JP2004215670A - 免疫調節オリゴヌクレオチド - Google Patents
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Abstract
【解決手段】 式I:5’ X1X2CGX3X4 3’に従う少なくとも1つの核酸配列を含む、免疫刺激オリゴヌクレオチド:ここで、CGは、該オリゴヌクレオチドに免疫刺激能力を付与する非メチル化CpGジヌクレオチドであり;X1およびX2の少なくとも1つはプリンであり;そして、X3およびX4の少なくとも1つはピリミジンである。
【選択図】 なし
Description
(政府の援助)
本発明において得られる研究は、一部、米国衛生研究所認可番号 R29−AR42556−01号により援助された。従って、本発明のある種の権利が米国政府に与えられ得る。
1970年代には、幾人かの研究者が、高分子量DNAの細胞膜への結合を報告した(Lerner,R.A.,W.Meinke,およびD.A.Goldstein,1971,「二倍体ヒトリンパ球の細胞質における膜結合DNA」,Proc.Natl.Acad.Sci.USA 68:1212;Agrawal,S.K.,R.W.Wagner,P.K.McAllister,およびB.Rosenberg,1975,「白金−ピリミジン錯体を用いて電子顕微鏡により視覚化された腫瘍発生細胞における細胞表面結合核酸」,Proc.Natl.Acad.Sci.USA 72:928)。1985年には、Bennettらが、DNAのリンパ球への結合がリガンド−レセプター相互作用に類似することを初めて示した:すなわち、結合は飽和可能であり、競合的であり、そしてDNAのエンドサイトーシスおよび分解を引き起こす(Bennett,R.M.,G.T.Gabor,およびM.M.Merritt.1985,「DNAのヒト白血球への結合。DNAのレセプター媒介結合、インターナリゼーションおよび分解の証拠」,J.Clin.Invest.76:2182)。DNAと同様に、オリゴデオキシリボヌクレオチド(ODN)は、飽和可能であり、配列独立性であり、そして温度およびエネルギー依存性の様式で細胞に入り得る(Jaroszewski,J.W.,およびJ.S.Cohen,1991,「アンチセンスオリゴデオキシヌクレオチドの細胞取り込み」,Advanced Drug Delivery Reviews 6:235;Akhtar,S.,Y.Shoji,およびR.L.Juliano,1992,「アンチセンスオリゴヌクレオチドの生物学的安定性および膜輸送特性の薬学的局面」;Gene Regulation: Biology of Antisense RNA and DNA,R.P.Erickson,およびJ.G.Izant編,Raven Press,Ltd.New York,pp.133;ならびに、Zhao,Q.,T.Waldschmidt,E.Fisher,C.J.Herrera,およびA.M.Krieg,1994,「マウス骨髄B細胞前駆体における時期特異的オリゴヌクレオチド取り込み」,Blood 84:3660)。DNAまたはODN取り込みのレセプターはクローン化されておらず、そしてODN結合および細胞取り込みが高分子量DNAと同一のメカニズムを介して起こるのか異なるメカニズムを介して起こるのかはいまだ明らかではない。
(核酸の免疫効果)
いくつかのポリヌクレオチドが、生体応答調節因子として広範に評価されている。その最良の例は、おそらくポリ(I,C)であろう。これは、IFN産生の強力なインデューサーであり、そしてマクロファージのアクチベーターおよびNK活性のインデューサーである(Talmadge,J.E.,J.Adams,H.Phillips,M.Collins,B.Lenz,M.Schneider,E.Schlick,R.Ruffmann,R.H.Wiltrout,およびM.A.Chirigos,1985,「ポリ−L−リジンおよびカルボキシメチルセルロースと複合体化されたポリイノシン−ポリシチジル酸のマウスにおける免疫調節効果」,Cancer Res.45:1058;Wiltrout,R.H.,R.R.Salup,T.A.Twilley,およびJ.E.Talmadge,1985,「ポリリボヌクレオチドによるナチュラルキラー活性の免疫調節」,J.Biol.Resp.Mod.4:512;Krown,S.E.1986,「ガン処置におけるインターフェロンおよびインターフェロンインデューサー」,Sem.Oncol.13:207;ならびに、Ewel,C.H.,S.J.Urba,W.C.Kopp,J.W.Smith II,R.G.Steis,J.L.Rossio,D.L.Longo,M.J.Jones,W.G.Alvord,C.M.Pinsky,J.M.Beveridge,K.L.McNitt,および S.P.Creekmore,1992,「ガン患者におけるポリ−L−リジンおよびカルボキシメチルセルロースで複合体化されたポリイノシン−ポリシチジル酸とインターロイキン2の組み合わせ:臨床的および免疫学的効果」,Cans.Res.52:3005)。このマウスNKの活性化は、IFN β分泌の誘導のみに起因し得るようである(Ishikawa,R.,および C.A.Biron,1993,「IFN誘導およびそれに関連する脾臓白血球分布における変化」,J.Immunol.150:3713)。デオキシリボースは有効ではなかったので、この活性化はリボース糖に特異的であった。インビトロにおけるその強力な抗腫瘍活性により、(RNAseによる分解を減少させるために)ポリ−L−リジンおよびカルボキシメチルセルロースで複合体化されたポリ(I,C)を用いるいくつかの臨床的試験がなされている(Talmadge,J.E.ら,1985,前述;Wiltrout,R.H.ら,1985,前述;Krown,S.E.ら,1986,前述;および、Ewel,C.H.ら,1992,前述)。不運なことに、毒性の副作用により、ポリ(I,C)は有用な治療薬剤になるにはほど遠かった。
(転写因子のCREB/ATFファミリーおよび複製におけるそれらの役割)
cAMP応答エレメント結合タンパク質(CREB)および活性化転写因子(ATF)、すなわち転写因子のCREB/ATFファミリーは、偏在して発現する転写因子のクラスであり、そのうちの11のメンバーが今までのところクローン化されている(de Groot,R.P.,およびP.Sassone−Corsi,「遺伝子発現のホルモンによる制御:環状アデノシン3’,5’−モノホスフェート−応答性核レギュレーターの多様性および多変性」,Mol.Endocrin.7:145,1993;Lee.K.A.W.,およびN.Masson,「CREBおよびその関連物質による転写調節」,Biochim.Biophys.Acta 1174:221,1993)。これらはすべて、塩基性領域/ロイシンジッパー(bZip)クラスのタンパク質に属する。すべての細胞は1つ以上のCREB/ATFタンパク質を発現するようであるが、発現されるメンバーおよびmRNAスプライシングの調節は組織特異的であるようである。活性化ドメインのディファレンシャルなスプライシングが、特定のCREB/ATFタンパク質が転写インヒビターであるかアクチベーターであるかを決定し得る。多くのCREB/ATFタンパク質がウィルス性転写を活性化し得るが、活性ドメインを有さないいくつかのスプライシング変異体は阻害性である。CREB/ATFタンパク質は、cAMP応答エレメント(CRE)を介してホモダイマーまたはヘテロダイマーとしてDNAを結合し得る。CREのコンセンサス形態は、非メチル化配列TGACGTCである(CpGがメチル化されている場合には、結合がなくされる)(Iguchi−Ariga,S.M.M.,およびW.Schaffner,「cAMP応答性エンハンサー/プロモーター配列TGACGTCAのCpGのメチル化が、特定の因子の結合および転写活性化をなくさせる」,Genes & Develop.3:612,1989)。
ここで、CGは、オリゴヌクレオチドに免疫刺激能力を付与する非メチル化CpGジヌクレオチドであり;X1およびX2の少なくとも1つはプリンであり;そして、X3およびX4の少なくとも1つはピリミジンである。
3’からなる群から選択される。
5’ X1X2CGX3X4 3’
ここで、CおよびGは、非メチル化であり;X1、X2、X3およびX4はヌクレオチドであり;そしてGCGトリヌクレオチド配列は、5’および3’末端にもその近傍にも存在しない。
5’ GCGXnGCG 3’
ここで、Xはヌクレオチドであり;nは0〜50の範囲である。好ましい実施態様においては、Xはピリミジンである。
(定義)
本明細書において用いられるように、以下の用語および表現は下記の意味を有する:
「オリゴヌクレオチド」または「オリゴ」は、複数のヌクレオチド(すなわち、ホスフェート基および置換可能な有機塩基(置換ピリミジン(例えば、シトシン(C)、チミン(T)またはウラシル(U))あるいは置換プリン(例えば、アデニン(A)またはグアニン(G))のいずれかである)に結合した糖(例えば、リボースまたはデオキシリボース)を含む分子)を意味する。本明細書において用いられるように、用語「オリゴヌクレオチド」は、オリゴリボヌクレオチド(ORN)およびオリゴデオキシリボヌクレオチド(ODN)の両方を意味する。用語「オリゴヌクレオチド」はまた、オリゴヌクレオシド(すなわち、ホスフェートを含まないオリゴヌクレオチド)および任意の他の有機塩基含有ポリマーを包含する。オリゴヌクレオチドは、既存の核酸源(例えば、ゲノムまたはcDNA)から得られ得るが、好ましくは合成である(例えば、オリゴヌクレオチド合成により産生される)。
5’ X1X2CGX3X4 3’
ここで、CおよびGは、非メチル化であり;X1、X2、X3およびX4はヌクレオチドであり;そしてGCGトリヌクレオチド配列は、5’および3’末端にもその近傍にも存在しない。
好ましくは免疫刺激オリゴヌクレオチドは8〜40塩基対のサイズの範囲である。さらに、免疫刺激オリゴヌクレオチドは、好ましくは安定化されたオリゴヌクレオチドであり、特に好ましくはホスホロチオエートで安定化されたオリゴヌクレオチドである。好ましい1つの実施態様においては、X1X2はジヌクレオチドGpAである。好ましい別の実施態様においては、X3X4は、好ましくはジヌクレオチドTpCまたはTpTである。特に好ましい実施態様においては、コンセンサスモチーフX1X2CGX3X4は5’末端においてTにより先行される。特に好ましいコンセンサス配列は、TGACGTTまたはTGACGTCである。
5’ GCGXnGCG 3’
ここで、Xはヌクレオチドであり;nは0〜50の範囲である。好ましい実施態様においては、Xはピリミジンである。
(ある種の非メチル化CpG含有オリゴは、インビトロおよびインビボで示されるようにB細胞刺激活性を有する)
後述の実施例1および2に記載のプロトコールを用いて内在性レトロウィルス配列に特異的な2つのアンチセンスオリゴヌクレオチドのリンパ球刺激効果を調べると、驚くべきことに、24の「コントロール」(「アンチセンス」ODNのパネルについての種々のスクランブル、センスおよびミスマッチコントロールを含む)のうちの2つもまたB細胞活性化およびIgM分泌を媒介するが、他の「コントロール」は効果を有さないことが見いだされた。
MHCの発現について、ならびに3Hチミジンを用いてそれらの自然増殖について、ODN注射の24時間後にマウス由来の脾臓細胞を調べた。3種の活性化マーカーすべての発現が、CpG ODN注射マウス由来のB細胞において有意に増加したが、PBSまたは非CpG ODN注射マウス由来のB細胞においては増加しなかった。刺激性ODNを注射したマウス由来の脾臓細胞は、PBSまたは非CpG ODN注射マウスと比較して、自然3Hチミジン取り込みが2〜6倍増加した。4日後、インビボでのCpG ODN注射マウスの血清IgMレベルは、コントロールと比較して約3倍増加した。これらの薬剤がT細胞を活性化する能力がないことと一致して、IL−2RまたはCD−44のT細胞発現における変化は最小限であった。
実施例4でさらに詳細に記載するように、CpG含有オリゴヌクレオチドがB細胞に加えてナチュラルキラー(NK)細胞の活性を刺激するかどうかを決定するために実験を行った。表3に示すように、CpG ODN 1および3Ddと共に培養された脾臓細胞においてNK活性の顕著な誘導が観察された。これに対して、非CpGコントロールODNで処理されたエフェクターにおいては、誘導はほとんど存在しなかった。
ODN(CpGモチーフまたは他の部分でのシトシンが5−メチルシトシンで置換されたもの)のB細胞マイトジェン性を、実施例1に記載のようにして調べた。上記表1に示すように、メチル化CpGを含むODNは、非マイトジェン性であった(表1;ODN 1c、2f、3De、および3Mc)。しかし、CpGジヌクレオチド以外のシトシンのメチル化では、刺激特性は維持された(表1;ODN 1d、2d、3Df、および3Md)。
(両末端およびその近傍にGCGトリヌクレオチド配列を含むオリゴの免疫阻害活性)
いくつかの場合においては、上記の刺激モチーフ内部ではないCpGジヌクレオチドを含むODNは、他のマイトジェン性CpG ODNの刺激効果をブロックすることが見いだされた。具体的には、CpG ODNの5’および/または3’末端およびその近傍にGCGからなる非定型のCpGモチーフを加えることにより、他のCpGモチーフによる増殖の刺激が実際に阻害された。GCGモチーフにおけるシトシンのメチル化または置換は、この効果を逆転する。好ましいCpGモチーフに見られるよりもずっと低いが、ODN中のGCGモチーフはそれ自体が低いマイトジェン性効果を有する。
(免疫刺激、中和および免疫阻害オリゴヌクレオチドの作用の提唱されるメカニズム)
その表面Igレセプターを介してB細胞をトリガーする抗原とは異なり、CpG−ODNは、検出可能なCa2+流出、タンパク質チロシンリン酸化における変化またはIP 3生成のいずれも誘導しなかった。CpGモチーフ存在下または非存在下でのFITC−結合ODNを用いるフローサイトメトリーを、Zhao,Qら(Antisense Research and Development 3:53−66(1993))に記載のようにして行った。これにより、等価な膜結合、細胞取り込み、流出および細胞内局在化が示された。このことは、CpG ODNに対して特異的な細胞膜タンパク質は存在しないかもしれないことを示唆している。細胞膜を介して作用するよりもむしろ、これらのデータは、非メチル化CpG含有オリゴヌクレオチドが活性のために細胞取り込みを必要とすることを示唆している:固体Teflon支持体に共有結合したODNは非刺激性であり、アビジンビーズまたはアビジンコートされたペトリ皿上に固定化されたビオチン化ODNも同様であった。FITCまたはビオチンのいずれかと結合されたCpG ODNは、完全なマイトジェン性特性を維持し、このことは立体障害を有さないことを示した。
刺激CpGモチーフは、微生物ゲノムDNAに共通であるが、脊椎動物DNAにおいてはきわめてまれである。さらに、細菌DNAは、B細胞増殖および免疫グロブリン(Ig)産生を誘導することが報告されているが、哺乳動物DNAは誘導しない(Messina,J.P.ら、J.Immunol.147:1759(1991))。さらに実施例3に記載の実験(この実験で、CpGメチラーゼを用いる細菌DNAのメチル化により、マイトジェン性がなくされることが見いだされた)により、CpGの状態の違いが細菌DNAによるB細胞刺激の原因であることが示された。このデータは以下の結論を支持する:細菌DNA内に存在する非メチル化CpGジヌクレオチドが、細菌DNAの刺激効果の原因となる。
目的論的には、CpGモチーフによる白血球活性化によって免疫防御メカニズムが代表され、これにより、宿主DNAと細菌DNAとが区別され得るようである。宿主DNAは、そのCpG抑制およびメチル化に起因してリンパ球活性化をほとんど誘導しないか全く誘導しない。細菌DNAは、感染組織において選択的なリンパ球活性化を引き起こす。CpG経路は抗原レセプターを介するB細胞活性化と共働するので、細菌抗原に特異的な抗原レセプターを有するB細胞は、細胞膜Igを介する1つの活性化シグナルと細菌DNAからの第2のシグナルとを受信し、従って、優先的に活性化される傾向を有する。B細胞活性化におけるこの経路と他の経路との相互関係が、ポリクローナル抗原を用いて抗原特異性応答を誘導する生理学的メカニズムを提供する。
(免疫刺激オリゴの作製方法)
本発明において使用するために、オリゴヌクレオチドが、当該分野で周知の多くの方法のうちの任意の方法を用いて新たに合成され得る。例えば、β−シアノエチルホスホルアミダイト法(S.L.BeaucageおよびM.H.Caruthers,(1981)Tet.Let.22:1859);ヌクレオシド
H−ホスホネート法(Gareggら,(1986)Tet.Let.27:4051−4054;Froehlerら,(1986)Nucl.Acid.Res.14:5399−5407;Gareggら,(1986)Tet.Let.27:4055−4058;Gaffneyら,(1988)Tet.Let.29:2619−2622)。これらの化学反応は、種々の市販の自動化オリゴヌクレオチド合成機により行われ得る。あるいは、オリゴヌクレオチドは、公知の技術(例えば、制限酵素、エクソヌクレアーゼまたはエンドヌクレアーゼを使用する技術)を用いて、既存の核酸配列(例えば、ゲノムまたはcDNA)から調製され得る。
(免疫刺激オリゴの治療的使用)
その免疫刺激特性に基づいて、少なくとも1つの非メチル化CpGジヌクレオチドを含むオリゴヌクレオチドは、インビボで被験体に投与され、「免疫系不全」を処置し得る。あるいは、少なくとも1つの非メチル化CpGジヌクレオチドを含むオリゴヌクレオチドは、免疫系不全を有する被験体から得られるリンパ球(例えば、B細胞またはNK細胞)とエクスビボで接触され得、次いで、活性化リンパ球が被験体に再度移植され得る。
(中性オリゴヌクレオチドの治療的使用)
特定の標的配列に相補的なオリゴヌクレオチドが合成され得、そしてインビボで非検体に投与され得る。例えば、アンチセンスオリゴヌクレオチドは相補的なmRNAにハイブリダイズし、これにより特異的な標的遺伝子の発現を防止する。アンチセンスオリゴヌクレオチドの配列特異的な効果により、それらはタンパク質機能の研究に有用な調査手段となった。全身アンチセンス療法の第I/II相のヒトへの試験が、急性骨髄性白血病およびHIVについて現在行われている。
上記で報告された研究によれば、非メチル化CpG含有オリゴヌクレオチドは、リンパ球(例えば、B細胞およびNK細胞)について直接的にマイトジェン性であることが示される。細菌DNAにおけるこれらの配列の存在とあわせて、これらの結果は、動物ゲノム中のCpGジヌクレオチドが脱表現されないこと(underrepresentation)、および、このようなジヌクレオチド中に存在するシトシンの広範囲のメチル化が、宿主DNAと細菌DNAとを区別し得る免疫防御メカニズムの存在により説明され得ることを示唆する。宿主DNAは、通常、多くの解剖学的領域およびアポトーシス(細胞死)による炎症領域に存在するが、一般に、リンパ球活性化をほとんど誘導しないか全く誘導しない。しかし、非メチル化CpGモチーフを含む細菌DNAの存在は、それが有益である感染した解剖学的領域において、正確にリンパ球活性化を引き起こし得る。この新規な活性化経路は、T細胞依存抗原特異的B細胞活性化の迅速な代替物を提供する。しかし、B細胞活性化は、全体的には非特異的ではないようである。細菌産物に特異的な抗原レセプターを有するB細胞は、細胞膜Igを介する1つの活性化シグナルおよび細菌DNAからの第2のシグナルとを受信し得、これにより、抗原特異的免疫応答をさらに激しくトリガーし得る。
(両端またはその近傍にGCGトリヌクレオチド配列を含むオリゴの治療的使用)
オリゴヌクレオチドと標的化されるウィルス配列との間の相補性に起因する任意のアンチセンス効果に関係なく、CREB/ATFとのその相互作用に基づいて、両端またはその近傍にGCGトリヌクレオチド配列を含むオリゴヌクレオチドは、抗ウィルス活性を有する。この活性に基づいて、阻害オリゴヌクレオチドの有効量が、被験体に投与されてウィルス感染を処置または防止し得る。
抗−Thy−1.2および補体を用いてT細胞を放血し、lympholyte M(Cedarlane Laboratories,Hornby,Ontario,Canada)で遠心分離した、6〜12週齢で特定の病原体を有さないDBA/2またはBXSBマウス(アイオワ大学動物管理施設で飼育された;実質的な系統の違いは示されなかった)から得られた脾臓からB細胞を精製した(「B細胞」)。B細胞は、1%未満のCD4+またはCD8+細胞を含んでいた。10%FBS(65℃で30分間熱失活させた)、50μMの2−メルカプトエタノール、100U/mlのペニシリン、100μg/mlのストレプトマイシン、および2mMのL−グルタメートを含む100μl RPMI中の8×104のB細胞を、96ウェルのマイクロタイタープレートに3連で分配した。20μMのODNを、37℃で20時間の培養開始時に加え、1μCiの3Hウリジンで細胞をパルスし、そして4時間後に細胞を回収し、そしてカウントした。20μMのODNとともに脾臓細胞全体を48時間培養した後、ELISAスポットアッセイを用いてIg分泌B細胞を数えた。データ(表1に報告する)は、ODNなしで培養した細胞と比較した刺激指数を表す。本実験においては、ODNなしで培養した細胞は687cpmを与えたが、一方、20μg/mlのLPS(最適濃度であることを滴定により決定した)と共に培養した細胞は99,699cpmを与えた。3Hチミジン取り込みアッセイは、同様の結果を示したが、分解したODNから放出されたチミジンによる非特異的阻害をいくらか示した(Matson,SおよびA.M.Krieg(1992),「コントロールオリゴヌクレオチドによる3H−チミジン取り込みの非特異的抑制」,Antisense Research and Development 2:325)。
(実施例2:B細胞由来のIgM産生に対するODNの効果)
新たに殺したマウスの脾臓由来の単一細胞懸濁液を、Leibsonらの方法(J.Exp.Med.154:1681(1981))により抗−Thyl、抗−CD4、および抗−CD8ならびに補体で処理した。休止B細胞(<,02%のT細胞混入)を、DeFrancoらの手順(J.Exp.Med.155:1523(1982))により非連続Percoll勾配の63〜70%バンドから単離した。上記のようにして、これらを30μM ODNまたは20μg/ml LPS中で48時間培養した。ELIスポットアッセイ(Klinman,D.M.ら,J.Immunol.144:506(1990))により決定したところ、活発にIgMを分泌するB細胞の数はこの時点で最大であった。このアッセイにおいては、B細胞を抗Igでコートされたマイクロタイタープレート上で6時間インキュベートした。それらが産生したIg(>99% IgM)を、ホスファターゼ標識抗Ig(Southern Biotechnology Associated,Birmingham,AL)を用いて検出した。個々のB細胞により産生された抗体を、ホスファターゼの存在下で不溶性青色沈殿を形成するBCIP(Sigma Chemical Co.,St.Louis,MO)を加えることにより視覚化した。20〜40のスポット/ウェルを生じる細胞の希釈を用いて、抗体分泌B細胞/試料の総数を決定した。すべてのアッセイを3連で行った。いくつかの実験において、培地の上清をELISAによりIgMについてアッセイしたところ、CpG−ODNに対する応答の同様な増加を示した。
(実施例3:細菌DNAによるB細胞刺激)
DBA/2 B細胞を、DNAなしで、あるいは、50μg/mlの(a)Micrococcus lysodeikticus;(b)NZB/Nマウス脾臓;およびNFS/Nマウス脾臓ゲノムDNAと共に48時間培養し、次いで、3Hチミジンで4時間パルスし、そして、その後細胞を回収した。2連のDNA試料を、37℃で30分間DNAseIで消化し、次いで、細胞培養物に加えた。ELISAスポットアッセイを用いると、E coli DNAもまた、48時間までIgM分泌B細胞の数の8.8倍の増加を誘導した。
(実施例4:ナチュラルキラー(NK)活性に対するODNの効果)
10×106のC57BL/6脾臓細胞を、2mlのRPMI(実施例1に記載のように補充した)中で、40μMのCpGまたは非CpG ODNの存在下または非存在下で48時間培養した。細胞を洗浄し、次いで、2つのNK感受性標的細胞株(YAC−1および2C11)を用いる短期51Cr放出アッセイにおけるエフェクター細胞として用いた(Ballas,Z.K.ら(1993)J.Immunol.150:17)。0.2ml中V底マイクロタイタープレート中の104の51Cr標識標的細胞に、種々の濃度でエフェクター細胞を加え、そして5%CO2中、37℃で4時間インキュベートした。次いで、プレートを遠心分離し、上清のアリコートを放射能についてカウントした。エフェクター細胞の存在下で放出された51Crから標的細胞単独で培養された場合に放出された51Cr放出を引いた値の、2%酢酸中での細胞溶解後に放出された総カウントから細胞単独で培養された場合に放出された51Cr cpmを引いた値に対する比率を計算することにより、特異的溶解パーセントを決定した。
(実施例5:CpGホスホロチオエートODNについてのインビボでの研究)
マウスを計量し、0.25mlの滅菌PBSまたはPBSに溶解した示されたホスホロチオエートODNをIPで注射した。24時間後、脾臓細胞を回収し、洗浄し、そして、B細胞のゲートのためのファイコエリトリン結合6B2を、ビオチン結合抗Ly−6A/Eまたは抗Iad(Pharmingen,San Diego,CA)または抗Bla−1(Hardy,R.R.ら,J.Exp.Med.159:1169(1984))と組み合わせて用いて、フローサイトメトリーのために染色した。それぞれの条件について2匹のマウスを調べ、個々に分析した。
(実施例6:B細胞刺激についてのホスホロチオエートODNの滴定)
コントロールODN 1a、またはCpG ODN 1dおよび3Ddの配列を有するホスホロチオエートODNと共にB細胞を培養し、次いで、20時間後に3Hウリジン、または44時間後に3Hチミジンのいずれかでパルスし、次いで、細胞を回収し、そしてcpmを決定した。
(実施例7:アポトーシスからのB細胞のレスキュー)
WEHI−231細胞(5×104/ウェル)を、LPSあるいはコントロールODN 1aまたはCpG ODN 1dおよび3Ddの存在下または非存在下、37℃で1時間培養し、次いで、抗IgM(1μ/ml)を加えた。細胞をさらに20時間培養し、次いで2μCi/ウェルの3Hチミジンで4時間パルスした。この実験において、ODNも抗IgMも加えない細胞は、抗IgMの添加により90.4×103を与えた。表1に示すホスホジエステルODNは、ODN分解に起因する非特異的抑制をいくらか示すものの、同様の保護を与えた。各実験を少なくとも3回繰り返し、同様の結果を得た。
(実施例8: IL−6のインビボでの誘導)
DBA/2雌性マウス(2ヶ月齢)に、500μgのCpGまたはコントロールホスホロチオエートODNをIPで注射した。注射後、種々の時点で、マウスを採血した。2匹のマウスを各時点について調べた。IL−6をElisaにより測定し、そしてIL−6濃度を組換えIL−6を用いて得られる標準曲線と比較することにより計算した。アッセイの感度は、10pg/mlであった。レベルは8時間後に検出不能であった。
(実施例9:B細胞CREB/ATFの放射性標識2本鎖CREプローブ(CREB)への結合)
CREプローブ(遊離プローブは、像の底部から離れている)を用いるEMSAにより分析すると、CH12.LX B細胞由来の全細胞抽出物は、2つの遅延バンドを示した。CREへのCREB/ATFタンパク質の結合は、示された量のコールドCREおよび1本鎖CpG ODNにより競合されたが、非CpG
ODNによっては競合されなかった。
(等価物)
当業者は、日常的な実験程度を用いて、本明細書に記載の本発明の特定の実施態様の多くの等価物を認識し、または確認し得る。このような等価物は、添付の特許請求の範囲に包含されることが意図される。
(配列表)
(1)一般情報:
(i)出願人: アーサー エム.クリーグ,エム.ディー.
(ii)発明の名称: 免疫調節オリゴヌクレオチド
(iii)配列数: 27
(iv)連絡住所:
(A)名称: ラヒブ アンド コックフィールド
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(C)OS:PC−DOS/MS−DOS
(D)ソフトウェア: ASCIItext
(vi)現在の出願データ:
(A)出願番号: US
(B)出願日:
(C)分類:
(viii)代理人/事務所情報:
(A)氏名: アーノルド,ベス イー.
(B)登録番号: 35,430
(C)照会/記録番号:UIZ−013CP
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(A)電話:(617)227−7400
(B)テレファックス:(617)227−5941
(2)配列番号1の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号1:
GGGGTCAACGTTCAGGGGGG 20
(2)配列番号2の情報:
(i)配列の特色:
(A)長さ: 15 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号2:
GCTAGACGTTAGCGT 15
(2)配列番号3の情報:
(i)配列の特色:
(A)長さ: 15 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号3:
GCTAGATGTTAGCGT 15
(2)配列番号4の情報:
(i)配列の特色:
(A)長さ: 15 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(ix)配列の特徴:
(A)特徴を表す記号: misc_feature
(B)存在位置: 7
(D)他の情報: 「Nは5メチルシトシンを表す」
(xi)配列: 配列番号4:
GCTAGANGTTAGCGT 15
(2)配列番号5の情報:
(i)配列の特色:
(A)長さ: 15 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(ix)配列の特徴:
(A)特徴を表す記号: misc_feature
(B)存在位置: 13
(D)他の情報: 「Nは5 メチルシトシンを表す」
(xi)配列: 配列番号5:
GCTAGACGTT AGNGT 15
(2)配列番号6の情報:
(i)配列の特色:
(A)長さ: 15 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号6:
GCATGACGTTGAGCT 15
(2)配列番号7の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号7:
ATGGAAGGTCCAGCGTTCTC 20
(2)配列番号8の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号8:
ATCGACTCTCGAGCGTTCTC 20
(2)配列番号9の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(ix)配列の特徴:
(A)特徴を表す記号: misc_feature
(B)存在位置: 3
(D)他の情報: 「Nは5 メチルシトシンを表す」
(ix)配列の特徴:
(A)特徴を表す記号: misc_feature
(B)存在位置: 10
(D)他の情報: 「Nは5 メチルシトシンを表す」
(ix)配列の特徴:
(A)特徴を表す記号: misc_feature
(B)存在位置: 14
(D)他の情報: 「Nは5 メチルシトシンを表す」
(xi)配列: 配列番号9:
ATNGACTCTNGAGNGTTCTC 20
(2)配列番号10の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(ix)配列の特徴:
(A)特徴を表す記号: misc_feature
(B)存在位置: 3
(D)他の情報: 「Nは5 メチルシトシンを表す」
(xi)配列: 配列番号10:
ATNGACTCTC GAGCGTTCTC 20
(2)配列番号11の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(ix)配列の特徴:
(A)特徴を表す記号: misc_feature
(B)存在位置: 18
(D)他の情報: 「Nは5 メチルシトシンを表す」
(xi)配列: 配列番号11:
ATCGACTCTCGAGCGTTNTC 20
(2)配列番号12の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号12:
ATGGAAGGTCCAACGTTCTC 20
(2)配列番号13の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号13:
GAGAACGCTGGACCTTCCAT 20
(2)配列番号14の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号14:
GAGAACGCTCGACCTTCCAT 20
(2)配列番号15の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号15:
GAGAACGCTCGACCTTCGAT 20
(2)配列番号16の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号16:
GAGCAAGCTGGACCTTCCAT 20
(2)配列番号17の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(ix)配列の特徴:
(A)特徴を表す記号: misc_feature
(B)存在位置: 6
(D)他の情報: 「Nは5 メチルシトシンを表す」
(xi)配列: 配列番号17:
GAGAANGCTG GACCTTCCAT 20
(2)配列番号18の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(ix)配列の特徴:
(A)特徴を表す記号: misc_feature
(B)存在位置: 14
(D)他の情報: 「Nは5 メチルシトシンを表す」
(xi)配列: 配列番号18:
GAGAACGCTGGACNTTCCAT 20
(2)配列番号19の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号19:
GAGAACGATGGACCTTCCAT 20
(2)配列番号20の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号20:
GAGAACGCTCCAGCACTGAT 20
(2)配列番号21の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号21:
TCCATGTCGGTCCTGATGCT 20
(2)配列番号22の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号22:
TCCATGCTGGTCCTGATGCT 20
(2)配列番号23の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(ix)配列の特徴:
(A)特徴を表す記号: misc_feature
(B)存在位置: 8
(D)他の情報: 「Nは5 メチルシトシンを表す」
(xi)配列: 配列番号23:
TCCATGTNGGTCCTGATGCT 20
(2)配列番号24の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(ix)配列の特徴:
(A)特徴を表す記号: misc_feature
(B)存在位置: 12
(D)他の情報: 「Nは5 メチルシトシンを表す」
(xi)配列: 配列番号24:
TCCATGTCGGTNCTGATGCT 20
(2)配列番号25の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号25:
TCCATGACGTTCCTGATGCT 20
(2)配列番号26の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号26:
TCCATGTCGGTCCTGCTGAT 20
(2)配列番号27の情報:
(i)配列の特色:
(A)長さ: 20 塩基対
(B)型: 核酸
(C)鎖の数: 一本鎖
(D)トポロジー: 直鎖状
(ii)配列の種類: DNA
(xi)配列: 配列番号27:
GGGGTCAAGTCTGAGGGGGG 20
Claims (1)
- 免疫刺激オリゴヌクレオチド。
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US27635894A | 1994-07-15 | 1994-07-15 |
Related Parent Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2002302338A Division JP2003144184A (ja) | 1994-07-15 | 2002-10-16 | 免疫調節オリゴヌクレオチド |
Related Child Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2009057160A Division JP2009148296A (ja) | 1994-07-15 | 2009-03-10 | 免疫調節オリゴヌクレオチド |
Publications (1)
Publication Number | Publication Date |
---|---|
JP2004215670A true JP2004215670A (ja) | 2004-08-05 |
Family
ID=23056334
Family Applications (7)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP50499196A Expired - Lifetime JP3468773B2 (ja) | 1994-07-15 | 1995-02-07 | 免疫調節オリゴヌクレオチド |
JP2002302338A Withdrawn JP2003144184A (ja) | 1994-07-15 | 2002-10-16 | 免疫調節オリゴヌクレオチド |
JP2003178741A Expired - Lifetime JP4126252B2 (ja) | 1994-07-15 | 2003-06-23 | 免疫調節オリゴヌクレオチド |
JP2003178740A Withdrawn JP2004024261A (ja) | 1994-07-15 | 2003-06-23 | 免疫調節オリゴヌクレオチド |
JP2004069838A Withdrawn JP2004215670A (ja) | 1994-07-15 | 2004-03-11 | 免疫調節オリゴヌクレオチド |
JP2008015654A Withdrawn JP2008169216A (ja) | 1994-07-15 | 2008-01-25 | 免疫調節オリゴヌクレオチド |
JP2009057160A Withdrawn JP2009148296A (ja) | 1994-07-15 | 2009-03-10 | 免疫調節オリゴヌクレオチド |
Family Applications Before (4)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP50499196A Expired - Lifetime JP3468773B2 (ja) | 1994-07-15 | 1995-02-07 | 免疫調節オリゴヌクレオチド |
JP2002302338A Withdrawn JP2003144184A (ja) | 1994-07-15 | 2002-10-16 | 免疫調節オリゴヌクレオチド |
JP2003178741A Expired - Lifetime JP4126252B2 (ja) | 1994-07-15 | 2003-06-23 | 免疫調節オリゴヌクレオチド |
JP2003178740A Withdrawn JP2004024261A (ja) | 1994-07-15 | 2003-06-23 | 免疫調節オリゴヌクレオチド |
Family Applications After (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2008015654A Withdrawn JP2008169216A (ja) | 1994-07-15 | 2008-01-25 | 免疫調節オリゴヌクレオチド |
JP2009057160A Withdrawn JP2009148296A (ja) | 1994-07-15 | 2009-03-10 | 免疫調節オリゴヌクレオチド |
Country Status (12)
Country | Link |
---|---|
US (1) | US6194388B1 (ja) |
EP (4) | EP0772619B2 (ja) |
JP (7) | JP3468773B2 (ja) |
AT (3) | ATE509102T1 (ja) |
AU (1) | AU713040B2 (ja) |
CA (2) | CA2194761C (ja) |
DE (2) | DE69535036T3 (ja) |
DK (1) | DK0772619T4 (ja) |
ES (3) | ES2366201T3 (ja) |
HK (3) | HK1043598A1 (ja) |
PT (1) | PT772619E (ja) |
WO (1) | WO1996002555A1 (ja) |
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US6426334B1 (en) | 1997-04-30 | 2002-07-30 | Hybridon, Inc. | Oligonucleotide mediated specific cytokine induction and reduction of tumor growth in a mammal |
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1995
- 1995-02-07 EP EP95911630A patent/EP0772619B2/en not_active Expired - Lifetime
- 1995-02-07 EP EP01202811A patent/EP1167377B2/en not_active Expired - Lifetime
- 1995-02-07 US US08/386,063 patent/US6194388B1/en not_active Expired - Lifetime
- 1995-02-07 AT AT01202813T patent/ATE509102T1/de not_active IP Right Cessation
- 1995-02-07 DE DE69535036T patent/DE69535036T3/de not_active Expired - Lifetime
- 1995-02-07 DE DE69535905T patent/DE69535905D1/de not_active Expired - Lifetime
- 1995-02-07 AT AT01202811T patent/ATE420171T1/de not_active IP Right Cessation
- 1995-02-07 ES ES01202813T patent/ES2366201T3/es not_active Expired - Lifetime
- 1995-02-07 PT PT95911630T patent/PT772619E/pt unknown
- 1995-02-07 WO PCT/US1995/001570 patent/WO1996002555A1/en active IP Right Grant
- 1995-02-07 DK DK95911630.2T patent/DK0772619T4/da active
- 1995-02-07 AT AT95911630T patent/ATE328890T1/de active
- 1995-02-07 EP EP01202813A patent/EP1167378B1/en not_active Expired - Lifetime
- 1995-02-07 CA CA002194761A patent/CA2194761C/en not_active Expired - Lifetime
- 1995-02-07 EP EP01202814A patent/EP1167379A3/en not_active Ceased
- 1995-02-07 CA CA002560114A patent/CA2560114A1/en not_active Abandoned
- 1995-02-07 AU AU19127/95A patent/AU713040B2/en not_active Expired
- 1995-02-07 ES ES95911630T patent/ES2267100T5/es not_active Expired - Lifetime
- 1995-02-07 ES ES01202811T patent/ES2320315T5/es not_active Expired - Lifetime
- 1995-02-07 JP JP50499196A patent/JP3468773B2/ja not_active Expired - Lifetime
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2002
- 2002-05-13 HK HK02103584.4A patent/HK1043598A1/zh unknown
- 2002-06-26 HK HK02104746.7A patent/HK1044949B/zh not_active IP Right Cessation
- 2002-06-26 HK HK02104747.6A patent/HK1044950A1/zh not_active IP Right Cessation
- 2002-10-16 JP JP2002302338A patent/JP2003144184A/ja not_active Withdrawn
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2003
- 2003-06-23 JP JP2003178741A patent/JP4126252B2/ja not_active Expired - Lifetime
- 2003-06-23 JP JP2003178740A patent/JP2004024261A/ja not_active Withdrawn
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2004
- 2004-03-11 JP JP2004069838A patent/JP2004215670A/ja not_active Withdrawn
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2008
- 2008-01-25 JP JP2008015654A patent/JP2008169216A/ja not_active Withdrawn
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2009
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