JP2006513691A - 免疫原性が減少したズブチリシン・カールスバーグタンパク質 - Google Patents
免疫原性が減少したズブチリシン・カールスバーグタンパク質 Download PDFInfo
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- JP2006513691A JP2006513691A JP2003571434A JP2003571434A JP2006513691A JP 2006513691 A JP2006513691 A JP 2006513691A JP 2003571434 A JP2003571434 A JP 2003571434A JP 2003571434 A JP2003571434 A JP 2003571434A JP 2006513691 A JP2006513691 A JP 2006513691A
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Abstract
Description
本発明はズブチリシン・カールスバーグタンパク質におけるCD4+T細胞エピトープを同定する方法を提供する。本発明は、野生型ズブチリシン・カールスバーグタンパク質(Carlsberg protein)内に組込まれた場合、ヒトにおいて変化した免疫原性反応、好ましくは低免疫原性反応を生じる変性ペプチドを生成する方法も提供する。特に、本発明ALCALASE(登録商標)酵素の免疫原性を減少させるために適した方法及び組成物を含む手段を提供する。
工業的、医薬的及び商業的用途に用いられるタンパク質の普及及び重要性は増加してきている。しかしながら、これによりこれらのタンパク質に対する多く個体への感作を生じ、広範囲にわたってこれらのタンパク質に対するアレルギー反応の発生が生じている。例えば、いくつかのプロテアーゼは特定個体の超過敏反応に関連する。結果として、プロテアーゼの工業的(例えば、洗濯用洗剤、化粧品、織物処理等)有用性及び改善されたプロテアーゼ(例えば、一般的な洗剤条件下でより効果的にシミを除去する変異体ズブチリシン・カールスバーグ酵素)を提供しようとする分野で行われる広範囲の研究にも関わらず、工業上のプロテアーゼの使用は問題を含むものであった。
本発明はズブチリシン・カールスバーグタンパク質においてCD4+T細胞エピトープを同定する方法を提供する。本発明は、野生型ズブチリシン・カールスバーグタンパク質(Carlsberg protein)内に組込まれた場合、ヒトにおいて変化した免疫原性反応、好ましくは低免疫原性反応を生じる変性ペプチドを生成する方法も提供する。特に、本発明ALCALASE(登録商標)酵素の免疫原性を減少させるために適した方法及び組成物を含む手段を提供する。本発明は、野生型ズブチリシン・カールスバーグタンパク質配列に組込まれた場合、もはやCD4+T細胞反応を開始することができず、または少なくともアレルギー反応が減少した変性ペプチドを生成する方法も提供する。特に、本発明は野生型ズブチリシン・カールスバーグの免疫原性を減少するために適した方法及び組成物を含む手段を提供する。
酵素は野生型ズブチリシン・カールスバーグ酵素と比較して減少した免疫原性/アレルギー性を示す。これらの変異体酵素は、パーソナル/消費者ケア用品から工業的生産及び使用にわたる多数の製品及び方法に使用できる。
本発明はズブチリシン・カールスバーグタンパク質においてCD4+T細胞エピトープを同定する方法を提供する。本発明は、野生型ズブチリシン・カールスバーグタンパク質(Carlsberg protein)内に組込まれた場合、ヒトにおいて変化した免疫原性反応、好ましくは低免疫原性反応を生じる変性ペプチドを生成する方法も提供する。特に、本発明ALCALASE(登録商標)酵素の免疫原性を減少させるために適した方法及び組成物を含む手段を提供する。本発明は、野生型ズブチリシン・カールスバーグタンパク質配列に組込まれた場合、もはやCD4+T細胞反応を開始することができず、または少なくともアレルギー反応が減少した変性ペプチドを生成する方法も提供する。特に、本発明は野生型ズブチリシン・カールスバーグの免疫原性を減少するために適した方法及び組成物を含む手段を提供する。
別段に定めない限り、ここで用いる全ての技術及び科学用語は本発明が属する技術の当業者により通常理解される意味と同じ意味を有する。例えば、Singleton and Sainsbury,Dictionary of Microbiology and molecular Biology,第2版、John Wiley and Sons,NY(1994);及びHale and Marham,The Harper Collins Dictionary of Biology,Harper Perennial,NY(1991)は当業者にとってここで用いる用語の多くの一般的な辞書となるものである。ここに記載した方法及び物質に類似または同等のものは本発明の実施に用いることができるが、好ましい方法及び物質についてここに記載する。従って、下記に定義される用語は本明細書の全体を参照することによりさらに詳細に説明される。また、文脈で明らかに示さない限り、ここで用いる単数形は複数のものも含むものとする。
いくつかの実施態様において、本発明により提供される組成物は約0.1重量%〜約20重量%、好ましくは約1重量%〜約10重量%、より好ましくは約2重量%〜約8重量%のレベルでスキンケア活性を含む。ここで使用する適当なスキンケア活性の非限定的な例として、ビタミンB3成分、パンテノール、ビタミンE、ビタミンE酢酸、レチノール、レチニルプロピオネート、レチニルパルミテート、レチノイン酸、ビタミンC、テオブロミン、α−ヒドロキシ酸、ファルネソール、フィタントリオール、サリチル酸、パルミチル ペプタペプチド−3及びこれらの混合物などがある。
他の適当なスキンケア活性はレチノイドである。ここで用いる、“レチノイド”は、肌においてビタミンAの生物学的活性を有するビタミンAまたはレチノイド様化合物の天然及び/または合成類似体の全て、及びこれらの化合物の幾何異性体及び立体異性体を含む。レチノイドがここに記載の組成物に含まれる場合、通常は約0.005%〜約2%、より好ましくは0.01%〜約2%レチノイドを含む。レチノールは好ましくは約0.01%〜約0.15%の量で用い、レチノールエステルは好ましくは約0.01%〜約2%(例えば、約1%)の量で用いる。
本発明の組成物は安全で有効量の皮膚科学的に許容できるキャリアであって、必須物質及び任意のその他の物質が肌または髪に適当な濃度で運ばれることを可能にするために組込む範囲で肌及び/または髪への局所用途に適したものを使用できることがさらに考えられる。従って、当該キャリアは、選択した標的上に適当な濃度で確実に均一塗布または分布できるように必須成分の希釈剤、分散剤、溶媒等として作用する。
いくつかの実施態様において、本発明の組成物は好ましくは約0.01%〜約20%、より好ましくは約0.1%〜約15%及び特に好ましくは約0.5%〜約10%のレベルで存在する保湿剤を含む。好ましい保湿剤は、限定されないが、多価アルコール、尿素、DまたはDLパンテノール、パントテン酸カルシウム、ロイヤルゼリー、パンテチン、パントテイン、パンテニルエチルエーテル、パンガミン酸、ピリドキシン、パントイルラクトース・ビタミンB複合体、ヘキサン−1,2,6−トリオール、グアニジンまたはその誘導体及びこれらの混合物から選択される化合物を含む。
いくつかの実施態様において、本発明の水中油型エマルジョンの実施態様は約1%〜約20%、好ましくは約1.5%〜約15%、より好ましくは約0.1%〜約8%及びさらにより好ましくは約0.5%〜約5%の皮膚科学的に許容される皮膚軟化剤を含む。皮膚軟化剤は皮膚を円滑にする傾向があり、滑らかさ及び柔軟性を増加させ、乾燥を防止または軽減し、及び/または肌を保護する傾向がある。皮膚軟化剤は通常、水と不混和性であり、高分子量の油性またはワックス性物質及び皮膚軟化剤は局所用組成物に粘着特性を与えることができる。多種多様の適当な皮膚軟化剤が公知であり、本発明で使用できる。例えば、Sagarin,Cosmetics,Science and Technology,第2版、Vol.1、第32〜43頁(1972)は皮膚軟化剤としての使用に適した物質の多数の例を含む。さらに、WO00/24372で議論されている全ての皮膚軟化剤は本発明の使用に適したものと考えられるが、好ましい例についてさらに以下に詳細を概説する:
i)約7〜約40炭素原子を有する直鎖及び分岐鎖炭化水素、例えばドデカン、スクアラン、コレステロール、水素化ポリイソブチレン、イソヘキサデカン、イソエイコサン、イソオクタヘキサコンタン、イソヘキサペンタコンタヘクタン、及びC7−C40分岐鎖炭化水素であるC7−C40イソパラフィン。本発明の使用に適した分岐鎖炭化水素はイソペンタコンタオクタクタン、流動パラフィン及びこれらの混合物から選択される。Permethyl(登録商標)の商標で販売されており、Presperse Inc.,South Plainfield,N.J.から市販の分岐鎖脂肪族炭化水素は本発明の使用に適している。
ii)C1−C30カルボン酸、C12−C15安息香酸アルキル及びC2−C30ジカルボン酸のC1−C30アルコールエステル、例えば、イソノナン酸イソノニル、ネオペンタン酸イソステアリル、オクタン酸イソデシル、イソノナン酸イソデシル、イソノナン酸トリデシル、オクタン酸ミリスチル、ペラルゴン酸オクチル、イソノナン酸オクチル、ミリスチン酸ミリスチル、ネオペンタン酸ミリスチル、オクタン酸ミリスチル、ミリスチン酸イソプロピル、プロピオン酸ミリスチル、ステアリン酸イソプロピル、イソステアリン酸イソプロピル、イソステアリン酸メチル、ベヘン酸ベヘニル、マレイン酸ジオクチル、アジピン酸ジイソプロピル及びジリノール酸ジイソプロピル及びこれらの混合物。
iii)糖類及び関連物質のC1−C30モノ−及びポリ−エステル。これらのエステルは糖またはポリオール部分及び1以上のカルボン酸部分から得られる。構成酸及び糖に応じて、これらのエステルは室温で液体または固体である。例としては、テトラオレイン酸グルコース、オレイン酸のガラクトーステトラエステル、テトラオレイン酸ソルビトール、テトラオレイン酸スクロース、ペンタオレイン酸スクロース、ヘキサオレイン酸スクロース、ヘプタオレイン酸スクロース、オクタオレイン酸スクロース、ソルビトールヘキサエステルがあり、カルボン酸エステル部分はモル比が1:2のパルミトレイン酸とアラキジン酸及びスクロースのオクタエステル(octaester)であり、エステル化カルボン酸部分はモル比が1:3:4のラウリン酸、リノレン酸及びベヘン酸である。その他の物質は綿実油またはスクロースの大豆油脂肪酸エステルを含む。当該物質のその他の例としては、WO96/16636に記載されている。特に好ましい物質はINCLの名前のスクロースポリコットンシーデート(polycottonseedate)により公知である。
iv)植物油及び水素化植物油。植物油及び水素化植物油の例としては、ベニバナ油、ココナッツ油、綿実油、メンハーデン油、パーム核油、ヤシ油、ピーナッツ油、大豆油、菜種油、リンシード油、ぬか油、松根油、ゴマ油、ヒマワリ油、前述の供給源から部分及び完全に水素化された油、及びこれらの混合物が挙げられる。
v)溶性またはコロイド性−溶性保湿剤。例としては、ヒアルロン酸及びでんぷんグラフトポリアクリル酸ナトリウム、例えばCelanese Superabsorbent Materials,Portsmith,VAから市販のSanwet(登録商標)IM−1000、IM−1500及びIM−2500があり、米国特許第4,076,663号に記載されている。
いくつかの実施態様において、本発明の組成物は乳化剤及び/または界面活性剤を含み、通常は連続水相内の分散相が分散及び懸濁するのを助ける。界面活性剤は製品が肌洗浄を目的とするものである場合も有用である。以下、便宜上、乳化剤は“界面活性剤”の語に含むものとする。従って、“界面活性剤”とは乳化剤として用いるか、肌洗浄などその他の界面活性目的であるかに関わらず、表面活性剤をいう。公知または従来の界面活性剤は、選択した物質が組成物の必須成分と化学的及び物理的に適合性であり、所望の性質を与える場合、本発明の組成物に使用できる。適当な界面活性剤は非シリコーン由来物質及びその混合物を含む。WO00/24372に説明されている全ての界面活性剤は本発明での使用に適していると考えられる。
いくつかの実施態様において、本発明の組成物は少なくとも1のポリマー増粘剤(thickening agent)を含む。本発明で有用なポリマー増粘剤の数平均分子量は好ましくは20,000以上、より好ましくは50,000以上及び特に100,000以上である。いくつかの実施態様において、本発明の組成物は組成物の約0.01重量%〜約10重量%、好ましくは約0.1重量%〜約8重量%及び最も好ましくは約0.5重量%〜約5重量%のポリマー増粘剤またはこれらの混合物を含む。
いくつかの実施態様において、本発明は少なくとも1のシリコーン油相を含む。シリコーン油相は通常、組成物の約0.1%〜約20%、好ましくは約0.5〜約10%、より好ましくは約0.5%〜約5%を含む。各シリコーン油相は好ましくは1以上のシリコーン成分を含む。
(i)ジメチコノール、フルオロシリコーン及びジメチコン及びこれらの混合物から選択された約200,000〜約4,000,000の分子量を有するシリコーン;及び
(ii)シリコーン流動体のキャリアであって、当該キャリアの粘度は約0.65mm2s−1〜約100mm2s−1である。
さらに別の実施態様において、本発明は有機サンスクリーンを含んだ組成物を提供する。いくつかの実施態様において、適当なサンスクリーンはUVA吸収特性及び/またはUVB吸収特性を含む。サンスクリーン活性の正確な量は組成物に望ましい太陽光線保護指数(すなわち、“SPF”)及び望ましいUV保護レベルに応じて変化する。本発明の組成物は好ましくはSPFが少なくとも10、好ましくは少なくとも15である。SPFは紅斑に対するサンスクリーンの光保護指数に一般的に用いられる。SPFは保護した肌に生じる紅斑が最小限となるように必要とされる紫外線エネルギーの、同じ個体における保護されていない肌に同じ最小限の紅斑を生じるために必要な紫外線エネルギーに対する比として定義される(Fed.Reg.,43,No.166、38206−38269頁、1978年8月25日を参照)。使用するサンスクリーンの量は一般的には約2%〜約20%、より一般的には約4%〜14%である。適当なサンスクリーンは、限定されないが、Wenninger and McEwen(編集)、CTFA International Cosmetic Ingredient Dictionary and Handbook,第7版、第2巻、1672頁(コスメティック、トイレタリー、アンド フレグランス・アソシエーション,Inc.,ワシントン、D.C.、1977)に記載されているものがある。
いくつかの実施態様において、本発明の組成物は抗菌及び/または抗真菌作用剤を含む。本発明に有用な抗菌及び抗真菌作用剤の非限定的な例は、限定されないが、β−ラクタム剤、キノロン剤、シプロフロキサシン、ノルフロキサシン、テトラサイクリン、エリスロマイシン、アミカシン、2,4,4’−トリクロロ−2’−ヒドロキシジフェニルエーテル、3,4,4’−トリクロロバニリド(trichlorobanilide)、フェノキシエタノール、フェノキシプロパノール、フェノキシイソプロパノール、ドキシサイクリン、カプレオマイシン、クロルヘキシジン、クロルテトラサイクリン、オキシテトラサイクリン、クリンダマイシン、エタンブトール、ヘキサミジン、イセチオン酸塩、メトロニダゾール、ペンタミジン、ゲンタマイシン、カナマイシン、リネオマイシン(lineomycin)、メタサイクリン、メテンアミン、ミノサイクリン、ネオマイシン、ネチルミシン、パロモマイシン、ストレプトマイシン、トブラマイシン、ミコナゾール、塩酸テトラサイクリン、亜鉛エリスロマイシン、エリスロマイシン・エストレート、ステアリン酸エリスロマイシン、硫酸アミカシン、塩酸ドキシサイクリン、硫酸カプレオマイシン、グルコン酸クロルヘキシジン、塩酸クロルヘキシジン、塩酸クロルテトラサイクリン、塩酸オキシテトラサイクリン、塩酸クリンダマイシン、塩酸エタンブトール、塩酸メトロニダゾール、塩酸ペンタミジン、硫酸ゲンタマイシン、硫酸カナマイシン、塩酸リネオマイシン(lineomycin)、塩酸メタサイクリン、馬尿酸メテナミン、マンデル酸メテナミン、塩酸ミノサイクリン、硫酸ネオマイシン、硫酸ネチルミシン、硫酸パロモマイシン、硫酸ストレプトマイシン、硫酸トブラマイシン、塩酸ミコナゾール、塩酸アマンファジン(amanfadine)、硫酸アマンファジン、octopirox、パラクロロメタ(parachlorometa)キシレノール、ナイスタチン、トルナフテート、クロトリマゾール、塩化セチルピリジニウム(CPC)、ピロクトン・オラミン、硫化セレン、ケトコナゾール、トリクロカーボン、トリクロサン、亜鉛パイリシオン、イトラコナゾール、アジアティック酸、ヒノキチオール、mipirocin、塩化clinacycin、過酸化ベンゾイル、過酸化ベンジル、ミノサイクリン、フェノキシイソプロパノール、及びこれらの混合物及び欧州特許第0 680 745に記載されているものを含む。
いくつかの実施態様において、中和剤、香料及び着色料などの種々の任意の成分が本発明の組成物で使用できる。製品が肌の柔軟性/円滑性を高める追加成分は好ましい。さらに、製品の風合いにマイナスの影響を与えないような成分は好ましい。従って、コラーゲン及びエラスチンなどの高レベルのタンパク質は本発明に有用な組成物に通常、好ましいものではない。
本発明の組成物は当業界に公知の標準技術により調製する。通常、水相及び/または油相は別々に調製し、分割した類似相の物質を任意の順番で加える。最終生成物がエマルジョンである場合、2つの相はそれから勢いよくかき混ぜながら混合する。高揮発性の処方中の成分、または高温で加水分解しやすい成分は、該当する場合、乳化後、処理の最後の方で穏やかにかき混ぜながら加えることができる。
本発明はズブチリシン・カールスバーグタンパク質においてCD4+T細胞エピトープを同定する方法を提供する。本発明は、野生型ズブチリシン・カールスバーグタンパク質(Carlsberg protein)内に組込まれた場合、ヒトにおいて変化した免疫原性反応、好ましくは低免疫原性反応を生じる変性ペプチドを生成する方法も提供する。特に、本発明ALCALASE(登録商標)酵素の免疫原性を減少させるために適した方法及び組成物を含む手段を提供する。本発明は、野生型ズブチリシン・カールスバーグタンパク質配列に組込まれた場合、もはやCD4+T細胞反応を開始することができず、または少なくともアレルギー反応が減少した変性ペプチドを生成する方法も提供する。特に、本発明は野生型ズブチリシン・カールスバーグの免疫原性を減少するために適した方法及び組成物を含む手段を提供する。
以下の実施例は本発明の特定の好ましい実施態様及び側面を説明するためのものであり、本発明の範囲を限定するものとして解釈されるものではない。
ヒトT細胞を用いるALCALASE(登録商標)におけるペプチドT細胞エピトープを同定するための分析システムに用いる細胞調製
新しいヒト末梢血細胞をALCALASE(登録商標)酵素への曝露状態が未知の92人のヒトから収集した。これらの細胞を実施例3に記載するように、ALCALASE(登録商標)における抗原エピトープを決定するために試験した。末梢血単核細胞(24時間以下、室温で保存)を以下の通り調製して使用した:1単位の全血由来の約30mlの軟膜調製物溶液を50mlのダルベッコリン酸緩衝液(DPBS)に加え、2つの管に分割した。当該サンプルを12.5mlの室温リンフォプレップ(Lymphoprep)密度分離培地(Nycomed;密度1.077g/ml)下に置いた。当該管を600×重力(g)で30分間遠心分離した。2つの相の接合部分を回収、プールし、DPBSで洗浄した。最終的な溶液の細胞密度を当業界に公知の血球計算板により測定した。存続性を当業界に公知のトリパンブルー排除により測定した。
(1)50mlの血清フリーAIM V培地(Gibco/BRL)を1:100希釈β−メルカプトエタノール(Gibco/BRL)を用いて捕捉した。フラスコを2時間、37℃で、5%CO2中に倒して、フラスコ壁に単球を付着させた;
(2)単球細胞の樹状細胞への分化を以下の通り行った:非付着細胞を除去し、得られた付着細胞(単球)を30mlのAIM V、800単位/mlのGM−CSF(Endogen)及び500単位/mlのIL−4(Endogen)と混合し;得られた混合物を5日間、37℃で5%CO2中で培養した。培養の5日後、サイトカインTNFα(Endogen)を0.2単位/mlに加え、及びサイトカインIL−1α(Endogen)を最終濃度50単位/mlに加え、当該混合物を37℃、5%CO2中で、もう2日間培養した。
(3)7日目に、マイトマイシンCを100mM EDTA含有リン酸緩衝生理食塩水(PBS)中、濃度50マイクログラム/mlまで加え、分化中の樹状細胞培養物の成長を止めた。当該溶液を60分間、37℃、5%CO2中で培養した。樹状細胞を穏やかにフラスコを湯出しすることにより、プラスティック表面から除去した。樹状細胞をそれから、5分間、600×gで遠心分離し、DPBSで洗浄し、上述の通り計算した。
(4)調製した樹状細胞を、100マイクロリットル合計体積のAIM V培地中、ウェル当たり2×104細胞/ウェル濃度で96−ウェル丸底プレート内に置いた。
分析システムに用いるALCALASE(登録商標)におけるT細胞エピトープの同定
実施例3に記載の分析に用いるペプチドをALCALASE(登録商標)酵素の完全長アミノ酸配列(配列番号1)に基づいて調製し、ALCALASE(登録商標)の全体配列を含む15マーを合成的に調製した。連続ペプチドは12アミノ酸が重複した。合計88のペプチド(配列番号2〜89)を作成し、その配列を図2に示す。
ペプチド抗原を2mg/mlのDMSO原液として調製した。まず、0.5マイクロリットルの原液を分化樹状細胞を前もって加えた96ウェルプレートの各ウェル中に入れた。そして、上述の通り調製した100マイクロリットルの希釈CD4+T細胞溶液を各ウェルに加えた。有用な対照は希釈DMSOを含まないもの、及び破傷風トキソイド溶性対照を含む。
2×104 CD4+ T細胞
2×105 樹状細胞 (R:Sが10:1)
5μM ペプチド
実施例3
ヒトT細胞を用いるALCALASE(登録商標)酵素におけるペプチドT細胞エピトープを同定する分析
いったん分析試薬(すなわち、細胞、ペプチド等)を調製し、96ウェルプレート中に分配すると、当該分析が行われた。対照は樹状細胞とCD4+ T細胞だけ(DMSOキャリアを含む)を含み、及び約5Lf/mLで破傷風トキソイド(Wyeth−Ayerst,フィラデルフィア、ペンシルベニア州)を含む。
変異体ペプチドの分析
ペプチド番号7及び29はさらなる分析のために選択する。変性ペプチドのセットはペプチド番号7及びペプチド番号29の配列に基づいて構築し、ここでアミノ酸残基は親配列から修飾する。これはMimostopes(サンディエゴ)などの製造供給元により達成できる。アラニンスキャンを各ペプチドについて行う(例えば、Herris,et al.,Immunol.,84:555−561[1995];及び)Maillere et al.,Mol.Immunol.,32:1073−1080[1995]を参照)。当該分析は実施例3に説明の通り行い、ドナーサンプルのセット上の変性ペプチドを利用する。増殖性反応を照合する。
エピトープペプチド番号とHLAの関連
上述の分析試験ラウンドにおける試験ドナー全員のHLA−DR及びDQ発現は市販のPCRベースのHLA割出しキット(Bio−Synthesis)を用いて評価する。いくつかの実施態様において、ペプチド番号に対する反応者と非反応者間の個々のHLA−DR及びDQ抗原の表現型頻度を自由度1でカイ二乗分析を用いて試験する。ペプチド番号に対応するエピトープに対して反応する増加または減少可能性は問題のHLA抗原が反応及び非反応ドナーサンプルの両方に存在し、対応エピトープがHLA関連エピトープであると考えられるときに計算する。
突然変異体ズブチリシンによるジメチルカゼイン(“DMC”)の加水分解
本発明に記載した方法により単離及び精製された、突然変異体ズブチリシンを市販合成基質、ジメチルカゼイン(Sigma C−9801)を加水分解する能力について分析する。5mg/ml DMC基質溶液を適当な緩衝液中で調製する(5mg/ml DMC、0.005%(w/w)Tween 80(登録商標)(ポリオキシエチレン・ソルビタンモノ−オレアート、Sigma P−1754)。適当なDMC基質緩衝液を調製する(例えば、pH5.5の50mM 酢酸ナトリウム;pH6.5の50mM N−tris(ヒドロキシメチル)メチル−2−アミノエタンスルホン酸(“TES”);pH7.5の50mM ピペラジン−N−N’−bis−2−エタンスルホン酸(“PIPES”);及びpH8.5の50mM Tris)。試験を始めるために、200μlの所望のpH基質をマイクロタイタープレート(例えば、96ウェルプレート)のウェル中に入れ、酵素添加前に20分間、37℃で前もって培養する。2,4,6−トリニトロベンゼンスルホン酸塩(“TNBS”)呈色反応法をSpectra Max250分光光度計における活性を測定するために用いる。この分析は遊離アミノ基を含むペプチド内のDMCの酵素的加水分解を測定する。これらのアミノ基は2,4,6−トリニトロ−ベンゼンスルホン酸と反応して黄色複合体を形成する。
吸収405(酵素溶液) − 吸収405(酵素なし)
公知の突然変異体由来ズブチリシン(例えば、特性付けられた変異ズブチリシン)と比較した当該基質を加水分解する突然変異体の能力はこの方法で測定できる。
変異体ズブチリシン・カールスバーグ酵素によるコラーゲン、エラスチン及びケラチンの加水分解
上述の方法により単離及び精製した突然変異体ズブチリシン・カールスバーグ酵素は、例えば、ウシコラーゲン(Sigma C−9879)、ウシエラスチン(Sigma E−1625)及び/またはウシケラチン(ICN Biomedical 902111)などの市販基質を加水分解する能力について分析されることが多い。5mg/mlの基質溶液を調製する(0.005% Tween 80(登録商標)中)。各基質を当業界に公知の適当なpHで調製する(例えば、pH5.5、6.5、7.5及び8.5)。試験のため、1.5mlの各基質を37℃で24ウェルCostarプレート内に移す。プレートは酵素を添加する前に37℃、20分で前もって培養する。上述のTNBS検出分析を37℃で2時間培養した後に上澄みについて行う。
ピペラジン−N−N’−ビス−2−エタンスルホン酸(“PIPES”)緩衝液における変異体タンパク質の熱安定性
これらの実験では、PIPES中のタンパク質(例えば、ズブチリシン・カールスバーグ)変異体の熱安定性について測定する。通常、これらの測定はストラタジーン・ロボサイクラー(Stratagene Robocycler)のタイプのPCRサーモサイクラーを用いて行う。5.0ppm酵素、5.0ppm酵素(例えば、目的変異体及び対照変異酵素)の安定性は5つの時点(例えば、5、10、20、40及び60分)、pH6.5で各温度について試験する。例えば、サンプルは42〜56℃の範囲で2度毎及び42℃〜56℃の温度でその他の各温度で、PCRサーモサイクラー勾配(gradient)において試験する。これらの実験では、50mM PIPES緩衝液を調製する(50mM PIPES、0.005% Tween80(登録商標)。通常、pHは6.5に調節する。しかしながら、本発明は特定の方法に限定されるものではなく、酵素の熱安定性を測定するための種々の方法が当業界に公知である。
N−tris(ヒドロキシメチル)メチル−2−アミノエタンスルホン酸(“TES”)におけるズブチリシン・カールスバーグ変異体の熱安定性
これらの実験では、TES中の変異体の安定性を測定する。上述の通り、5.0ppm酵素(例えば、目的変異体及び対照)を各温度について、pH6.5、5つの時点(例えば、5、10、20、40及び60分)で試験する。例えば、サンプルをPCRサーモサイクラー勾配において、42〜56℃の範囲で2℃毎に試験し、42℃〜56℃の温度でその他の各温度で試験する。TES緩衝液は50mM TES(Sigma T1375)、0.005% Tween80(登録商標)を混合することにより調製する。通常、pHは6.5に調節する。
ボディウォッシュ溶液及びその他のパーソナルケア製品におけるズブチリシン・カールスバーグ変異体の安定性
種々のズブチリシン・カールスバーグ変異体の安定性を以下の手順を用いて測定した。
これらの実験では、ズブチリシン・カールスバーグ及び突然変異体を少なくとも2つの研究において試験し、第1の研究は45℃で30分間試験し、第2の研究は50℃で30分間試験する。これらの試験に関して、50/50(w/w)ボディウォッシュ溶液を市販のボディウォッシュ(例えば、商標名ZEST(登録商標)でプロクター&ギャンブルから市販のボディウォッシュ)と脱イオン水を混合することにより調製する。緩衝液ブレンドのpHは約6.8である。
洗浄組成物
上述の組成物に加え、本発明は特定の性質を有する洗浄組成物を開発する手段を提供する。実際に、本発明は修飾プロテアーゼ(例えば、ズブチリシン・カールスバーグ)を含む種々の洗浄組成物を提供する。特に好ましい実施態様において、効果的な量の1以上の上述のプロテアーゼ酵素はタンパク性のシミ除去が必要な種々の表面を洗浄するのに有用な組成物に含まれる。当該洗浄組成物は硬い表面を洗浄する洗剤組成物、繊維を洗浄する洗剤組成物;食器洗剤組成物;口内洗浄組成物;及び入れ歯洗浄用組成物を含む。これらの組成物は特定の使用目的に適した形態で提供される。好ましくは、本発明の洗浄組成物は約0.0001%〜約10%の1以上、より好ましくは約0.001%〜約1%、及びさらに好ましくは約0.001%〜約0.1%のプロテアーゼ酵素を含む。プロテアーゼ酵素が使用できる種々の洗浄組成物のいくつかの例としては下記にさらに詳細に説明する。ここで使用する全ての割合、比率、及び比は別に定めない限り重量によるものとする。
本発明のプロテアーゼ酵素(例えば、変異体ズブチリシン・カールスバーグ酵素)は高い泡立ち及び/または不溶性基質の優れた除去が望まれる洗剤組成物において使用できる。従って、本発明のプロテアーゼ酵素は硬い表面用洗浄剤、食器洗い用組成物、織物洗浄組成物等の十分な処方を提供するために種々の従来の成分を用いて使用できる。これらの組成物は特定用途に許容される形態(例えば、液体、顆粒、バー等)での使用に適している。さらに、これらの組成物は界面活性剤の30重量%〜60重量%程度を含む市販の“濃縮”洗剤での使用にも適している。
好ましい実施態様において、本発明の硬い表面用洗浄組成物は効果的な量の1以上のプロテアーゼ酵素(例えば、変異体ズブチリシン・カールスバーグ酵素)を含み、好ましくは組成物の約0.0001重量%〜約10重量%、より好ましくは約0.001重量%〜約5重量%、さらにより好ましくは約0.001重量%〜約1重量%の活性プロテアーゼ酵素を含む。1以上のプロテアーゼ酵素を含むことに加え、当該硬い表面用洗浄組成物は通常、界面活性剤及び水溶性金属イオン封鎖ビルダーを含む。しかしながら、スプレー窓拭き用洗剤などのある特殊化製品において、界面活性剤は、ガラス表面上に薄膜/縞むらを生じ得るので使用しない場合もある。
本発明の別の実施態様において、1以上のプロテアーゼ酵素(例えば、変異ズブチリシン・カールスバーグ酵素)を含む食器洗い用組成物を提供する。本発明の好ましい食器洗い用組成物の実施態様を以下に示す。プロテアーゼは0.5、0.4、0.1、0.05、0.03及び0.02パーセントで含まれる。これらの組成物では、製品pHは7に調節する。
本発明はさらに、1以上のプロテアーゼ酵素(例えば、変異体ズブチリシン・カールスバーグ酵素)を含む織物洗浄組成物を提供する。
本発明の顆粒織物洗浄組成物は効果的な量の1以上のプロテアーゼ酵素(例えば、変異体ズブチリシン・カールスバーグ酵素)を含み、好ましくは組成物の約0.001重量%〜約10重量%、より好ましくは約0.005重量%〜約5重量%、より好ましくは約0.01重量%〜約1重量%の活性プロテアーゼ酵素を含む。1以上のプロテアーゼ酵素に加えて、顆粒織物洗浄組成物は通常、少なくとも1の界面活性剤、1以上のビルダー及び場合によっては、漂白剤を含む。本発明の顆粒織物洗浄組成物の実施態様は以下の実施例により説明する。
本発明の液体織物洗浄組成物は効果的な量の1以上プロテアーゼ酵素(例えば、変異体ズブチリシン・カールスバーグ酵素)を含み、好ましくは組成物の約0.0001重量%〜約10重量%、より好ましくは約0.001重量%〜約1重量%、及び最も好ましくは約0.001重量%〜約0.1重量%を含む。当該液体織物洗浄組成物は通常、さらに陰イオン性界面活性剤、脂肪酸、水溶性洗剤ビルダー及び水を含む。本発明の液体織物洗浄組成物の実施態様は以下の例により説明する。
本発明のバー状織物洗浄組成物は汚れた織物を手洗いするのに適しており、効果的な量の1以上プロテアーゼ酵素(例えば、変異体ズブチリシン・カールスバーグ酵素)を含み、好ましくは組成物の約0.001重量%〜約10重量%、より好ましくは約0.01重量%〜約1重量%を含む。本発明のバー状織物洗浄組成物の実施態様は以下の例により説明する。
上述の硬い表面用洗浄、食器洗い用及び織物洗浄組成物に加え、1以上のプロテアーゼ酵素(例えば、変異体ズブチリシン・カールスバーグ酵素)は不溶性基質を加水分解することが望ましい種々のその他の洗浄組成物の成分として使用できる。当該他の洗浄組成物は、限定されないが、口内洗浄組成物、入れ歯洗浄組成物、及びコンタクトレンズ洗浄組成物、並びにその他のパーソナルケア洗浄組成物を含む。
本発明の他の実施態様において、薬学的に許容できる量の1以上のプロテアーゼ酵素(変異体ズブチリシン・カールスバーグ酵素)は歯または入れ歯からタンパク性のシミを除去するのに有用な組成物に含まれる。好ましくは、本発明の口内洗浄組成物は組成物の約0.0001重量%〜約20重量%の1以上のプロテアーゼ酵素、より好ましくは約0.001重量%〜約10重量%、さらにより好ましくは約0.01重量%〜約5重量%及び薬学的に許容できるキャリアを含む。通常、口内洗浄組成物の口内洗浄成分の薬学的に許容できる口内洗浄キャリア成分は組成物の約50重量%〜約99.99重量%、好ましくは約65重量%〜約99.99重量%、より好ましくは約65重量%〜約99重量%を含む。
さらに別の実施態様において、本発明は1以上のプロテアーゼ酵素(例えば、変異体ズブチリシン・カールスバーグ酵素)を含む口腔の外側の入れ歯を洗浄するための種々の入れ歯組成物を提供する。当該入れ歯洗浄組成物は効果的な量で1以上のプロテアーゼ酵素(例えば、変異体ズブチリシン・カールスバーグ酵素)を含み、好ましくは組成物の約0.0001重量%〜約50重量%の1以上のプロテアーゼ酵素、より好ましくは約0.001重量%〜約35重量%、さらにより好ましくは約0.01重量%〜約20重量%及び入れ歯洗浄キャリアを含む。発泡錠など種々の入れ歯洗浄組成物形態は当業界に公知であり(例えば、ここに引用する米国特許第5,055,305号を参照)、通常は1以上のプロテアーゼ酵素を入れ歯からタンパク性シミを除去するために含めるのが好ましい。本発明の入れ歯洗浄組成物の実施態様は以下の例により説明する。
本発明の別の実施態様において、肌を洗浄するためのパーソナル洗浄組成物は1以上のプロテアーゼ酵素(例えば、変異体ズブチリシン・カールスバーグ酵素)を含む。当該組成物は通常、組成物の約0.001重量%〜約5重量%プロテアーゼ酵素(例えば、変異体ズブチリシン・カールスバーグ酵素)を含み、好ましくは約0.005重量%〜約2重量%、及び最も好ましくは約0.1重量%〜約0.8重量%を含む。ここに記載のプロテアーゼ酵素を含むことができる好ましいパーソナル洗浄組成物は限定されないが、米国特許出願第08/121,623号及び第08/121,624号に記載のものを含む。種々の組成物が本発明で考えられるが、石けん成分を含む1の液体パーソナル洗浄組成物は以下を含む(重量%):石けん(KまたはNa)(15.00)、30%ラウレート、30%ミリステート、25%パルミテート、15%ステアレート、脂肪酸(上述の比)(4.50)、Naラウリルサルコシネート(6.00)、ナトリウムラウレス−3硫酸(0.66)、コカミドプロピルベタイン(1.33)、グリセリン(15.00)、プロピレングリコール(9.00)、ポリクオタニウム10(0.80)、エチレングリコールジステアレート(EDTA)(1.50),プロピルパラベン(0.10)、メチルパラベン(0.20)、プロテアーゼ#(0.10)、KOHまたはNaOH(pHを調節する必要がある場合)、硫酸カルシウム(3)、酢酸(3)及び水(100に調整)。
洗浄性能試験
本発明組成物で有用な変異体の洗浄性能を当業界に公知の適当な手段により評価できる。EMPA116(綿上の血液/ミルク/カーボンブラック)布見本(Testfabrics,Inc.,Middlesex,N.J.07030)からのシミ除去を測定する1の適当な方法をこの実施例で説明する。
液体洗剤製剤中の変異体ズブチリシン・カールスバーグ安定性
この実施例は液体洗剤製剤中での不活性化に対するプロテアーゼ(例えば、変異体ズブチリシン・カールスバーグ酵素)安定性をバチルス・アミロリケファシエンスズブチリシン及びその変異体酵素と比較する方法を提供する。他の方法が本発明で使用できるので、本発明はこの方法に限定されるものではない。
Claims (21)
- 細菌性ズブチリシンの少なくとも1のT細胞エピトープを同定する方法であって、前記ズブチリシンはズブチリシン・カールスバーグを含み、以下の工程を含む:
(i)1のヒト血液源から樹状細胞溶液及びナイーブCD4+及び/またはCD8+T細胞溶液を得る工程;
(ii)前記樹状細胞を分化して、分化樹状細胞溶液を生成する工程;
(iii)分化樹状細胞及び前期ズブチリシン・カールスバーグのペプチド断片を有する前記ナイーブCD4+及び/またはCD8+T細胞溶を混合する工程;及び
(iv)工程(iii)の前記T細胞の増殖を測定する工程。 - 前記細菌性ズブチリシン・カールスバーグがバチルス属のメンバーから得られる、請求項1の方法。
- バチルスがB.ズブチリス、B.リケニホルミス、B.レンタス、B.ブレビス、B.ステロサーモフィラス、B.アルカロフィラス(alkalophilus)、B.アミロリケファシエンス、B.clausii、B.ハロデュランス、B.メガテリウム、B.コアグランス、B.サーキュランス、B.レンタス及びB.チューリンゲンシスからなる群より選択される、請求項2の方法。
- 前記細菌性バチルス・カールスバーグが配列番号1に示す配列の少なくとも一部を含む、請求項1の方法。
- 細菌性ズブチリシン・カールスバーグの免疫原性を減少させる方法であって、以下の工程を含む:
(a)以下の方法により前記タンパク質中の少なくとも1のT細胞エピトープを同定する工程(i)in vitroで少なくとも1のサイトカインに曝露することにより分化された接着性単球由来樹状細胞と前記T細胞エピトープを含む少なくとも1のペプチドを接触させる、及び(ii)前記樹状細胞及び前期ペプチドとナイーブT細胞を接触させ、ここで、前記ナイーブT細胞は前記接着性単球由来樹状細胞と同じ供給源から得たものであり、それにより前記T細胞増殖は前記ペプチドに反応する;及び
(b)前記T細胞エピトープを中性化するために前記ズブチリシン・カールスバーグを修飾し、変異体タンパク質を生成する工程であって、前記変異体タンパク質が前記ナイーブT細胞より少ないまたは実質的に等しい基準増殖を誘発するようにする工程。 - 前記細菌性ズブチリシンがバチルス属のメンバー由来である、請求項5の方法。
- バチルスがB.ズブチリス、B.リケニホルミス、B.レンタス、B.ブレビス、B.ステロサーモフィラス、B.アルカロフィラス(alkalophilus)、B.アミロリケファシエンス、B.clausii、B.ハロデュランス、B.メガテリウム、B.コアグランス、B.サーキュランス、B.レンタス及びB.チューリンゲンシスからなる群より選択される、請求項6の方法。
- 前記細菌性ズブチリシン・カールスバーグが配列番号1に示される配列の少なくとも一部を含む、請求項5の方法。
- (a)前記T細胞エピトープのアミノ酸配列を前記細菌性ズブチリシンの相同体由来の類似配列で置換し、前記置換がT細胞エピトープの主要な3次構造属性を擬態するようにすることにより前記細菌性ズブチリシン・カールスバーグの前記エピトープを修飾する、請求項5の方法。
- 前記細菌性ズブチリシン・カールスバーグが、配列番号2、配列番号90、配列番号15、配列番号30、及び配列番号40からなる群より選択される少なくとも1のエピトープを改変することにより修飾される、請求項5の方法。
- 前記エピトープが少なくとも1の前記エピトープに対応する残基のアミノ酸配列を置換することにより修飾される、請求項10の方法。
- 前記エピトープが少なくとも1の前記エピトープに対応する残基のアミノ酸配列を欠失することにより修飾される、請求項10の方法。
- 前記エピトープが少なくとも1の前記エピトープにアミノ酸を付加することにより修飾される、請求項10の方法。
- 修飾ズブチリシン・カールスバーグ酵素であって、前記ズブチリシン・カールスバーグは配列番号2、配列番号90、配列番号15、配列番号30、及び配列番号40からなる群より選択されたアミノ酸配列を含む少なくとも1のエピトープにおいて少なくとも1の変異を含む。
- 前記修飾ズブチリシン・カールスバーグがバチルス属の生物内で発現する、請求項14の修飾ズブチリシン・カールスバーグ。
- 前記修飾ズブチリシン・カールスバーグにより生じる免疫反応が野生型修飾ズブチリシン・カールスバーグにより生じる前期免疫反応より少ない、請求項14の修飾ズブチリシン・カールスバーグ。
- 前記修飾ズブチリシン・カールスバーグにより生じる免疫反応が野生型修飾ズブチリシン・カールスバーグにより生じる前期免疫反応より大きい、請求項14の修飾ズブチリシン・カールスバーグ。
- 請求項14の前記修飾ズブチリシン・カールスバーグをエンコードする核酸を含む組成物。
- 請求項18の核酸を含む発現ベクター。
- 請求項19の発現ベクターを用いて形質転換した宿主細胞。
- 洗浄組成物、パーソナルケア組成物及びヘルスケア組成物からなる群より選択される組成物であって、請求項14の修飾ズブチリシン・カールスバーグを含む組成物。
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JP2018527882A (ja) * | 2015-05-30 | 2018-09-27 | モレキュラー テンプレーツ, インク.Molecular Templates, Inc. | 脱免疫化された志賀毒素aサブユニット足場及びそれを含む細胞標的化分子 |
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US11365223B2 (en) | 2015-05-30 | 2022-06-21 | Molecular Templates, Inc. | De-immunized, Shiga toxin a subunit scaffolds and cell-targeting molecules comprising the same |
JP7228931B2 (ja) | 2015-05-30 | 2023-02-27 | モレキュラー テンプレーツ,インク. | 脱免疫化された志賀毒素aサブユニット足場及びそれを含む細胞標的化分子 |
US11389542B1 (en) | 2016-12-07 | 2022-07-19 | Molecular Templates, Inc. | Shiga toxin a subunit effector polypeptides, Shiga toxin effector scaffolds, and cell-targeting molecules for site-specific conjugation |
US11857628B2 (en) | 2016-12-07 | 2024-01-02 | Molecular Templates, Inc. | Shiga toxin A subunit effector polypeptides, Shiga toxin effector scaffolds, and cell-targeting molecules for site-specific conjugation |
US11406692B2 (en) | 2017-01-25 | 2022-08-09 | Molecular Templates, Inc. | Cell-targeting molecules comprising de-immunized, Shiga toxin a subunit effectors and CD8+ t-cell epitopes |
Also Published As
Publication number | Publication date |
---|---|
US20090162917A1 (en) | 2009-06-25 |
WO2003072746A3 (en) | 2005-03-24 |
EP1530637A2 (en) | 2005-05-18 |
ATE457352T1 (de) | 2010-02-15 |
WO2003072746A2 (en) | 2003-09-04 |
CA2476890C (en) | 2013-07-16 |
AU2003213580A1 (en) | 2003-09-09 |
EP1530637A4 (en) | 2007-03-21 |
US20050239043A1 (en) | 2005-10-27 |
CA2476890A1 (en) | 2003-09-04 |
JP4597528B2 (ja) | 2010-12-15 |
DK1530637T3 (da) | 2010-05-31 |
DE60331224D1 (de) | 2010-03-25 |
AU2003213580A8 (en) | 2003-09-09 |
MXPA04008144A (es) | 2004-11-26 |
EP1530637B1 (en) | 2010-02-10 |
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