JP2010539927A - ファージφMRUポリヌクレオチドおよびポリペプチドならびにその使用 - Google Patents
ファージφMRUポリヌクレオチドおよびポリペプチドならびにその使用 Download PDFInfo
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Abstract
Description
本出願は、2007年9月25日に提出した米国特許出願第60/975,104号、2007年11月22日に提出した米国特許出願第60/989,840号、および2007年11月22日に提出した米国特許出願第60/989,841号の利益を主張するものであり、これら全ての出願内容はその全体が参照によりここに取り込まれる。
定義
ここで用いられる、ファージポリペプチドをコードする「変化した」核酸配列は、好ましくは同じかまたは機能的に同等なポリペプチドをコードするポリヌクレオチドをもたらす、異なるヌクレオチドの欠失、挿入、または置換による核酸配列を含む。コードされるポリペプチドまたは抗体もまた「変化」してよく、サイレント変化を生じて機能的に同等なポリペプチドをもたらすアミノ酸残基の欠失、挿入、または置換を含む。意図されたアミノ酸置換が、残基の極性、電荷、溶解度、疎水性、親水性、および/または両親媒性性質の類似性に基づき、生物学的活性(例えば細胞結合、細胞透過性、もしくは細胞融解)もしくはポリペプチドの免疫学的活性(例えば1つ以上の抗体結合部位)を保持する限りにおいて行なわれてよい。例えば陰性荷電アミノ酸はアスパラギン酸およびグルタミン酸を含んでよく;陽性荷電アミノ酸はリジンおよびアルギニンを含んでよく;類似の親水性値を有する非荷電の極性頭部基をもつアミノ酸はロイシン、イソロイシン、およびバリン、グリシンおよびアラニン、アスパラギンおよびグルタミン、セリンおよびスレオニン、ならびにフェニルアラニンおよびチロシンを含んでよい。
Dveksler (1995) PCR Primer, a Laboratory Manual, Cold Spring Harbor Press, Plainview, NY)。
Molecular Cloning, A Laboratory Manual, Cold Spring Harbor Press, Plainview, NY, および Ausubel, F. M. et al. (1989) Current Protocols in Molecular Biology, John Wiley & Sons, New York, NY. を参照のこと。低または高ストリンジェンシーのいずれかを含む多数の同等な条件は、配列(DNA、RNA、塩基組成物)の長さおよび性質、標的(DNA、RNA、塩基組成物)の性質、環境(溶液中または固体基質上での不動化)、塩およびその他の構成成分(例えばホルムアミド、硫酸デキストランおよび/またはポリエチレングリコール)の濃度、ならびに反応温度(プローブの融解温度より約5℃低い温度から、融解温度より約20℃から25℃低い温度の範囲内)のような因子に依存する。上に列挙した条件とは異なるが同等である、低または高ストリンジェンシーのいずれかの条件を作り出すため、1つ以上の因子が変化させられてよい。
メタンは反すう動物の前腸内で、反すう胃システムにおける炭素の最終還元作用を行うメタン生成菌により産生される。多段階メタン生成経路は、主に非反すう胃メタン生成菌の研究によって十分に解明されているが、反すう胃においてメタン生成菌の生育および存続を可能にするための適応はよく理解されていない。Methanobrevibacter ruminantiumは、ニュージーランドの反すう動物における有名なメタン生成菌である。ここに述べるように、M.ルミナンチウム(M. ruminantium)のゲノムが配列決定され、約3.0Mbのサイズにおける33.68%のGC含有量が示された。予想外の発見として、M.ルミナンチウム(M. ruminantium)のゲノムは、ファージ組み込み、DNA複製およびパッケージング、カプシドタンパク質、溶解、ならびに溶原性変換機能をコードする異なる機能モジュールを持つプロファージ配列(φmruと命名された)を含むことが見出された。
AS, . Hartl, DL. Genetics. 1988 Nov; 120(3):621-3を参照)。逆PCRは、標的DNAの内部配列のみが既知である場合に用いることができる。逆PCR法は、DNAを制限酵素で切断することによる、一連の消化および自己ライゲーションを含む。この切断は、未知の配列のいずれかの末端において既知の配列をもたらす。この方法に従い、標的DNAは制限酵素消化によって数キロベースの小さめの断片に容易に切断される。続いて自己ライゲーションは、リン酸骨格の再編成をもたらし、かつ環状DNAライゲーション産物を産生する低濃度において誘導される。標的DNAは次に既知の制限酵素により制限消化される。これは、既知の末端配列を有する直線状産物を生じる、既知の内部配列内の切断を生じる。この産物は次に、既知の内部配列に相補的なプライマーを用いて行われる標準PCRのために使用できる。
7417 (1987); Bothwell et al., Methods for Cloning and Analysis of Eukaryotic Genes, Eds., Jones and Bartlett Publishers Inc., Boston, Mass. (1990), Ausubel et al., Short Protocols in Molecular Biology, John Wiley and Sons, New York, NY (1992);およびFarhood, Annal. NY Acad. Sci., 716:23 34 (1994))、プロトプラスト(Bothwell、上記)または電気的パルス(Vatteroni et al., Mutn. Res., 291:163 169 (1993); Sabelnikov, Prog. Biophys. Mol. Biol., 62: 119 152 (1994); Bothwell et al.、上記;および Ausubel et al.、上記)の使用、弱毒化ウィルスの使用(Davis et al., J. Virol. 1996, 70(6), 3781 3787; Brinster et al. J. Gen. Virol. 2002, 83(Pt 2), 369 381; Moss, Dev. Biol. Stan., 82:55 63 (1994); および Bothwell et al.、上記)、同様に物理的方法(Fynan et al., 上記、 Johnston et al., Meth Cell Biol., 43(Pt A): 353 365 (1994); Bothwell et al.、上記; および Ausubel et al.、上記)を含む。
Biotech、Promega、およびUS Biochemicalの様々な市販キットを用いて行われてよい。検出を容易にするために用いられてよい適切なレポーター分子または標識は、放射性核種、酵素、蛍光、化学発光、または発色薬剤、同様に基質、補因子、抑制剤、磁性粒子などを含む。
Nature 312:604-608; Takeda, S. et al. (1985) Nature 314:452-454)。あるいは、特異的な単鎖抗体を産生するために、単鎖抗体の産生のために記述された技術が当該技術分野において公知の方法を用いて適応されてよい。ランダムコンビナトリアル免疫グロブリンライブラリーからの鎖のシャッフリングにより、明確なイディオタイプ構成成分ではないが関連した特異性を有する抗体が作られてよい(Burton D. R. (1991) Proc. Natl. Acad. Sci. 88:11120-3)。
Sciences (Maack Publishing Co., Easton, PA)の最新版に見出されるであろう。本発明で利用される医薬組成物は、経口、静脈内、筋肉内、動脈内、延髄内、包膜内、心室内、経皮、皮下、腹腔内、鼻内、経腸、外用、舌下、または直腸の手段を含むがこれらに限定されないいずれの数の経路により投与されてよい。
は、得られる配列に融合または連結される細胞抑制剤をさらに含む。好ましい野菜材料は、乾草、草、穀粒、もしくは穀粉、例えば豆乾草、草乾草、トウモロコシサイレージ、草サイレージ、豆サイレージ、トウモロコシ粒子、カラスムギ、オオムギ、蒸留かす、ビールかす、大豆穀粉、および綿実穀粉のいずれか1種を含む。特に、反すう動物の食物組成物として草サイレージが有用である。植物材料は、本発明の構成成分の1種以上、例えばポリペプチドもしくはペプチド、ポリヌクレオチド、またはベクターのうち1種以上を含むように遺伝的に改変できる。
メタノブレビバクター・ルミナンチウム(Methanobrevibacter ruminantium)のM1T株(DSM1093)は、[g/l]NaCl(1)、KH2PO4(0.5)、(NH4)2SO4(0.25)、CaCL2.2H2O(0.13)、MgSO4.7H2O(0.2)、K2HPO4(1)、浄化した反すう胃液(300ml)dH2O(360ml)、NaHCO3(5)、レザズリン(0.2ml)L−システイン−HCl(0.5)、酵母抽出物(2)、ならびに、(g/l)ニトリロ三酢酸(1.5)、MgSO4.7H2O(3)、MnSO4.H2O(0.5)、NaCl(1)、FeSO4.7H2O(0.1)、CoCl2.6H2O(0.1)、CaCl2(0.1)、ZnSO4.7H2O(0.1)、CuSO4.5H2O(0.01)、AlK(SO4)2.12H2O(0.01)、H3BO3(0.01)、Na2MoO4.2H2O(0.01)、NiSO4.6H2O(0.03)、Na2SeO3(0.02)、およびNa2Wo4.2H2O(0.02)から成るBalchの微量元素溶液(10ml)(微量元素の添加;Balch et al., 1979)、から成るBY+培地(基本培地、Joblin et al., 1990)中で生育した。凍結粉砕法を用いてゲノムDNAを抽出した。細胞を遠心によって回収し、細胞ペレットを予め冷却した乳鉢内に配置し、液体窒素により凍結し、かつ予め冷却した滅菌乳鉢および乳棒を用いて穏やかに粉砕して微粉にした。ゲノムDNAの物理的せん断を減少させるため、細胞ホモジネートをアガロースプラグ上に包埋し、続く操作をプラグ内で行った。制限酵素により消化を行い、DNA断片をパルスフィールドゲル電気泳動(PFGE)を用いて分離した。
M.ルミナンチウム(M. ruminantium)ゲノムのDNAは、Agencourt Biosciences Corporation(マサチューセッツ州、米国)によりランダムショットガンクローニングアプローチ(Fleischmann et al., 1995)を用いて、およびMacrogen Corporation(ロックビル、メリーランド州、米国)によりピロシーケンスを用いて配列決定された。簡単に述べると、M.ルミナンチウム(M. ruminantium)のDNAのライブラリーを、ゲノムDNAのランダムな物理的破壊およびゲル電気泳動による断片の分離により、Escherichia coli内へ構築した。40kb範囲の大きな断片をゲルから回収し、大インサートのフォスミドライブラリーを作製するために使用した。2ないし4kb範囲のDNA断片を回収し、小インサートのプラスミドライブラリーを作製するために使用した。大および小インサートライブラリーの両方からもたらされたクローンを生育させ、それらのフォスミドまたはプラスミドDNAを回収し、ハイスループット配列決定技術を用いて配列決定した。M.ルミナンチウム(M. ruminantium)ゲノムの理論的な8倍のカバー率を生ずるために十分な数のクローンを配列決定した。10倍の最終理論的なカバー率を得るため、ランダムにせん断されたゲノムDNA断片についてピロシーケンスを行った。
配列の重複を見出すためにDNA配列を整列し、Paracel Genome Assembler(Paracel Inc、カリフォルニア州、米国)およびStadenパッケージ(Staden et al., 1998)を用い、標準および逆PCRの両方から得られた配列を組み合わせて、近接する(コンティグ)配列へ構築した。コンティグは翻訳領域(ORF)ファインダーGLIMMER(Gene Locator Interpolated Markov Model ER、Delcher et al., 1999)を用いて分析し、各ORFは、National Center for Biotechnology Information(NCBI)の非重複性ヌクレオチドおよびタンパク質データベースに対するギャップ付きBLAST(Basic Local Alignment Search Tool(Altschul et al., 1997))により分析した。8倍のドラフト段階の配列からのコンティグを、「偽分子」を産生するために配列の人工連結によってランダムに連結し、自動アノテーションのためThe Institute for Genomic Research(TIGR、ワシントンDC、米国)へ提出した。10倍のピロシーケンスから構築されたコンティグはGLIMMERを用いて再分析し、ORFはGAMOLA(Global Annotation of Multiplexed On-site Blasted DNA sequences; Altermann and Klaenhammer, 2003)を用いて自動アノテートした。ORFはオルソログタンパク質(COG)データベース(閾値1e−02)(Tatusov et al., 2001)のクラスターを用いる関数により分類した。
ゲノムDNAの制限酵素消化およびPFGEによる断片のサイズ決定によるM.ルミナンチウム(M. ruminantium)ゲノムのサイズ推定は、約2.5〜2.9Mbの単一染色体を示した。大および小インサートクローン(6倍ドラフトカバー率)の最初の配列決定および配列のコンティグへの構築は、ゲノムの40kb範囲が、特に小インサートライブラリー内で高度に過剰表現(>20倍)されていることを示した。これは高コピー数のプラスミド(染色体外DNAは同定されていないが)、またはDNA抽出のために使用した培養物の生育の間に複製した溶原性バクテリオファージによる可能性がある。この大きな配列バイアスのため、さらなる配列決定(2倍の理論的ゲノムカバー率)を、サンガー配列決定法により最終の8倍のカバー率をもたらす小インサートクローンのみについて行った。8倍のドラフト段階の配列を、105のスキャフォールドを通して連結した756のコンティグへ構築した。さらなる〜10倍のカバー率に対してさらなるピロシーケンスを行い、これらの配列の構築への取り込みはコンティグの数を27に低下させた。これに続く逆および長距離PCR技術を用いるギャップ閉鎖は、コンティグの数を14に減少させ、1の誤構築が残った。
M.ルミナンチウム(M. ruminantium)ゲノム配列内のプロファージ配列の発見は予想外であった。これまでにメタノブレビバクター・ルミナンチウム(Methanobrevibacter ruminantium)系統M1(DSM1093)が溶解または溶原性ファージに感受性であるという報告はないが、その他のメタノブレビバクター種において同定されたファージについては報告されている(Baresi and Bertani, 1984; Knox and Harris, 1986)。φmruプロファージの配列は、周囲のM.ルミナンチウム(M. ruminantium)ゲノムよりも著しく高いG+C含量であり、これが別の生物に由来することが示唆される。観察されるレベルでの相同性はそれが由来する明らかなホストを示唆せず、φmruはこれまでに遭遇したいずれのその他のファージとも異なることが示される。
X, Liang J, Li A, Xu T, Kieser T, Helmann JD, Deng Z. A novel DNA modification by sulphur. Mol Microbiol. 2005 Sep;57(5):1428-38)。
ruminantium)または外来性DNAの保護または修飾における役割は明らかではない。φmru配列の別の興味ある特徴は、アンチセンス鎖上にコードされる幾つかのORFである。これらのORFは低GC領域に相当し、様々な生物由来のタンパク質に対して弱いBLASTマッチを有する。このことは、これらの遺伝子がM.ルミナンチウム(M. ruminantium)への組み込み以来、φmruゲノム内に蓄積していることを示唆し得る。これらのORFが、最終的にファージの不活性化および順化をもたらし得る挿入の進行中の蓄積を表すか、またはφmruが完全に活性であるかについては明らかではない。
メタノブレビバクター・ルミナンチウム(Methanobrevibacter ruminantium)のM1T株(DSM1093)は、[g/l]NaCl(1)、KH2PO4(0.5)、(NH4)2SO4(0.25)、CaCL2.2H2O(0.13)、MgSO4.7H2O(0.2)、K2HPO4(1)、浄化した反すう胃液(300ml)dH2O(360ml)、NaHCO3(5)、レザズリン(0.2ml)L−システイン−HCl(0.5)、酵母抽出物(2)、ならびに、(g/l)ニトリロ三酢酸(1.5)、MgSO4.7H2O(3)、MnSO4.H2O(0.5)、NaCl(1)、FeSO4.7H2O(0.1)、CoCl2.6H2O(0.1)、CaCl2(0.1)、ZnSO4.7H2O(0.1)、CuSO4.5H2O(0.01)、AlK(SO4)2.12H2O(0.01)、H3BO3(0.01)、Na2MoO4.2H2O(0.01)、NiSO4.6H2O(0.03)、Na2SeO3(0.02、およびNa2WO4.2H2O(0.02)から成るBalchの微量元素溶液(10ml)(微量元素の添加;Balch et al., 1979)、から成るBY+培地(基本培地、Joblin et al., 1990)中で生育した。
ORF2058によりコードされるポリペプチドは、反すう胃メタン生成菌特異的な溶解酵素として有用であり、組み換えタンパク質の産生のため大腸菌(E. coli)発現ベクターにサブクローン化されている。ORF2058は、プライマーMbbrum11for22(1122For,cac cat ggt tag aft cag cag age c;配列番号148)およびMbbrev11rev22(1122Rev,tca tgc agg ace gac aac ata gta g;配列番号149)を用い、121.5ng M.ルミナンチウム(M. ruminantium)系統M1ゲノムDNA;0.2pM 1122Forおよび1122Revプライマー;15pL Accuprime Pfx緩衝液(dNTPと共に、InVitrogen);2.4pL Accuprime Pfx(InVitrogen)を含む150μL反応量中でPCRにより増幅した。PCR条件は、95℃、2分間の最初の変性に続き、95℃、15秒間、55℃、30秒間、および68℃、40秒間の35サイクルであった。最終伸長は行わなかった。PCR産物を精製し、Nanodrop(Thermo Scientific、ジョージア州、米国)を用いて定量した。
ruminantium)はRM02培地中で生育した。RM02培地は以下の成分(g/L):KH2PO4(1.4)、(NH4)2SO4(0.6)、KCl(1.5、)微量元素溶液 SL10(1ml)、亜セレン酸塩/タングステン酸塩溶液(1ml)、0.1%(w/v)レザズリン溶液(4滴)から構成される。構成成分を混合し、O2を含まない100%CO2下で沸騰させ、100%CO2により泡立てながら氷浴中で冷却した。冷却後、NaHCO3(4.2g)およびL−システインHCl・H2O(0.5g)を加え、9.5mlの培地をHungateチューブに分注する一方、チューブに100%CO2を供給した。チューブはオートクレーブし、使用前24時間暗所に保管した。接種に先立ち、NoSubRFV(1チューブあたり0.5ml、基質、酵母抽出液、ビタミンを含む)を加えた。接種チューブに80%CO2/20%H2を25lb/in2で供給した後、M.ルミナンチウム(M. ruminantium)を中期対数期(OD600nm〜0.1)まで生育させ、この点で様々な濃度のORF2058溶解酵素(pET 151Dトポクローンから調製された)を培養物へ加えた。培養物のインキュベーションを続け、OD読み取りを記録した。M.ルミナンチウム(M. ruminantium)生育およびメタン形成における酵素添加の効果(無添加に比較した%メタン産生;217時間生育後のコントロールを角括弧内に示す)を図8に示す。結果はORF2058溶解酵素が、M.ルミナンチウム(M. ruminantium)の生育に量依存的に劇的に影響したことを示し、添加2時間以内に生育中の培養物のOD600nmを減少させた。二つの最も高い酵素添加濃度もまたメタン形成を、クロロホルム添加(100μl/10ml培養物添加)と同程度まで減少させた。
M.ルミナンチウム(M. ruminantium)ゲノム配列決定からの予想外の発見はプロファージ配列の存在であった。ゲノム配列の分析は幾つかのファージ関連遺伝子を含む異常に高いGC含有領域を同定した。予測されるプロファージの全体構造はさらなるバイオインフォティック分析により同定され、φmruと名付けられた。約40%のファージ遺伝子が、ファージ組み込み、DNA複製およびパッケージング、ファージ構造タンパク質ならびに溶解を含む機能的グループを分離するために割り当てられた。ファージゲノムに隣接するDNA配列は、ファージ組み込みの潜在的部位を表すことが見出された(attLおよびattR)。ファージは、φmruファージゲノムであるattBの本来のメタン生成菌組み込み部位を有すると思われる、M.ルミナンチウム(M. ruminantium)の予測される膜タンパク質へそれ自体で組み込まれると考えられる。さらに、DNA複製モジュール内に見出された転写終結区様構造は、ファージDNA複製の起点を表すと考えられる。ファージゲノムの3’末端の低GC領域は、dndシステムの発現を制御すると思われる遺伝子を含む、硫黄によるDNA修飾システムであると考えられる領域を有する。これらの遺伝子はおそらくファージ組み込みの間にM.ルミナンチウム(M. ruminantium)ゲノム内に運ばれたと考えられ、そのファージ、ホストまたは外来性DNAについての役割は解明されていない。M.ルミナンチウム(M. ruminantium)によるdndシステムの保持は、それがホストに利益を与えることを示唆する。しかしながら、φmru dndシステムのM.ルミナンチウム(M. ruminantium)または外来性DNAの修飾における役割は、なお研究途上である。
Claims (57)
- 配列番号2〜5から成る群より選択されるアミノ酸配列を含む、単離されたポリペプチド。
- 配列番号62から成る群より選択されるアミノ酸配列を含む、単離されたポリペプチド。
- 配列番号63および72から成る群より選択されるアミノ酸配列を含む、単離されたポリペプチド。
- 配列番号64〜68から成る群より選択されるアミノ酸配列を含む、単離されたポリペプチド。
- 配列番号6〜61、および69から成る群より選択されるアミノ酸配列を含む、単離されたポリペプチド。
- 配列番号2〜5から成る群より選択されるアミノ酸配列と90%の同一性を共有する、単離されたポリペプチド。
- 配列番号62から成る群より選択されるアミノ酸配列と90%の同一性を共有する、単離されたポリペプチド。
- 配列番号63および72から成る群より選択されるアミノ酸配列と90%の同一性を共有する、単離されたポリペプチド。
- 配列番号64〜68から成る群より選択されるアミノ酸配列と90%の同一性を共有する、単離されたポリペプチド。
- 配列番号1、6〜61、および69から成る群より選択されるアミノ酸配列と90%の同一性を共有する、単離されたポリペプチド。
- 配列番号2〜5から成る群より選択されるアミノ酸配列をコードする、単離されたポリヌクレオチド。
- 配列番号62から成る群より選択されるアミノ酸配列をコードする、単離されたポリヌクレオチド。
- 配列番号63および72から成る群より選択されるアミノ酸配列をコードする、単離されたポリヌクレオチド。
- 配列番号64〜68から成る群より選択されるアミノ酸配列をコードする、単離されたポリヌクレオチド。
- 配列番号1、6〜61、および69から成る群より選択されるアミノ酸配列をコードする、単離されたポリヌクレオチド。
- 配列番号75〜78から成る群より選択されるヌクレオチド配列を含む、単離されたポリヌクレオチド。
- 配列番号135から成る群より選択されるヌクレオチド配列を含む、単離されたポリヌクレオチド。
- 配列番号136から成る群より選択されるヌクレオチド配列を含む、単離されたポリヌクレオチド。
- 配列番号137〜141から成る群より選択されるヌクレオチド配列を含む、単離されたポリヌクレオチド。
- 配列番号74、79〜134および142から成る群より選択されるヌクレオチド配列を含む、単離されたポリヌクレオチド。
- 請求項1〜10のいずれか1項に記載のポリペプチドをコードするベクター。
- 請求項11〜20のいずれか1項に記載のポリヌクレオチドを含むベクター。
- 請求項21または22に記載のベクターを含むホスト細胞。
- 請求項1〜10のいずれか1項に記載のポリペプチドをコードするように遺伝的に改変されたホスト細胞。
- 請求項11〜20のいずれか1項に記載のポリヌクレオチドを含むように遺伝的に改変されたホスト細胞。
- 原核生物である、請求項23〜25のいずれか1項に記載のホスト細胞。
- Escherichia coliである、請求項26に記載のホスト細胞。
- メタン生成菌である、請求項23〜25のいずれか1項に記載のホスト細胞。
- メタノブレビバクター・ルミナンチウム(Methanobrevibacter ruminantium)である、請求項28に記載のホスト細胞。
- 請求項1〜10のいずれか1項に記載のポリペプチドを含む抱合体分子。
- 請求項3または8に記載のポリペプチドを含む抱合体分子。
- 抗メタン生成化合物、シグナル配列、抗体もしくは抗体断片、ペプチド核酸、抗菌ペプチド、または抗生剤をさらに含む、請求項30または31に記載の抱合体分子。
- 請求項1〜10のいずれか1項に記載のポリペプチドを含む融合体分子。
- 請求項3または8に記載のポリペプチドを含む融合体分子。
- 抗メタン生成化合物、シグナル配列、抗体もしくは抗体断片、ペプチド核酸、抗菌ペプチド、または抗生剤をさらに含む、請求項33または34に記載の融合体分子。
- 請求項1〜10のいずれか1項に記載のポリペプチドに結合する、抗体または抗体断片。
- ポリクローナルである、請求項36に記載の抗体または抗体断片。
- モノクローナルである、請求項36に記載の抗体または抗体断片。
- 請求項1〜10のいずれか1項に記載の少なくとも1つのポリペプチドを含む、単離されたφmruファージ。
- 請求項3または8に記載の少なくとも1つのポリペプチドを含む、単離されたφmruファージ。
- 請求項11〜20のいずれか1項に記載の少なくとも1つのポリヌクレオチドを含む、単離されたφmruファージ。
- 請求項13および18に記載の少なくとも1つのポリヌクレオチドを含む、単離されたφmruファージ。
- 請求項1〜10のいずれか1項に記載のポリペプチドを含む医薬組成物。
- 請求項11〜20のいずれか1項に記載のポリヌクレオチドを含む医薬組成物。
- 請求項39〜42のいずれか1項に記載のファージを含む医薬組成物。
- メタン生成菌細胞を抑制する方法であって、a)必要に応じて、請求項3または8に記載のポリペプチドを産生または単離すること;およびb)該細胞を該ポリペプチドに接触させることを含む方法。
- 該細胞がメタノブレビバクター・ルミナンチウム(Methanobrevibacter ruminantium)である、請求項46に記載の方法。
- 該細胞がメタノブレビバクター・ルミナンチウム(Methanobrevibacter ruminantium)のM1T株(DSM1093)である、請求項47に記載の方法。
- メタン生成菌細胞を抑制する方法であって、a)必要に応じて、請求項31または32に記載の抱合体分子を産生または単離すること;およびb)該細胞を該抱合体分子に接触させることを含む方法。
- 該細胞がメタノブレビバクター・ルミナンチウム(Methanobrevibacter ruminantium)である、請求項49に記載の方法。
- 該細胞がメタノブレビバクター・ルミナンチウム(Methanobrevibacter ruminantium)のM1T株(DSM1093)である、請求項50に記載の方法。
- メタン生成菌細胞を抑制する方法であって、a)必要に応じて、請求項34または35に記載の融合体分子を産生または単離すること;およびb)該細胞を該融合体分子に接触させることを含む方法。
- 該細胞がメタノブレビバクター・ルミナンチウム(Methanobrevibacter ruminantium)である、請求項52に記載の方法。
- 該細胞がメタノブレビバクター・ルミナンチウム(Methanobrevibacter ruminantium)
のM1T株(DSM1093)である、請求項53に記載の方法。 - メタン生成菌細胞を抑制する方法であって、a)必要に応じて、請求項40または42に記載のファージを産生または単離すること;およびb)該細胞を該ファージに接触させることを含む方法。
- 該細胞がメタノブレビバクター・ルミナンチウム(Methanobrevibacter ruminantium)である、請求項55に記載の方法。
- 該細胞がメタノブレビバクター・ルミナンチウム(Methanobrevibacter ruminantium)のM1T株(DSM1093)である、請求項56に記載の方法。
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