JP2011142915A - 抗原性髄膜炎菌性ペプチド - Google Patents
抗原性髄膜炎菌性ペプチド Download PDFInfo
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Abstract
【解決手段】WO99/36544は、Neisseria meningitidis由来の多数のタンパク質を開示する。本発明は、少なくとも1つの抗原決定基を含む、これらのタンパク質のフラグメントに関する。これらのフラグメントを含む相同配列およびタンパク質もまた開示される。本発明のタンパク質は、種々の手段(例えば、組換え発現、細胞培養物からの精製、化学合成など)によって、そして種々の形態(例えば、ネイティブ型、C末端および/またはN末端融合型など)で調製され得る。
【選択図】なし
Description
本発明は、細菌Neisseria meningitidis由来の抗原性ペプチド配列に関する。
Neisseria meningitidisは、ヒトにおいて病原性である非運動性のグラム陰性双球菌である。
本発明は、国際特許出願WO99/36544で開示されたタンパク質のフラグメントを提供する。この出願において、これらのフラグメントは、少なくとも1つの抗原決定基を含む。
本発明は、例えば、以下の項目を提供する。
(項目1)WO99/36544に開示されたタンパク質のフラグメントであって、該フラグメントは少なくとも1つの抗原決定基を含む、フラグメント。
(項目2)100アミノ酸以下の長さを有する、項目1に記載のフラグメント。
(項目3)3アミノ酸以上の長さを有する、項目1または項目2に記載のフラグメント。
(項目4)表Iの1769のフラグメントのうちの1つである、項目1〜3のいずれか1項に記載のフラグメント。
(項目5)項目1〜4のいずれか1項に記載のフラグメントに対して50%以上の配列同一性を有する、ポリペプチド。
(項目6)項目1、項目2、または項目3に記載の1つ以上のフラグメントを含むタンパク質であって、ただし該タンパク質は、WO99/36544に開示された45の完全タンパク質配列のうちの1つではない、タンパク質。
(項目7)項目1〜4のいずれか1項に記載のフラグメントを認識する、抗体。
(項目8)ペプチド配列を含むタンパク質であって、該ペプチド配列は、項目7に記載の抗体により認識される、タンパク質。
(項目9)項目1、項目2もしくは項目3に記載のフラグメント、項目5に記載のポリペプチド、または項目8に記載のタンパク質をコードする、核酸。
(項目10)項目1、項目2もしくは項目3に記載のフラグメント、項目5に記載のポリペプチド、項目8に記載のタンパク質、項目7に記載の抗体、および/または項目9に記載の核酸を含む組成物であって、該組成物は、ワクチン、診断試薬、または免疫原性組成物である、組成物。
(項目11)医薬としての使用のための、項目10に記載の組成物。
(項目12)項目1、項目2もしくは項目3に記載のフラグメント、項目5に記載のポリペプチド、項目8に記載のタンパク質、項目7に記載の抗体、および/または項目9に記載の核酸の使用であって、該使用は、(i)ナイセリア細菌による感染を処置もしくは予防するための医薬、(ii)ナイセリア細菌の存在、もしくはナイセリア細菌に対して惹起された抗体の存在を検出するための診断試薬、および/または(iii)ナイセリア細菌に対する抗体を惹起し得る試薬、の製造における、使用。
(項目13)治療有効量の項目10に記載の組成物を患者に投与する工程を包含する、患者を処置する方法。
本発明の実施は、他に示されなければ、分子生物学、微生物学、組換えDNA、および免疫学の従来の技術を使用し、これらは当該分野の技術の範囲内である。このような技術は以下の文献で十分説明されている(例えば、Sambrook Molecular Cloning;A Laboratory Manual 第2版(1989);DNA Cloning,第I巻およびii巻(D.N Glover編 1985);Oligonucleotide Synthesis(M.J.Gait編 1984);Nucleic Acid Hybridization(B.D.HamesおよびS.J.Higgins編 1984);Transcription and Translation(B.D.HamesおよびS.J.Higgins編 1984);Animal Cell Culture(R.I.Freshney編 1986);Immobilized Cells and Enzymes(IRL Press,1986);B.Perbal,A Practical Guide to Molecular Cloning(1984);the Methods in Enzymology series(Academic Press,Inc.),特に154および155巻;Gene Transfer Vectors for Mammalian Cells(J.H.MillerおよびM.P.Calos編1987,Cold Spring Harbor Laboratory);MayerおよびWalker,編(1987),Immunochemical Methods in Cell and Molecular Biology(Academic Press,London);Scopes,(1987)Protein Purification:Principles and Practice,第2版(Springer−Verlag,N.Y.)、およびHandbook of Experimental Immunology,I−IV巻(D.M.WeirおよびC.C.Blackwell編 1986)。
Xを含む組成物は、組成物中の全X+Yの少なくとも85重量%がXであるとき、Yを「実質的に含まない」。好ましくは、Xは、組成物中の全X+Yの少なくとも約90重量%を、さらに好ましくは少なくとも約95重量%または99重量%さえを含む。
髄膜炎菌のヌクレオチド配列は、種々の異なる発現系;例えば、哺乳動物細胞、バキュロウイルス、植物、細菌、および酵母と共に使用される発現系において発現され得る。
哺乳動物発現系は、当該分野において公知である。哺乳動物プロモーターは、哺乳動物RNAポリメラーゼを結合し、コード配列(例えば、構造遺伝子)のmRNAへの下流(3’)転写を開始し得る任意のDNA配列である。プロモーターは、転写開始領域(これはコード配列の5’末端の近位に通常位置する)およびTATAボックス(転写開始部位の25〜30塩基対(bp)上流に通常位置する)を有する。TATAボックスは、その正しい部位においてRNAポリメラーゼIIにRNA合成を開始させるよう指示すると考えられている。哺乳動物プロモーターはまた、TATAボックスの100〜200bp上流以内に通常位置する上流プロモーターエレメントを含む。上流プロモーターエレメントは、転写が開始され、そしていずれかの方向において作用し得る速度を決定する(Sambrookら(1989)「Expression of Cloned Genes in Mammalian Cells」 Molecular Cloning:A Laboratory Manual、第2版)。
タンパク質をコードしているポリヌクレオチドはまた、適切な昆虫の発現ベクター内に挿入され得、そしてそのベクター内で、制御エレメントに作動可能に連結される。ベクターの構築には、当該分野で公知の技術を使用する。一般に、その発現系の構成要素として、以下のものが挙げられる:バキュロウイルスゲノムのフラグメント、および発現される異種遺伝子の挿入用の好都合な制限部位の両方を有する転移ベクター(transfer vector)(通常は細菌プラスミド);転移ベクター内のバキュロウイルスに特異的なフラグメントに相同性のある配列を有する野生型バキュロウイルス(これは、バキュロウイルスゲノム内への異種遺伝子の相同組換えを可能にする);ならびに適切な昆虫宿主細胞および増殖培地。
へドリンプロモーターの下流に位置される。
当該分野で公知の多くの植物細胞培養および植物全体での遺伝子発現系が存在する。例示的な植物細胞遺伝子発現系としては、米国特許第5,693,506号;米国特許第5,659,122号;および米国特許第5,608,143号のような特許に記載されるものが挙げられる。植物細胞培養における遺伝子発現のさらなる例は、Zenk,Phytochemistry 30:3861−3863(1991)に記載された。植物タンパク質のシグナルペプチドの記載は、上記の参考文献に加え、以下に示すものの中においても見出され得る;Vaulcombeら,Mol.Gen.Genet.209:33−40(1987);Chandlerら,Plant Molecular Biology 3:407−418(1984);Rogers,J.Biol.Chem.260:3731−3738(1985);Rothsteinら,Gene 55:353−356(1987);Whittierら,Nucleic Acids Research 15:2515−2535(1987);Wirselら,Molecular Microbiology 3:3−14(1989);Yuら,Gene 122:247−253(1992)。植物ホルモン(ジベレリン酸およびジベレリン酸により誘導される分泌酵素)による植物遺伝子発現の調節の記載は、R.L.JonesおよびJ.MacMillin,Gibberellins:Advanced Plant Physiology,Malcolm B.Wilkins編 1984 Pitman Publishing Limited,London,21−52頁の中に見出され得る。他の代謝調節性遺伝子が記載される参考文献は、以下である:Sheen,Plant Cell,2:1027−1038(1990);Maasら,EMBO J.9:3447−3452(1990);BenkelおよびHickey、Proc.Natl.Acad.Sci.84:1337−1339(1987)。
細菌の発現技術は、当該分野で公知である。細菌のプロモーターは、細菌のRNAポリメラーゼに結合し得、そしてmRNAへのコード配列(例えば、構造遺伝子)の下流方向(3’方向)の転写を開始し得る任意のDNA配列である。プロモーターは、通常、コード配列の5’末端に近接して配置される転写開始領域を有する。この転写開始領域は、通常、RNAポリメラーゼ結合部位および転写開始部位を含む。細菌のプロモーターはまた、オペレーターと呼ばれる第二のドメインを有し得、このドメインは、RNA合成が始まる近接したRNAポリメラーゼ結合部位と重複し得る。オペレーターは、遺伝子リプレッサータンパク質が、オペレーターに結合し、それによって特定の遺伝子の転写を阻害し得るような、負の調節された(誘導性の)転写を可能にする。構成的発現は、オペレーターのような負の調節エレメントの非存在下で起こり得る。さらに、正の調節は、遺伝子アクチベータータンパク質結合配列により達成され得、その配列が存在する場合は通常、RNAポリメラーゼ結合配列に(5’側で)近接している。遺伝子アクチベータータンパク質の例は、カタボライトアクチベータータンパク質(CAP)であり、それはEscherichia coli(E.coli)におけるlacオペロンの転写の開始を助ける[Raibaudら(1984)Annu.Rev.Genet.18:173]。調節される発現は、それゆえ正または負のいずれかであり、従って転写を増強し得るかまたは低下させ得る。
酵母発現系もまた、当業者に公知である。酵母プロモーターは、酵母RNAポリメラーゼに結合可能であり、そしてコード配列(例えば、構造遺伝子)からmRNAへの下流の(3’側の)転写を開始し得る、任意のDNA配列である。プロモーターは、通常、コード配列の5’末端の近接して位置する転写開始領域を有する。この転写開始領域は、通常、RNAポリメラーゼ結合部位(「TATAボックス」)および転写開始部位を含む。酵母プロモーターはまた、上流アクチベーター配列(UAS)と呼ばれる第2のドメインを有し得、これは、もし存在するならば、通常、構造遺伝子に対して遠位である。このUASは、調節される(誘導できる)発現を可能にする。構成的発現は、UASの非存在下で生じる。調節される発現は、正または負のいずれかであり得、それによって転写を増加させるかまたは減少させるかのいずれかであり得る。
あるいは、上記の成分のうちのいくつかは、組み立てられて形質転換ベクターになり得る。形質転換ベクターは、通常、上記のように、レプリコンのままで保持されるか、または組み込みベクターに開発されるかのいずれかである、選択マーカーを含む。
本明細書中で使用される場合、用語「抗体」とは、少なくとも1つの抗体結合部位から構成されるポリペプチドまたはポリペプチド群をいう。「抗体結合部位」は、内部表面形状および抗原のエピトープの特徴に相補的な電荷分布を有する、3次元結合空間であり、これが、抗体と抗原の結合を可能にする。「抗体」は、例えば、脊椎動物抗体、ハイブリッド抗体、キメラ抗体、ヒト化抗体、改変された抗体、単価抗体、Fabタンパク質、および単一ドメイン抗体を含む。
薬学的組成物は、本発明のポリペプチド、抗体または核酸のいずれかを含み得る。この薬学的組成物は、治療上有効な量の、本願発明のポリペプチド、抗体、またはポリヌクレオチドのいずれかを含む。
一旦処方されると、本発明の組成物は、その被験体へ直接投与され得る。処置される被験体は、動物であり得;特に、ヒト被験体が処置され得る。
本発明に従うワクチンは、予防的(すなわち、感染を予防するため)または治療(すなわち、感染後の疾患を処置するため)のいずれかであり得る。
本発明の治療剤のコード配列を含む、哺乳動物における発現のためにその哺乳動物へ送達される構築物の送達のための遺伝子治療ビヒクルは、局所または全身的のいずれかで投与され得る。これらの構築物は、ウイルスベクターアプローチまたは非ウイルスベクターアプローチを、インビボまたはエキソビボの様式で利用し得る。このようなコード配列の発現は、内因性哺乳動物プロモーターまたは外因性プロモーターを用いて誘導され得る。このコード配列のインビボでの発現は、構成性または調節性のいずれかであり得る。
一旦処方されると、本発明のポリヌクレオチド組成物は、(1)被験体に直接);(2)エキソビボで被験体由来の細胞に送達されて;または(3)組換えタンパク質の発現のためにインビトロで、投与され得る。処置される被験体は、哺乳動物または鳥類であり得る。ヒト被験体もまた処置され得る。
上記の薬学的に受容可能なキャリアおよび塩に加えて、以下のさらなる薬剤がポリヌクレオチド組成物および/またはポリペプチド組成物とともに使用され得る。
1つの例は、限定することなく以下を包含するポリペプチドである:アシアロオロソムコイド(ASOR);トランスフェリン;アシアロ糖タンパク質;抗体;抗体フラグメント;フェリチン;インターロイキン;インターフェロン;顆粒球、マクロファージコロニー刺激因子(GM−CSF)、顆粒球コロニー刺激因子(G−CSF)、マクロファージコロニー刺激因子(M−CSF)、幹細胞因子およびエリスロポエチン。ウイルス抗原(例えば、エンベロープタンパク質)もまた、使用され得る。また、他の侵襲性生物由来のタンパク質(例えば、RIIとして知られるPlasmodium falciparumの環境スポロゾイト(circumsporozoite)タンパク質由来の17アミノ酸ペプチド)。
包含され得る他の群は、例えば、ホルモン、ステロイド、アンドロゲン、エストロゲン、甲状腺ホルモン、またはビタミン、葉酸である。
また、ポリアルキレングリコールが、所望のポリヌクレオチド/ポリペプチドとともに含有され得る。好ましい実施形態において、ポリアルキレングリコールは、ポリエチレングリコールである。さらに、モノサッカリド、ジサッカリド、またはポリサッカリドが含有され得る。この局面の好ましい実施形態において、このポリサッカリドは、デキストランまたはDEAEデキストランである。また、キトサンおよびポリ(乳酸−コ−グリコリド)。
所望のポリヌクレオチド/ポリペプチドはまた、被験体またはそれに由来する細胞への送達の前に、脂質中にカプセル化され得るか、またはリポソーム中にパッケージングされ得る。
さらに、リポタンパク質が、送達されるポリヌクレオチド/ポリペプチドとともに含まれ得る。利用されるリポタンパク質の例は、キロミクロン、HDL、IDL、LDL、およびVLDLを含む。これらのタンパク質の変異体、フラグメント、または融合物もまた、使用され得る。また、天然に存在するリポタンパク質の改変体(例えば、アセチル化されたLDL)が使用され得る。これらのリポタンパク質は、リポタンパク質レセプターを発現する細胞へ、ポリヌクレオチドの送達を標的化し得る。好ましくは、リポタンパク質が、送達されるポリヌクレオチドとともに含まれる場合、他の標的化リガンドはその組成物中には含まれない。
ポリカチオン性薬剤は、送達される所望のポリヌクレオチド/ポリペプチドを有する組成物中に、リポタンパク質を伴って、またはリポタンパク質を伴わずに含まれ得る。
本発明の髄膜炎菌性抗原は、抗体レベルを検出するためのイムノアッセイにおいて使用され得る(または、逆に抗髄膜炎菌性抗体は抗原レベルを検出するために使用され得る)。充分に規定された組換え抗原に基づくイムノアッセイは、侵襲性の診断方法と置き換えるために開発され得る。生物学的サンプル(例えば、血液サンプルまたは血清サンプルを含む)内の髄膜炎菌性タンパク質に対する抗体が検出され得る。このイムノアッセイの設計は、多くのバリエーションの対象であり、そして種々のこれらは当該分野で公知である。イムノアッセイのプロトコルは、例えば、競合アッセイ、または直接反応アッセイ、またはサンドイッチ型アッセイに基づき得る。プロトコルはまた、例えば、固体支持体を使用し得、または免疫沈降によってなされ得る。ほとんどのアッセイは、標識された抗体またはポリペプチドの使用を含み、その標識は、例えば、蛍光分子、化学発光分子、放射性分子、または色素分子であり得る。プローブからのシグナルを増幅するアッセイは公知である;これらの例は、ビオチンおよびアビジンを利用するアッセイ、ならびに酵素標識および酵素媒介イムノアッセイ(例えば、ELASAアッセイ)である。
「ハイブリダイゼーション」とは、水素結合による2つの核酸配列の互いの会合をいう。代表的には、1つの配列は、固体支持体に固定され、そして他方は溶液中で遊離している。次いで、2つの配列は水素結合に好ましい条件下で互いに接触される。この結合に影響を与える因子は以下を含む:溶媒のタイプおよび容量;反応温度;ハイブリダイゼーションの時間;撹拌;液体相の配列の固体支持体への非特異的な付着をブロックする薬剤(Denhardt’s試薬またはBLOTTO);配列の濃度;配列の会合の速度を増大させる化合物(硫酸デキストランまたはポリエチレングリコール)の使用;およびハイブリダイゼーション後の洗浄条件のストリンジェンシー。Sambrookら(前出)第2巻、第9章、9.47〜9.57頁。
Tm=81+16.6(log10Ci)+0.4[%(G+C)]−0.6(%ホルムアミド)−600/n−1.5(%ミスマッチ)。
ここでCiは塩濃度(一価イオン)であり、およびnは塩基対内のハイブリッドの長さである(MeinkothおよびWahl(1984)Anal.Biochem.138:267/284からわずかに改変した)。
本発明に従う核酸プローブを利用する、PCR、分枝DNAプローブアッセイ、またはブロッティング技術のような方法は、cDNAまたはmRNAの存在を決定し得る。プローブは、検出されるに十分安定な、二重鎖または二本鎖複合体を形成し得る場合に、本発明の配列に「ハイブリダイズする」といわれる。
WO99/36544に開示されるタンパク質配列を、全長タンパク質内の推定抗原性ペプチドフラグメントに対するコンピューター分析に供した。この分析には以下の3つのアルゴリズムを用いた。
●AMPHI:このプログラムは、T細胞エピトープを予測するために用いられてきた[Gaoら(1989)J.Immunol.143:3007;Robertsら(1996)AIDS Res Hum Retrovir 12:593;Quakyiら(1992)Scand J Immunol 補遺.11:9]そして、DNASTAR,Inc.のProteanパッケージにおいて利用可能である(1228 South Park Street,Madison,Wisconsin 53715 USA)。
●JamesonおよびWolf(1988)The antigenic index:a novel algorithm for predicting antigenic determinants.CABIOS 4:181:186.によって開示されたような、ANTIGENIC INDEX(抗原性指標)。
●HoppおよびWoods(1981)Prediction of protein antigenic determinants from amino acid sequence.PNAS USA 78:3824〜3828によって開示されたような、HYDROPHILICITY(親水性)。
重要:本出願のフラグメント番号1(Fragment#1)は、WO99/36544に開示されたORF38−1のアミノ酸6〜14であり、本出願のフラグメント番号2(Fragment#2)は、WO99/36544に開示されたORF38−1のアミノ酸57〜59である、など。
本発明は、WO99/36544に開示される45のタンパク質配列のいずれかを含むタンパク質はその範囲内に包含しない。上記のようにWO99/36544に開示された任意の特定のタンパク質配列の長さがxアミノ酸である場合、本発明の抗原性フラグメントは、そのタンパク質の多くともx−1アミノ酸までを有する。WO99/36544に示された45のタンパク質配列のそれぞれについて、参照のためxの値を以下の表に示す。
Claims (8)
- 請求項1に記載の1つ以上のフラグメントを含むタンパク質であって、該タンパク質は、WO00/66741の配列番号13、14、15、16または17ではない、タンパク質。
- 請求項1に記載のフラグメントを認識する、抗体。
- 請求項1に記載のフラグメントまたは請求項2に記載のタンパク質をコードする、核酸。
- 請求項1に記載のフラグメント、請求項2に記載のタンパク質、請求項3に記載の抗体、および/または請求項4に記載の核酸を含む組成物であって、該組成物は、ワクチン、診断試薬、または免疫原性組成物である、組成物。
- 医薬としての使用のための、請求項5に記載の組成物。
- 請求項1に記載のフラグメント、請求項2に記載のタンパク質、請求項3に記載の抗体、および/または請求項4に記載の核酸の使用であって、該使用は、(i)ナイセリア細菌による感染を処置もしくは予防するための医薬、(ii)ナイセリア細菌の存在、もしくはナイセリア細菌に対して惹起された抗体の存在を検出するための診断試薬、および/または(iii)ナイセリア細菌に対する抗体を惹起し得る試薬、の製造における、使用。
- ナイセリア細菌による感染を処置または予防における使用のための、請求項1に記載のフラグメント、請求項2に記載のタンパク質、請求項3に記載の抗体、または請求項4に記載の核酸。
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JP2013078340A (ja) | 2013-05-02 |
MXPA02000463A (es) | 2002-07-02 |
AU5839300A (en) | 2001-01-30 |
CN1590404A (zh) | 2005-03-09 |
EP1196587A2 (en) | 2002-04-17 |
RU2253678C2 (ru) | 2005-06-10 |
ATE397068T1 (de) | 2008-06-15 |
CA2378547A1 (en) | 2001-01-18 |
CN1373805A (zh) | 2002-10-09 |
JP2003504062A (ja) | 2003-02-04 |
GB9916529D0 (en) | 1999-09-15 |
WO2001004316A3 (en) | 2001-08-09 |
RU2002103604A (ru) | 2004-03-10 |
EP1935979A2 (en) | 2008-06-25 |
WO2001004316A2 (en) | 2001-01-18 |
EP1935979A3 (en) | 2008-09-17 |
DE60039050D1 (de) | 2008-07-10 |
EP1196587B1 (en) | 2008-05-28 |
CA2801979A1 (en) | 2001-01-18 |
US7618636B1 (en) | 2009-11-17 |
BR0012424A (pt) | 2002-07-02 |
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