JPH09503396A - 診断用及び治療用の精製c型肝炎ウイルスエンベロープ蛋白 - Google Patents
診断用及び治療用の精製c型肝炎ウイルスエンベロープ蛋白Info
- Publication number
- JPH09503396A JPH09503396A JP8506189A JP50618996A JPH09503396A JP H09503396 A JPH09503396 A JP H09503396A JP 8506189 A JP8506189 A JP 8506189A JP 50618996 A JP50618996 A JP 50618996A JP H09503396 A JPH09503396 A JP H09503396A
- Authority
- JP
- Japan
- Prior art keywords
- hcv
- protein
- region
- recombinant
- epitope
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Withdrawn
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Abstract
Description
Claims (1)
- 【特許請求の範囲】 1.形質転換宿主細胞を溶解して組換えにより発現された蛋白を単離する際に、 ジスルフィド結合切断剤によりジスルフィド結合切断又は還元工程を行うことを 特徴とする、E1及び/又はE2及び/又はE1/E2よりなる群から選択され る組換えHCVの単一の又は特定オリゴマーのエンベロープ蛋白を精製する方法 。 2.ジスルフィド結合切断又は還元工程を、部分的切断又は還元条件下で行う、 請求の範囲第1項記載の方法。 3.ジスルフィド結合切断剤が、好適には0.1〜50mM、好適には0.1〜2 0mM、更に好適には0.5〜10mMの範囲の濃度の、ジチオスレイトール(DT T)である、請求の範囲第1項又は第2項記載の方法。 4.ジスルフィド結合切断剤が、界面活性剤である、請求の範囲第1項記載の方 法。 5.界面活性剤が、好適には1〜10%の濃度、更に好適には3.5%の濃度の 、エンピゲン−BB(Empigen-BB)である、請求の範囲第4項記載の方法。 6.ジスルフィド結合切断剤が、DTTのような古典的ジスルフィド結合切断剤 と、エンピゲン−BBのような界面活性剤との組合せを含む、請求の範囲第1項 又は第2項記載の方法。 7.SH基保護剤によりジスルフィド結合の再形成を阻止する工程を更に含む、 請求の範囲第1項〜第6項のいずれか1項記載の方法。 8.SH基保護剤が、N−エチルマレイミド(NEM)又はその誘導体である、 請求の範囲第7項記載の方法。 9.ジスルフィド結合の再形成を阻止する工程を、低pH条件により達成 する、請求の範囲第7項記載の方法。 10.少なくとも以下の工程: − 組換えE1及び/又はE2及び/又はE1/E2発現宿主細胞を、場合によ りN−エチルマレイミド(NEM)のようなSH基保護剤の存在下で、溶解し、 − レンチルレクチンクロマトグラフィーのようなレクチンクロマトグラフィー 、あるいは抗E1及び/又は抗E2特異的モノクローナル抗体を用いる免疫親和 性などの親和性精製により、上記HCVエンベロープ蛋白を回収し、 − DTTのようなジスルフィド結合切断剤を用いて、好適にはNEM又はビオ チン−NEMのようなSH基保護剤の存在下で、ジスルフィド結合を還元又は切 断して、そして − 還元されたE1及び/又はE2及び/又はE1/E2エンベロープ蛋白を、 ゲル濾過、及び場合によりこれに続くNi2+−IMACクロマトグラフィーと脱 塩工程により回収する工程、 により更に特徴づけられる、請求の範囲第1項〜第9項のいずれか1項記載の方 法。 11.請求の範囲第1項〜第10項のいずれか1項記載の方法により単離される ことを特徴とする、E1及び/又はE2及び/又はE1/E2よりなる群から選 択される実質的に精製された組換えHCVの単一の又は特定オリゴマーの組換え エンベロープ蛋白を含む組成物。 12.更に、組換えHCVエンベロープ蛋白が、ワクシニアのような組換え哺乳 動物細胞から発現されることを特徴とする、請求の範囲第11項記載の組成物。 13.更に、組換えHCVエンベロープ蛋白が、組換え酵母細胞から発現 されることを特徴とする、請求の範囲第11項記載の組成物。 14.更に、組換えHCVエンベロープ蛋白が、請求の範囲第15項〜第24項 のいずれか1項記載の少なくとも1つの組換えベクターの発現生成物であること を特徴とする、請求の範囲第11項記載の組成物。 15.ベクター配列、適切な原核生物性、真核生物性又はウイルス性プロモータ ー配列及びその後に続く単一の又は特定オリゴマーのE1及び/又はE2及び/ 又はE1/E2蛋白の発現を可能にするヌクレオチド配列を含む組換えベクター 。 16.ヌクレオチド配列が、更に、アミノ酸1位と192位の間の領域で開始し 、アミノ酸250位と400位の間の領域で終わるか、より好適には250位と 341位の間の領域で終わるか、更により好適には290位と341位の間の領 域で終わる単一のHCVのE1蛋白をコードすることを特徴とする、請求の範囲 第15項記載の組換えベクター。 17.ヌクレオチド配列が、更に、アミノ酸117位と192位の間の領域で開 始し、アミノ酸263位と400位の間の領域で終わるか、より好適には250 位と326位の間の領域で終わる単一のHCVのE1蛋白をコードすることを特 徴とする、請求の範囲第16項記載の組換えベクター。 18.ヌクレオチド配列が、更に、264〜293位プラスマイナス8アミノ酸 の間の最初の疎水性ドメインが欠失している単一のHCVのE1蛋白をコードす ることを特徴とする、請求の範囲第16項又は第17項記載の組換えベクター。 19.ヌクレオチド配列が、更に、アミノ酸290位と406位の間の領域で開 始し、アミノ酸600位と820位の間の領域で終わるか、より好適には322 位と406位の間の領域で開始するか、更により好適には 347位と406位の間の領域で開始するか、そして最も好適には364位と4 06位の間の領域で開始する単一のHCVのE2蛋白をコードすることを特徴と する、請求の範囲第15項記載の組換えベクター。 20.ヌクレオチド配列が、更に、アミノ酸623、650、661、673、 710、715、720、746又は809位のいずれかの位置で終わることを 特徴とする、請求の範囲第19項記載の組換えベクター。 21.ヌクレオチド配列が、更に、それに5’末端ATGコドン及び3’末端停 止コドンを加えられていることを特徴とする、請求の範囲第16項〜第20項の いずれか1項記載の組換えベクター。 22.ヌクレオチド配列が、更に、コード領域の3’末端に第Xa因子切断部位 及び/又は3〜10個、好適には6個のヒスチジンコドンを加えられていること を特徴とする、請求の範囲第16項〜第21項のいずれか1項記載の組換えベク ター。 23.配列番号3、5、7、9、11、13、21、23、25、27、29、 31、35、37、39、41、43、45、47及び49に示されるいずれか の配列又はこれらの部分を含む核酸。 24.請求の範囲第23項記載の組換え核酸を有する組換えベクター。 25.更に、上記E1又はE2蛋白に存在する少なくとも1つのグリコシル化部 位が、核酸レベルで除去されていることを特徴とする、請求の範囲第15項〜第 24項のいずれか1項記載の組換えベクター。 26.ベクターが、宿主細胞中で機能することが可能、かつHCVのE1及び/ 又はE2及び/又はE1/E2蛋白の発現を制御することが可能な制御配列に加 えて、請求の範囲第15項〜第23項のいずれか1項記載のHCVのE1及び/ 又はE2及び/又はE1/E2蛋白をコードするヌク レオチド配列を含む、請求の範囲第15項〜第25項のいずれか1項記載の少な くとも1つの組換えベクターで形質転換された宿主細胞。 27.請求の範囲第26項記載の宿主細胞により発現された組換えE1及び/又 はE2及び/又はE1/E2蛋白。 28.少なくとも以下の工程: − 請求の範囲第15項〜第25項のいずれか1項記載の組換えベクターで形質 転換された請求の範囲第26項記載の宿主細胞を、適切な培地中で増殖させ、 − 適切な条件下で請求の範囲第16項〜第25項のいずれか1項記載のベクタ ー配列を発現させ、そして − 好適にはN−エチルマレイミド(NEM)のようなSH基保護剤の存在下で 、上記形質転換細胞を溶解し、 − 例えばレクチンクロマトグラフィーあるいは抗E1及び/又は抗E2特異的 モノクローナル抗体を用いる免疫親和性クロマトグラフィーのような親和性精製 (上記レクチンは好適にはレンチルレクチンである)により、上記HCVエンベ ロープ蛋白を回収し、次に − 前工程の溶出液を、DTTのようなジスルフィド結合切断剤と、好適にはN EM又はビオチン−NEMのようなSH基保護剤の存在下で、インキュベートし て、そして − ゲル濾過、及び場合により更にNi2+−IMACクロマトグラフィーと脱塩 工程により、HCVの単一の又は特定オリゴマーのE1及び/又はE2及び/又 はE1/E2蛋白を単離する工程、 を含むことを更に特徴とする、請求の範囲第1項〜第10項のいずれか1項記載 の方法。 29.少なくとも1つの下記のE1及び/又はE2ペプチド: コア/E1V1領域のアミノ酸181〜200位にわたるE1−31(配列 番号56)、 E1領域のアミノ酸193〜212位にわたるE1−33(配列番号57) 、 E1V2領域のアミノ酸205〜224位にわたるE1−35(配列番号5 8)(エピトープB)、 E1V2領域のアミノ酸208〜227位にわたるE1−35A(配列番号 59)(エピトープB)、 E1領域〔V1、C1及びV2領域(エピトープBを含有する)〕のアミノ 酸192〜228位にわたる1bE1(配列番号53)、 E1領域のアミノ酸301〜320位にわたるE1−51(配列番号66) 、 E1C4領域のアミノ酸313〜332位にわたるE1−53(配列番号6 7)(エピトープA)、 E1領域のアミノ酸325〜344位にわたるE1−55(配列番号68) 、 E2領域のアミノ酸397〜416位にわたるEnv67即ちE2−67( 配列番号72)(エピトープA)、 E2領域のアミノ酸409〜428位にわたるEnv69即ちE2−69( 配列番号73)(エピトープA)、 E2領域の583〜602位にわたるEnv23即ちE2−23(配列番号 86)(エピトープE)、 E2領域の595〜614位にわたるEnv25即ちE2−25(配列番号 87)(エピトープE)、 E2領域の607〜626位にわたるEnv27即ちE2−27(配 列番号88) (エピトープE)、 E2領域の547〜566位にわたるEnv17B即ちE2−17B(配列 番号83)(エピトープD)、 E2領域の523〜542位にわたるEnv13B即ちE2−13B(配列 番号82)(エピトープC)、 を含む組成物。 30.少なくとも1つの下記のコンフォメーション性エピトープ: モノクローナル抗体15C8C1、12D11F1、及び8G10D1H9 により認識されるエピトープF、 モノクローナル抗体9G3E6により認識されるエピトープG、 モノクローナル抗体10D3C4及び4H6B2により認識されるエピトー プH(又はC)、 モノクローナル抗体17F2C2により認識されるエピトープI、 を含む組成物。 31.請求の範囲第11項〜第14項又は第29項〜第30項のいずれか1項記 載の組成物で免疫して作成されるE1及び/又はE2特異的モノクローナル抗体 。 32.薬剤としての使用のための、更に詳しくはHCVのE1又はE2抗原の存 在の検出のための免疫測定用キットに組み込むため、疾患の予知/監視のため、 又はHCV治療のための、請求の範囲第31項記載のE1及び/又はE2特異的 モノクローナル抗体。 33.HCVのE1又はE2抗原の検出のための免疫測定用キットの調製のため の、HCV疾患の予知/監視のためのキットの調製のための、又はHCV薬剤の 調製のための、請求の範囲第31項記載のE1及び/又はE2特異的モノクロー ナル抗体の用途。 34.少なくとも下記の工程: (i)免疫複合体の形成を可能にする適切な条件下で、好適には固定化された形 で、請求の範囲第31項記載のE1及び/又はE2特異的モノクローナル抗体に 、生物学的試料を接触させ、 (ii)結合しなかった成分を除去し、 (iii) 形成された免疫複合体を、適切な条件下で検出可能な標識物に結合されて いる異種抗体とインキュベートし、 (iv)該免疫複合体の存在を視覚的又は機械的に検出する工程 を含む、生物学的試料中に存在するHCV抗原のインビトロ診断の方法。 35.以下のもの: − 好適には固体基材上に固定された形の、請求の範囲第31項記載の少なくと も1つのE1及び/又はE2特異的モノクローナル抗体、 − これらの抗体と、生物学的試料中に存在するHCV抗原との間の結合反応を 可能にする緩衝液又は前記緩衝液を生成するのに必要な成分、 − 前述の結合反応で形成された免疫複合体を検出する手段、 を含む、生物学的試料中に存在するHCV抗原の存在を測定するためのキット。 36.薬剤として使用するための、請求の範囲第11項〜第14項又は第29項 〜第30項のいずれか1項記載の組成物。 37.免疫応答を起こすために、場合により薬剤学的に許容しうる助剤と一緒に して、請求の範囲第11項〜第14項又は第29項〜第30項のいずれか1項記 載の有効量の組成物を投与することを特徴とする、HCVに対する哺乳動物(好 適にはヒト)の免疫のためのワクチンとして使用する ための、前記組成物。 38.免疫応答を起こすために、場合により薬剤学的に許容しうる助剤と一緒に して、請求の範囲第11項〜第14項又は第29項〜第30項のいずれか1項記 載の有効量の組成物を投与することを特徴とする、HCVに対する哺乳動物(好 適にはヒト)の免疫のためのワクチンを調製するための、前記組成物の用途。 39.場合により薬剤学的に許容しうる助剤と一緒にした、請求の範囲第11項 〜第14項又は第29項〜第30項のいずれか1項記載の有効量の組成物を含む 、HCVに対して哺乳動物(好適にはヒト)を免疫するためのワクチン組成物。 40.生物学的試料中に存在するHCV抗体のインビトロ検出のための、請求の 範囲第11項〜第14項又は第29項〜第30項のいずれか1項記載の組成物。 41.生物学的試料中に存在するHCV抗体の検出のための免疫測定用キットの 調製のための、請求の範囲第11項〜第14項又は第29項〜第30項のいずれ か1項記載の組成物の用途。 42.少なくとも以下の工程: (i)免疫複合体の形成を可能にする適切な条件下で、好適には固定化された形 で、請求の範囲第11項〜第14項又は第29項〜第30項のいずれか1項記載 の組成物に、生物学的試料を接触させ、 (ii)結合しなかった成分を除去し、 (iii) 形成された免疫複合体を、適切な条件下で検出可能な標識物に結合されて いる異種抗体とインキュベートし、 (iv)該免疫複合体の存在を視覚的又は機械的に検出する工程、 を含む、生物学的試料中に存在するHCV抗体のインビトロ診断の 方法。 43.以下のもの: − 好適には固体基材上に固定された形の、請求の範囲第11項〜第14項又は 第29項〜第30項のいずれか1項記載の少なくとも1つのペプチド又は蛋白組 成物、 − これらの蛋白又はペプチドと、生物学的試料中に存在するHCVに対する抗 体との間の結合反応を可能にする緩衝液又は前記緩衝液を生成するのに必要な成 分、 − 前述の結合反応で形成された免疫複合体を検出する手段、 を含む、生物学的試料中に存在するHCV抗体の存在を測定するためのキット。 44.以下の工程: − HCV感染患者からの生物学的試料を、E1蛋白又はその好適な部分と、免 疫学的複合体の形成を可能にする条件下でインキュベートし、 − 結合しなかった成分を除去し、 − 治療の開始時及び治療中の上記試料中の抗E1力価を計算し、 − 治療の開始時及び/又は治療中の上記試料中の抗E1力価に基づき、HCV 疾患の自然の経過を監視するか、又は上記患者の治療に対する応答を予知する工 程、 を含む、HCV感染に罹っている患者のHCV疾患のインビトロ監視、又は、特 にインターフェロンによる、治療に対する応答を予知するための、請求の範囲第 11項〜第14項のいずれか1項記載のE1蛋白又は請求の範囲第29項記載の その部分、更に詳しくはHCVの単一のE1蛋白又はE1ペプチドを含む組成物 の用途。 45.以下のもの: − 少なくとも1つのE1蛋白又はE1ペプチド、更に詳しくは請求の範囲第1 1項〜第14項又は第29項のいずれか1項記載のE1蛋白又はE1ペプチド、 − これらの蛋白又はペプチドと、生物学的試料中に存在する抗E1抗体との間 の結合反応を可能にする緩衝液又は前記緩衝液を生成するのに必要な成分、 − 前述の結合反応で形成された免疫複合体を検出する手段、 − 場合により治療の進行中の抗E1力価の低下を推定するための自動走査及び 解釈装置、 を含む、HCV感染に罹っている患者のHCV疾患の監視、又は、特にインター フェロンによる、治療に対する応答を予知するためのキット。 46.少なくとも以下の工程: (i)免疫複合体の形成を可能にする適切な条件下で、好適には固定化された形 で、請求の範囲第11項〜第14項のいずれか1項記載の少なくとも1つのE1 及び/又はE2及び/又はE1/E2蛋白組成物、あるいは請求の範囲第29項 記載の少なくとも1つのE1又はE2ペプチド組成物に、1つ又はそれ以上の血 清型のHCV抗体の存在について分析すべき生物学的試料を接触させ、 (ii)結合しなかった成分を除去し、 (iii) 形成された免疫複合体を、適切な条件下で検出可能な標識物に結合されて いる異種抗体とインキュベートし、 (iv)該免疫複合体の存在を視覚的又は機械的に(例えば、デンシトメーター、 蛍光測定、比色法により)検出し、観察された結合パターンから1つ又はそれ以 上のHCV血清型の存在を推定する工程、 を含む、生物学的試料中に存在するHCVの1つまたはそれ以上の血清型を検出 するための、更に詳しくは検出すべきHCVの異なる型の抗体を検出するための 、1つの測定フォーマットに組合せた血清型測定法。 47.以下のもの: − 請求の範囲第11項〜第14項のいずれか1項記載の少なくとも1つのE1 及び/又はE2及び/又はE1/E2蛋白、あるいは請求の範囲第29項記載の E1又はE2ペプチド、 − これらの蛋白又はペプチドと、生物学的試料中に存在する抗E1抗体との間 の結合反応を可能にする緩衝液又は前記緩衝液を生成するのに必要な成分、 − 前述の結合反応で形成された免疫複合体を検出する手段、 − 場合により、観察された結合パターンから1つ又はそれ以上の血清型の存在 を検出するための自動走査及び解釈装置、 を含む、生物学的試料中に存在するHCVの1つ又はそれ以上の血清型を分類す る(serotyping)ための、更に詳しくはHCVのこれらの血清型に対する抗体を 検出するためのキット。 48.請求の範囲第42項〜第46項のいずれか1項記載の方法によりHCVの 有無又は遺伝子型を決定するために、固体基材上に固定化するための、及び逆相 ハイブリダイゼーション測定法に取り込むための、好適には膜ストリップのよう な固体支持体上に平行線状に固定化するための、請求の範囲第11項〜第14項 又は第29項のいずれか1項記載のペプチド又は蛋白組成物。
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1995
- 1995-07-31 EP EP02003643A patent/EP1211315A1/en not_active Withdrawn
- 1995-07-31 DK DK95930434T patent/DK0721505T4/da active
- 1995-07-31 ES ES95930434T patent/ES2174957T5/es not_active Expired - Lifetime
- 1995-07-31 DE DE69526636T patent/DE69526636T3/de not_active Expired - Lifetime
- 1995-07-31 DE DE69526636A patent/DE69526636D1/de not_active Expired - Fee Related
- 1995-07-31 SG SG1997003877A patent/SG71728A1/en unknown
- 1995-07-31 EP EP07109345A patent/EP1845108A3/en not_active Withdrawn
- 1995-07-31 CA CA002172273A patent/CA2172273A1/en not_active Abandoned
- 1995-07-31 EP EP95930434A patent/EP0721505B2/en not_active Expired - Lifetime
- 1995-07-31 US US08/612,973 patent/US6150134A/en not_active Expired - Fee Related
- 1995-07-31 AT AT95930434T patent/ATE217345T1/de not_active IP Right Cessation
- 1995-07-31 WO PCT/EP1995/003031 patent/WO1996004385A2/en active IP Right Grant
- 1995-07-31 BR BR9506059A patent/BR9506059A/pt not_active IP Right Cessation
- 1995-07-31 JP JP8506189A patent/JPH09503396A/ja not_active Withdrawn
- 1995-07-31 PT PT95930434T patent/PT721505E/pt unknown
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1997
- 1997-09-11 US US08/927,597 patent/US6245503B1/en not_active Expired - Fee Related
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2001
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- 2001-10-10 US US09/973,025 patent/US7026457B2/en not_active Expired - Fee Related
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2002
- 2002-12-05 HK HK02108883.1A patent/HK1049022A1/zh unknown
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2004
- 2004-02-26 JP JP2004051709A patent/JP3892443B2/ja not_active Expired - Fee Related
-
2006
- 2006-10-10 JP JP2006276281A patent/JP4105203B2/ja not_active Expired - Fee Related
-
2007
- 2007-01-18 US US11/654,514 patent/US20070128721A1/en not_active Abandoned
- 2007-02-23 US US11/678,513 patent/US20080138894A1/en not_active Abandoned
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JP2014064594A (ja) * | 1999-01-14 | 2014-04-17 | Bolder Biotechnology Inc | 自由システイン残基を有するタンパク質の生産方法 |
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JP2020500837A (ja) * | 2016-09-29 | 2020-01-16 | マクファーレン バーネット インスティテュート フォー メディカル リサーチ アンド パブリック ヘルス リミテッドMacfarlane Burnet Institute For Medical Research And Public Health Ltd | アセンブルした糖タンパク質 |
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