlands)に個別にサブクローニングし、キメラC2B8軽鎖(pC2B8L)および重鎖(pC2B8H)に関する哺乳動物発現ベクターを得た。
IDEC−C2B8の産生および特異的抗原結合の立証。GnTIIIの安定テトラサイクリン調節発現およびIDEC−C2B8の安定構成性発現を示すCHO−tet−GnTIII細胞を確立し、一組の抗体サンプルの産生のためにスケールアップした。スケールアップ中、同一クローンからの並行培養を、3つの異なるテトラサイクリン濃度、25ng/ml、50ng/mlおよび2000ng/ml下で増殖させた。これらのレベルのテトラサイクリンは、異なるレベルのGnTIIIおよびバイセクトオリゴ糖を生じることが以前に示されている(Umana,P.ら、Nat Biotechnol.17:176−180(1999);Umana,P.ら、Biotechnol.Bioeng.65:542−549(1999))。GnTIIIを発現しないC2B8産生コントロール細胞株も確立し、CHO−tet−GnTIIIの3つの並行培養に関するのと同一条件下で培養した。プロテインAアフィニティークロマトグラフィー後、SDS−PAGEおよびクーマシーブルー染色により、mAb純度を95%より高いと概算した。それらの産生のために培養培地に添加されたテトラサイクリン濃度に従い、サンプルを以下のように命名した:C2B8−25t、C2B8−50t、C2B8−2000tおよびC2B8−nt(すなわち非バイセクトコントロールに関しては無テトラサイクリン)。サンプルC2B8−25tは、CD20陽性細胞およびCD20陰性細胞を用いた間接的免疫蛍光法により、特異的抗原結合を示したが(図1)、これは、合成VLおよびVHの遺伝子フラグメントが機能的に誤りがなかったことを示す。
異なるC2B8mAbグリコシル化改変体を、CD20陽性SB細胞のインビトロ溶解として測定したADCC活性について比較した。GnTIIIを欠いている親細胞株由来の、さらに別のmAbサンプルであるC2B8−ntも試験した。基底GnTIII発現レベルで産生され、低レベルのバイセクトオリゴ糖を保有するサンプルC2B8−2000tは、C2B8−tよりわずかに活性であった(図4A)。GnTIII発現の次に高いレベルでは、サンプルC2B8−50tはほぼ等レベルのバイセクトオリゴ糖および非バイセクトオリゴ糖を保有したが、有意により高い標的細胞溶解を媒介しなかった。しかしながら、最低テトラサイクリン濃度では、80%までのバイセクトオリゴ糖構造を含有するサンプルC2B8−25tは、全抗体濃度範囲で、残りのサンプルより有意に活性であった。C2B8−25tは10分の1の抗体濃度で、サンプルC2B8−ntの最大レベルのADCC活性に達した(図4A)。サンプルC2B8−25tは、コントロールに関しての最大ADCC活性の有意の増強も示した(50%対30%溶解)。
(chG250産生細胞株のグリコシル化操作により得られる抗体依存性細胞傷害性の増強を伴う、抗腎細胞癌抗体chG250の新規バージョン)
(1.細胞培養)
chG250キメラmAbを産生するSP2/0マウスミエローマ細胞(wt−chG250−SP2/0細胞)を、1:100(容量/容量)のペニシリン/ストレプトマイシン/抗真菌性溶液(SIGMA,Buchs,Switzerland)を補充した標準細胞培地中で増殖させた。細胞を、組織培養フラスコ中で5%CO2湿潤大気中、37℃で培養した。培地を、3〜4日ごとに取り替えた。細胞を、10%DMSOを含有する培地中で凍結させた。
IRESを介してプロマイシン耐性遺伝子に作動可能に連結されるGnTIIIの構成性発現のためのベクターを用いて、電気穿孔により、wt−chG250−SP2/0ミエローマ細胞をトランスフェクトした。電気穿孔の24時間前に、培地を取り替えて、細胞を5×105細胞/mlで接種した。700万個の細胞を、4℃にて1300rmpで4分間、遠心分離した。細胞を3mLの新しい培地で洗浄し、再び遠心分離した。培地中の1.25%(容量/容量)DMSOおよび20〜30μgのDNAを含有する反応混合物0.3〜0.5mlの容量中に細胞を再懸濁した。次に電気穿孔混合物を0.4cmキュベットに移して、遺伝子パルサー(Bio Rad製)を用いて、低電圧(250〜300V)および高キャパシタンス(960μF)でパルスをかけた。電気穿孔後、細胞を迅速にT25培養フラスコ中の6mLの1.25%(容量/容量)DMSO培地に移して、37℃でインキュベートした。電気穿孔後2日目に培地に2μg/mLのプロマイシンを適用することにより、安定構成部分を選択した。2〜3週間後、安定したプロマイシン耐性混合集団を得た。単一細胞由来クローンをFACSにより得て、その後、展開し、プロマイシン選択下で保持した。
ウエスタンブロッティングにより、GnTIII発現に関してプロマイシン耐性クローンをスクリーニングした。ウエスタンブロットは、クローン5H12、4E6および4E8が最高レベルのGnTIIIを発現していることを明らかに示した。5G2も中強度のGnTIII帯域を示したが、2F1、3D3および4G3は最低帯域強度を有し、したがって低量のGnTIIIを発現した(図5)。
クローン2F1、3D3、4E6、4E8、4G3、5G2、5H12および野生型(wt−chG250−SP2/0細胞)を、130ml培地の総容量中に3×105細胞/mLで接種し、単一三重フラスコ中で培養した。接種のために用いた細胞は、すべて完全対数増殖期であり、したがって細胞は、生産バッチ開始時に同一の増殖状態であったと考えられた。細胞を4日間培養した。抗体を含有する上清を後期対数増殖期に収集して、再現性を保証した。chG250モノクローナル抗体を、2クロマトグラフィー工程で精製した。各バッチから得られたchG250モノクローナル抗体を含有する培養上清をまず、HiTrapプロテインAアフィニティークロマトグラフィーを用いて精製した。プロテインAは、ヒトIgGFc領域に高度に特異的である。プロテイン溶離物からのプールサンプルを、ResourceS 1mlカラム(Amersham Pharmacia Biotech)上での陽イオン交換クロマトグラフィーによりPBSに緩衝液交換した。SDS染色およびクーマシーブルー染色から、最終純度を95%より高いと判定した(図6)。既知の濃度を有する野生型抗体を用いた標準較正曲線で、各サンプルの濃度を確定した。
異なるオリゴ糖構造の分子量を正確に提供するマトリクス支援レーザ脱離/イオン化飛行時間型質量分析法(MALDI/TOF−MS)によって、オリゴ糖プロフィールを得た。この技法は、混合物内の異なるオリゴ糖構造間の割合の定量的分析を可能にする。中性オリゴ糖は、主に[M+Na+]イオンとして出現したが、時としてそれらはより小さい[M+K+]イオンを伴い、m/z16の質量増大をもたらした。カリウムイオン付加物として出現する構造のパーセンテージはマトリクスの含量に依存し、したがってサンプル間で変化し得る。各抗体調製物由来の中性N結合型オリゴ糖の混合物を、マトリクスとして2,5−デヒドロ安息香酸(2,5−DHB)を用いて分析した。既知の単糖組成および独特の質量のために、スペクトル中のピークのいくつかは、特定のオリゴ糖構造に明確に割り当てられた。しかしながら、多重構造はしばしば、特定の質量に割り当てられ得る。MALDIによって質量を確定することはできるが、異性体間の区別はできない。生合成経路についての知識および過去の構造データは、ほとんどの場合に、スペクトル中のピークへのオリゴ糖構造の割り当てを可能にする。
細胞傷害性を測定するカルセイン−AM保持法は、抗体を用いたインキュベーション後に細胞中に残留する染料蛍光を測定する。400万個のG250抗原陽性細胞(標的)を、10%ウシ胎仔血清を補充した1.8mLのRPMI−1640細胞培地(GIBCO BRL,Basel,Switzerland)中の10μMのカルセイン−AM(Molecular Probes,Eugene,OR)を用いて、5%CO2湿潤大気中で37℃にて30分間標識した。細胞を培地中で2回洗浄し、12mLのAIMV無血清培地(GIBCO BRL, Basel, Switzerland)中に再懸濁した。次に、標識細胞をU底96ウェルに移し(30,000細胞/ウェル)、異なる濃度の抗体を用いて、4℃で1時間、三連でインキュベートした。フィコール−パック(Pharmacia Biotech,Dubendorf,Switzerland)勾配上での遠心分離により、ヘパリン処理新鮮ヒト血液(全実験において、同一健常ドナーから得た)から末梢血単核球(PBMC)を分離した。PBMCを50μL容量で三連ウェルに添加し、25:1のエフェクター対標的比(E:T比)および200μLの最終容量を生じた。次に96ウエルプレートを、5%CO2大気中で37℃にて4時間インキュベートした。その後、96ウエルプレートを700×gで5分間遠心分離し、上清を捨てた。細胞ペレットをハンクス平衡塩溶液(HBSS)で2回洗浄し、200μLの0.05M ホウ酸ナトリウム、pH9、0.1%トリトンX−100中で溶解した。標的細胞中の蛍光染料の保持を、FLUOstar微小プレート読取器(BMG LabTechnologies,Offenburg,Germany)で測定した。抗体に曝露する代わりに、サポニン(AIMV中200μg/mL;SIGMA,Buchs,Switzerland)に標的細胞を曝露することにより、特異的溶解を総溶解コントロールに関して算定した。以下の式を用いて、特異的溶解(%)を算定した:
細胞傷害性%=(Fmed−Fexp)/(Fmed−Fdet)
(式中、Fmedは培地単独で処理した標的細胞の蛍光を表し、PMBCによる非特異的溶解を考察し、Fexpは抗体で処理した細胞の蛍光を表し、Fdetは抗体の代わりにサポニンで処理した細胞の蛍光を表す)。
(慢性対宿主性移植片病を有する患者における免疫媒介性血小板減少症の処置)
慢性対宿主性移植片病における自己免疫血小板減少症は、臨床疾患を引き起こすB細胞調節不全の一例を示す。慢性対宿主性移植片病を有する被験者における免疫媒介性血小板減少症を処置するために、本発明の方法により調製され、ADCCの増強を伴う抗CD20キメラモノクローナル抗体を、Ratanatharathorn,V.ら、Ann.Intern.Med.133(4):275−79(2000)(この記載内容全体が、参照により本明細書中に援用される)に記載されたように被験者に投与する。特に、抗体375mg/m2の毎週注入を被験者に4週間施した。抗体療法は、末梢血中のB細胞の顕著な枯渇ならびに血小板関連抗体レベルの低減を生じた。
(重症免疫媒介性赤芽球ろうおよび溶血性貧血の処置)
免疫媒介性後天性赤芽球ろう(PRCA)は、しばしばその他の自己免疫現象に関連するまれな障害である。被験者における免疫媒介性後天性赤芽球ろうを処置するために、本発明の方法により調製され、ADCCの増殖を伴う抗CD20キメラモノクローナル抗体を、Zecca,M.ら、Blood 12:3995−97(1997)(この記載内容全体が、参照により本明細書中に援用される)に記載されたように、被験者に投与する。特に、PRCAおよび自己免疫性溶血性貧血を有する被験者には、抗体375mg/m2/週を2用量投与する。抗体療法後、静脈内免疫グロブリンを用いた変換処置を開始する。この処置は、B細胞の顕著な枯渇およびヘモグロビンレベル増大を伴う網状赤血球数の有意の増大を生じる。
Claims (38)
- β(1,4)−N−アセチルグルコサミニルトランスフェラーゼIII(GnTIII)をコードする少なくとも1つの核酸の発現によりFc媒介性細胞傷害性の増強を伴うポリペプチドを産生するよう操作された宿主細胞であって、該宿主細胞により産生される該ポリペプチドは、全抗体分子、抗体フラグメント、および免疫グロブリンのFc領域と等価の領域を含む融合タンパク質から成る群から選択され、ここで、該GnTIIIは、Fc領域中にバイセクト複合オリゴ糖を保有するポリペプチドと比較して、Fc領域中にバイセクトハイブリッドオリゴ糖またはガラクトシル化複合オリゴ糖、あるいはそれらの混合物を保有する該ポリペプチドの割合を増大するのに十分な量で発現される、宿主細胞。
- 前記ポリペプチドがIgGまたはそのフラグメントである、請求項1に記載の宿主細胞。
- 前記ポリペプチドがIgG1またはそのフラグメントである、請求項1に記載の宿主細胞。
- 前記ポリペプチドがヒトIgGのFc領域と等価の領域を含む融合タンパク質である、請求項1に記載の宿主細胞。
- GnTIIIをコードする少なくとも1つの遺伝子を含む核酸分子が前記宿主細胞中に導入されている、請求項1に記載の宿主細胞。
- 内因性GnTIII遺伝子が活性化されるよう操作されている、請求項1に記載の宿主細胞。
- 前記内因性GnTIIIが宿主染色体中への遺伝子発現を増強するDNA要素の挿入により活性化されている、請求項6に記載の宿主細胞。
- 内因性GnTIIIの発現を誘発する突然変異を保有するよう選択されている、請求項6に記載の宿主細胞。
- CHO細胞変異体lec10である、請求項8に記載の宿主細胞。
- CHO細胞、BHK細胞、NS0細胞、SP2/0細胞、Y0ミエローマ細胞、P3X63マウスミエローマ細胞、PER細胞、PER.C6細胞またはハイブリドーマ細胞である、請求項1に記載の宿主細胞。
- 前記ポリペプチドが抗CD20抗体である、請求項10に記載の宿主細胞。
- 前記抗CD20抗体がIDEC−C2B8である、請求項11に記載の宿主細胞。
- SP2/0細胞である、請求項10に記載の宿主細胞。
- 前記抗体がキメラ抗ヒト腎細胞癌モノクローナル抗体chG250である、請求項13に記載の宿主細胞。
- GnTIIIをコードする前記少なくとも1つの遺伝子が前記宿主細胞染色体中に導入されている、請求項5に記載の宿主細胞。
- 前記内因性GnTIIIは、前記宿主細胞染色体中へのプロモーター要素、トランスポゾンまたはレトロウイルス要素の挿入により活性化されている、請求項6に記載の宿主細胞。
- 抗体分子、抗体フラグメントまたは免疫グロブリンのFc領域と等価の領域を含む融合タンパク質をコードする少なくとも1つのトランスフェクトされた核酸をさらに含む、請求項1に記載の宿主細胞。
- GnTIIIをコードする前記少なくとも1つの核酸が、構成プロモーター要素に作動可能に連結される、請求項1に記載の宿主細胞。
- 請求項17に記載の宿主細胞であって、該宿主細胞は、以下:抗CD20抗体、キメラ抗ヒト神経芽細胞腫モノクローナル抗体chCE7、キメラ抗ヒト腎細胞癌モノクローナル抗体chG250、キメラ抗ヒト結腸、肺および乳癌モノクローナル抗体ING−1、ヒト化抗ヒト17−1A抗原モノクローナル抗体3622W94、ヒト化抗ヒト結腸直腸腫瘍抗体A33、GD3ガングリオシドR24に対して向けられる抗ヒト黒色腫抗体、キメラ抗ヒト扁平上皮細胞癌モノクローナル抗体SF−25、抗ヒトEGFR抗体、抗ヒトEGFRvIII抗体、抗ヒトPSMA抗体、抗ヒトPSCA抗体、抗ヒトCD22抗体、抗ヒトCD30抗体、抗ヒトCD33抗体、抗ヒトCD38抗体、抗ヒトCD40抗体、抗ヒトCD45抗体、抗ヒトCD52抗体、抗ヒトCD138抗体、抗ヒトHLA−DR改変体抗体、抗ヒトEpCAM抗体、抗ヒトCEA抗体、抗ヒトMUC1抗体、抗ヒトMUC1コアタンパク質抗体、抗ヒト異常グリコシル化MUC1抗体、ED−Bドメインを含有するヒトフィブロネクチン改変体に対する抗体または抗ヒトHER2/neu抗体、
をコードする少なくとも1つのトランスフェクトされた核酸を含む、宿主細胞。 - 宿主細胞中でのポリペプチドの産生方法であって、該方法は、Fc媒介性細胞傷害性の増強を伴う前記ポリペプチドの産生を可能にする条件下で、請求項1〜19のいずれか一項記載の宿主細胞を培養する工程を包含する、方法。
- Fc媒介性細胞傷害性の増強を伴う前記ポリペプチドを単離する工程をさらに包含する、請求項20に記載の方法。
- 前記宿主細胞が、免疫グロブリンのFc領域と等価の領域を含む融合タンパク質をコードする少なくとも1つの核酸を含む、請求項20に記載の方法。
- 前記ポリペプチドのFc領域中の50%より多いオリゴ糖がバイセクトされる、請求項20に記載の方法。
- 前記ポリペプチドのFc領域中の70%より多いオリゴ糖がバイセクトされる、請求項20に記載の方法。
- Fc領域中のバイセクトハイブリッドオリゴ糖またはガラクトシル化複合オリゴ糖あるいはそれらの混合物の割合が、前記ポリペプチドのFc領域中のバイセクト複合オリゴ糖の割合より大きい、請求項20に記載の方法。
- 前記ポリペプチドは、抗CD20抗体IDEC−C2B8であり、前記宿主細胞により産生されるIDEC−C2B8抗体は、MALDI/TOF−MSにより分析した場合に、図2Eに示されるものと実質的に等価であるグリコシル化プロフィールを有する、請求項20に記載の方法。
- 前記ポリペプチドは、chG250モノクローナル抗体であり、前記宿主細胞により産生される前記chG250抗体は、MALDI/TOF−MSにより分析した場合に、図7Dに示されるものと実質的に等価であるグリコシル化プロフィールを有する、請求項20に記載の方法。
- 請求項21に記載の方法により産生される抗体依存性細胞傷害性(ADCC)の増強を伴う、抗体。
- IDEC−C2B8、chCE7、ch−G250、ヒト化抗HER2モノクローナル抗体、ING−1、3622W94、SF−25、A33およびR24から成る群から選択される、請求項28に記載の抗体。
- 免疫グロブリンのFc領域と等価の領域を含み、請求項21に記載の方法により産生されるFc媒介性細胞傷害性の増強を伴う、抗体フラグメント。
- 免疫グロブリンのFc領域と等価の領域を含み、かつ請求項21に記載の方法により産生されるFc媒介性細胞傷害性の増強を伴う、融合タンパク質。
- 請求項28に記載の抗体および薬学的に受容可能なキャリアを含む、薬学的組成物。
- 請求項30に記載の抗体フラグメントおよび薬学的に受容可能なキャリアを含む、薬学的組成物。
- 請求項31に記載の融合タンパク質および薬学的に受容可能なキャリアを含む、薬学的組成物。
- 請求項32〜34のいずれか一項に記載の処置上有効な量の薬学的組成物を、該薬学的組成物を必要とする患者に投与する工程を包含する、癌の処置方法。
- 処置上有効な量の抗体を、該抗体を必要とするヒト被験者に投与するこ工程を包含する、B細胞欠乏を基礎にした疾患処置の改良型方法であって、該改良が、請求項28に記載の方法により産生される処置上有効な量の抗体を投与する工程を包含する、改良型方法。
- 前記抗体が抗CD20モノクローナル抗体である、請求項36に記載の改良型方法。
- 前記抗CD20抗体がIDEC−C2B8である、請求項37に記載の改良型方法。
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