KR20090114425A - 표적화 사람화된 모노클로날 항체와 복합체화된 다가변성 항원 - Google Patents
표적화 사람화된 모노클로날 항체와 복합체화된 다가변성 항원 Download PDFInfo
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Abstract
본 발명은 모듈러 재조합 항체 또는 이의 단편과 다가 항원 접합체의 신속한 어셈블리를 허용하는 코헤신-도커린 쌍의 절반을 설계, 제조 및 사용하기 위한 조성물 및 방법을 포함한다.
다가변성 항원 접합체, 재조합 모노클로날 항체, 모듈러 rAb 운반체, 코헤신-도커린 쌍
Description
본 발명은 일반적으로 신규 백신 분야, 및 보다 특히 표적화 사람화된 모노클로날 항체와 복합체화된 다가변성 항원의 설계, 제조 및 용도에 관한 것이다.
발명의 범위를 제한함이 없이, 이의 배경은 백신 개발과 관련하여 기술되어 있다.
모노클로날 항체와 관련되는 단백질 설계는 사람화(즉, 예를 들면, 설치류 mAb 서열이 사람 mAb 서열내로 통합되도록 하면서 원래의 mAb의 특이적인 항원 결합 부위는 보존함) 및 생산(통상적으로 포유동물 세포주로부터 분비됨)에 대하여 크게 진전되어 있다. 조사 및 개발에 있어 백신화과 관련한 rAb가 새로이 적용되고 있으며 현재 조작된 rAb-항원 융합 단백질(통상적으로 rAb 중쇄 또는 H 쇄의 C-말단 코돈과 프레임내에 위치한 항원 암호화 영역을 지님)을 기초로 한다. 이러한 기술에 대한 장애물은 완전한 작용적 rAb-항원의 성공적인 발현 및 생산에 있다. 많은, 아마도 대부분의 경우에서, 바람직한 항원은 조작된 rAb-항원의 분비와 섞인다. 또한, 바람직한 실체가 다수의 항원 암호화 영역을 포함하는 경우에 불량한 발현 또는 비 발현의 경향성이 증가한다.
발명의 개요
본 발명은 성분들을 단순 혼합함에 의해 조절된 방식으로 rAb 항원 복합체를 어셈블리하는 방법을 제공하며 개개의 rAb 및 특정 항원에 가장 적합한 상이한 발현 - 생산 시스템에서 rAb 및 항원(들)을 발현하고 생산하는 능력을 도모한다. 또한, 본 발명은 분비된 포유동물 발현 시스템에 대한 고 친화성 및 고 특이성 코헤신-도커린(cohesin-dockerin) 상호작용의 새로운 적용을 입증함으로써 조사 및 임상 적용을 위한 새로운 단백질 도구의 생산 및 독특한 단백질 조작 포맷의 개발을 허용한다.
보다 특히, 본 발명은 코헤신-도커린 단백질 도메인 및 이의 주변 링커를 사용한다. 예를 들면, 본 발명은 항원, 독소 또는 세포의 활성화제에 복합체화된 재조합 모노클노날 항체(rAb)의 조절된 어셈블리를 허용한다. 본 발명은 백신화 및 암 치료요법에서 광범위하고 강력하게 적용된다. 또한 다른 단백질에 대해 특이적인 친화성을 갖는 신규 단백질의 생산을 허용하는 당해 기술의 파생방법도 청구되어 있다.
본 발명은 셀룰로좀으로 불리는 잘 연구된 세균 셀룰로즈 분해 단백질 복합체의 특정 성분을 기초로 한다. 상세하게는, 2개의 단백질 도메인(코헤신 및 도커 린) 및 천연 단백질 링커 서열을 본 발명을 통해 신규 내용 및 출원에서 이용한다.
본 발명은, 특정 코헤신 및 도커린 도메인이 특이적이고 높은 친화성 코헤신-도커린 단백질-단백질 상호작용을 유지하면서 융합 단백질로서 포유동물 세포로부터 성공적이고 효율적으로 분비될 수 있다는 발견을 기초로 한다. 광범위한 코헤신-도커린 문헌은, 이러한 융합 단백질이 이러한 작용성을 가질 수 있다는 예측을 교시하고 있으나 포유동물 분비 시스템에서 이러한 융합 단백질의 생산을 기술하고 있지 않다. 현 과학 지식의 상태는, 성공적인 분비에 대한 규칙(시그날 펩타이드와 같은 특징 이외에)이 완전히 확립되어 있지 않기 때문에 발견의 예측을 허용하지 않는다. 또한, 코헤신 링커 영역은 이들의 천연 세균내에서 글리코실화되는 것으로 공지되어 있고, 코헤신 및 도커린 도메인은 예측된 글리코실화 부위를 함유한다. 이것이 실제로 포유동물 세포로부터의 분비를 선호할 수 있다고 해도, '비천연적인' 글리코실화는 코헤시스-도커린 상호작용을 방해할 것이라는 것은 명백하지 않다.
각종 상업적 적용을 위한 코헤신-도커린 상호작용이 공지되어 있지만, 본 발명은 조절된 어셈블리 효소 적용과 관련되지 않은 특이적인 단백질 복합체를 어셈블리하는 주변에서의 상호작용 구조에 대한 이미 알려져 있지 않은 가능성을 기초로 한다.
본 발명은 다양한 셀룰로즈 분해 미생물로부터의 모든 코헤신-도커린 서열의 용도를 포함하나, 미생물 클로스트리디움 써모셀룸(Clostridium thermocellum)으로부터의 특정 코헤신 및 도커린 및 링커 서열의 적용을 기술한다. 예를 들어, 본원 에 기술된 서열은 클로스트리디움 써모셀룸 도커린 서열(rAb.doc로 칭함)에 대해 C-말단 코돈에서 연결된 사람 IgG4의 H 쇄를 암호화한다. rAb.doc 단백질의 다른 양태는 상이한 H 쇄 실체를 암호화하는 벡터로 DNA 단편으로서의 도커린 암호화 영역을 단순히 이전시킴에 의해 조작되는 예로 단순하게 기술되어 있다.
보다 특히, 본 발명은 하나 이상의 항원 운반체 도메인 및 코헤신-도커린 결합 쌍의 절반에 연결된 항원-특이적인 결합 도메인을 포함하는 분자 rAb 운반체를 포함한다. 항원-특이적인 결합 도메인은 적어도 항체의 일부일 수 있으며 항체는 코헤신-도커린 결합 쌍의 절반과의 융합 단백질 및 융합 단백질내 결합 쌍이다. rAb는 또한 모듈러(modular) rAb 운반체와 함께 복합체를 형성하는 항원에 결합된 코헤신-도커린 결합 쌍의 상보적 절반을 포함할 수 있다. 코헤신-도커린 결합 쌍의 상보적 절반은 자체로 복합체[모듈러 rAb 운반체(코헤신/도커린) 항원 복합체]의 일부로서 수송된 항원과의 융합 단백질일 수 있다. 항원 특이적인 도메인의 예는 완전한 길이의 항체, 항체 가변 영역 도메인, Fab 단편, Fab' 단편, F(ab)2 단편, 및 Fv 단편, 및 Fabc 단편 및/또는 Fc 도메인의 일부와의 Fab 단편을 포함한다. 코헤신-도커린 결합 쌍에 대한 공급원의 비-제한 예는 클로스트리디움 써모셀룸, 클로스트리디움 조수이(Clostridium josui), 클로스트리디움 셀룰로라이티쿰(Clostridium cellulolyticum) 및 박테로이데스 셀룰로솔벤스(Bacteroides cellulosolvens) 및 이들의 조합을 포함한다.
항원-특이적인 결합 도메인에 의해 표적화하기 위한 비-제한적 예는 다음을 포함한다: MHC 클래스 I, MHC 클래스 II, CD1, CD2, CD3, CD4, CD8, CD11b, CD14, CD15, CD16, CD19, CD20, CD29, CD31, CD40, CD43, CD44, CD45, CD54, CD56, CD57, CD58, CD83, CD86, CMRF-44, CMRF-56, DCIR, DC-ASPGR, CLEC-6, CD40, BDCA-2, MARCO, DEC-205, 만노즈 수용체, 랑게린(Langerin), DECTIN-1, B7-1, B7-2, IFN-γ 수용체 및 IL-2 수용체, ICAM-1, Fcγ 수용체 또는 항원 제시 세포에 의해 비교적 특이적으로 발현된 다른 수용체 중에서 선택된 세포 표면 마커.
본 발명은 rAb는 또한 rAb.Doc; rAb.Coh; rAb.(Coh)x; rAb.(Doc)x; rAb.(Coh.Doc)x; 또는 rAb.(Coh)x(Doc)x(여기서, x는 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 또는 그 이상이다)로 정의된 도메인의 조합을 포함할 수 있다. 복합체내 모듈러 rAb 운반체의 예는 다음을 포함한다:
rAb.Doc:Coh.항원;
rAb.Coh:Doc.항원;
rAb.(Coh)x:(Doc.항원)x;
rAb.(Doc)x:(Coh.항원)x;
rAb.(Coh.Doc)x:(Doc.항원1)(Coh.항원2); 또는
rAb.(Coh)x(Doc)x:(Doc.항원1)x(Coh.항원2)x
(여기서, x는 1, 2, 3, 4, 5, 6, 7, 8, 9 또는 10이다).
본 발명은 또한 항원에 결합된 코헤신-도커린 결합 쌍의 상보적 절반에 결합된 코헤신-도커린 결합 쌍의 절반을 포함하는 하나 이상의 도메인에 결합된 항원 특이적인 도메인을 포함하는 모듈러 rAb 운반체의 백신을 포함한다. rAb를 표적화하는 비-제한된 예는 MHC 클래스 I, MHC 클래스 II, CD1, CD2, CD3, CD4, CD8, CD11b, CD14, CD15, CD16, CD19, CD20, CD29, CD31, CD40,CD43, CD44, CD45, CD54, CD56, CD57, CD58, CD83, CD86, CMRF-44, CMRF-56, DCIR, DC-ASPGR, CLEC-6, CD40, BDCA-2, MARCO, DEC-205, 만노즈 수용체, 랑게린, DECTIN-1, B7-1, B7-2, IFN-γ 수용체 및 IL-2 수용체, ICAM-1, Fcγ 수용체 또는 항원 제시 세포에 의해 비교적 특이적으로 발현된 다른 수용체 중에서 선택된 면역 세포 표면 단백질을 포함한다. rAb 항원 운반체를 사용한 백신화의 표적은 예를 들면, 세균, 바이러스, 진균, 원생동물 또는 암 단백질 및 이의 단편을 포함한다. 제11항에 따른 백신에 있어서, 모듈러 rAb 운반체가 rAb.Doc:Coh.항원; rAb.Coh:Doc.항원; rAb.(Coh)x:(Doc.항원)x; rAb.(Doc)x:(Coh.항원)x; rAb.(Coh.Doc)x:(Doc.항원1)(Coh.항원2); 또는 rAb.(Coh)x(Doc)x:(Doc.항원1)x(Coh.항원2)x(여기서, x는 1, 2, 3, 4, 5, 6, 7, 8, 9 또는 10이다)로 추가로 정의된다.
본 발명은 또한 표적-특이적인 도메인 및 하나 이상의 도메인 및 코헤신-도커린 결합 쌍의 절반에 대한 암호화 단편을 포함한다. 예를 들어, 표적은 항체의 적어도 일부를 암호화할 수 있는 표적 특이적인 도메인 및 항원일 수 있다. 하나 이상의 도메인은 하나 이상의 코헤신 도메인, 하나 이상의 도커린 도메인 또는 하나 이상의 코헤신 및 도커린 도메인의 조합을 암호화할 수 있다. rAb는 또한 rAb.Doc; rAb.Coh; rAb.(Coh)x; rAb.(Doc)x; rAb.(Coh.Doc)x; 또는 rAb.(Coh)x(Doc)x(여기서, x는 1, 2, 3, 4, 5, 6, 7, 8, 9 또는 10이다)로 정의된다.
본 발명은 또한 항원 특이적인 도메인 및 코헤신-도커린 결합 쌍의 절반, 운반될 단백질 분자와의 코헤신-도커린 결합 쌍의 절반 및 이들의 조합을 암호화하는 핵산을 포함하는 벡터를 포함한다. 코헤신-도커린 결합 쌍의 절반, 운반될 단백질과의 코헤신-도커린 결합 쌍의 절반 및 이들의 조합은 동일한 프로모터, 상이한 프로모터의 조절하에서, 동일한 방향으로 전사되거나 반대 방향으로 전사된다.
본 발명은 또한 항원 특이적인 도메인 및 하나 이상의 도메인 및 코헤신-도커린 결합 쌍의 절반을 암호화하는 핵산을 포함하는 벡터를 포함하는 숙주 세포를 포함한다.
모듈러 rAb 운반체를 제조하는 방법은 코헤신-도커린 결합 쌍의 절반의 하나 이상의 도메인에 연결된 항원 특이적인 도메인을 조합시킴에 의해 수행된다. rAb는 또한 rAb.Doc; rAb.Coh; rAb.(Coh)x; rAb.(Doc)x; rAb.(Coh.Doc)x; 또는 rAb.(Coh)x(Doc)x(여기서, x는 1, 2, 3, 4, 5, 6, 7, 8, 9 또는 10이다)로 정의된다. rAb의 예들은 항원에 결합된 코헤신:도커린 쌍의 상보적 절반과 복합체화되며 rAb.Doc:Coh.항원; rAb.Coh:Doc.항원; rAb.(Coh)x:(Doc.항원)x; rAb.(Doc)x:(Coh.항원)x; rAb.(Coh.Doc)x:(Doc.항원1)(Coh.항원2); 또는 rAb.(Coh)x(Doc)x:(Doc.항원 1)x(Coh.항원2)x(여기서, x는 1, 2, 3, 4, 5, 6, 7, 8, 9 또는 10이다) 중에서 선택된다.
본 발명은 또한 rAb.Doc:Coh.독소 자가-어셈블리된 접합체를 포함하는 면역독소일 수 있으며, 여기서, rAb는 세포 표적에 대해 특이적이다. 독소의 예는 방사성 동위원소, 금속, 효소, 보툴린, 테타누스, 리신(ricin), 콜레라, 디프테리아, 아플라톡신, 퍼프린젠스 독소, 마이코독소, 시가독소, 스타필로코코스 장독소 B, T2, 세구이독소, 삭시독소, 아브린, 시아노기노신, 알파독소, 테트로도독소, 아코노독소, 뱀독 및 거미 독을 포함한다. 면역독소에 대한 세포 표적은 질병이 있거나 감염된 세포를 포함한다. 표적화를 위한 질병이 있는 세포의 예는 예를 들면, 백혈병 및 림프종과 같은 혈액암, 별아교세포종 또는 아교모세포종과 같은 신경 종양, 흑색종, 유방암, 폐암, 두경부암, 위암 또는 결장암과 같은 위장관 종양, 간암, 췌장암, 자궁경부암, 자궁암, 난소암, 질암, 고환암, 전립선암 또는 음경암과 같은 비뇨생식기 종양, 골 종양, 혈관 종양, 또는 입술, 비인두, 인두 및 구강, 식도, 직장, 담낭, 담관, 후두, 폐 및 기관지, 방광, 신장, 뇌 및 신경계의 다른 부분, 갑상선의 암, 호지킨병(Hodgkin's disease), 비-호지킨 림프종(non-Hodgkin's lymphoma), 다발성 골수종 및 백혈병에 대한 암 세포를 포함한다. 면역독소는 병원체, 예를 들면, 세균, 원생동물, 연충, 바이러스-감염된 세포 또는 진균을 직접 표적화할 수 있다.
본 발명은 또한 융합 단백질을 기질에 결합된 상보성 코헤신 또는 도커린에 접합되는 rAb와 상호작용시킴으로써 코헤신 또는 도커린 융합 단백질을 분리함에 의한 단백질 정제 방법을 포함한다. 본 발명은 또한 활성인 코헤신.독소 융합 단백질을 용이하게 정제하는 유익한 생화학적 특성을 부여하기 위한 독소용 융합 파트너로서 코헤신을 사용할 수 있다. 본 발명은 또한 항-DC rAb.Doc를 사용하여 DC를 제거하는 치료학적 적용을 위해 DC를 표적화할 수 있다. 치료학적 적용은 예를 들면, 이식, 자가면역병, 감염성 질병 또는 암을 포함한다. 본 발명은 또한, 항체가 성숙하여 면역화를 위해 수지상 세포를 활성화시키는, 수지상 세포의 생존을 향상시키기에 충분한 양으로 제공된 항-DC-SIGN/L 항체를 포함한다. 항체는 생체내에서 백신중 애주번트로서 세포, 예를 들면 수지상 세포를 표적화할 수 있다.
본 발명은 또한 치료제, 진단제 및 산업적 제제로서 이가 및 다가(rAb1.Doc:Coh.rAb2) 자가-어셈블리된 접합체이다. 달리는, 본 발명은 치료학적, 세포 증식 또는 성숙제로서 이가 및 다가 (rAb.Doc:Coh.사이토카인), (rAb.Coh:Doc.사이토카인) 또는 (사이토카인1.Coh:사이토카인2.Doc) 자가-어셈블리된 접합체이다. 모듈러 rAbs 운반체는 표적 세포에 특이적으로 결합하여 사이토카인을 전달함으로써 표적 세포에 대해 효과를 발휘할 수 있는 하나 이상의 다가 rAb 및/또는 rAb.사이토카인 및/또는 사이토카인.사이토카인 조합을 스크리닝하는 것을 포함하는 방법으로 제조될 수 있다. 본 발명과 함께 사용하기 위한 사이토카인은 인터루킨, 전환 성장 인자(TGF), 섬유아세포 성장 인자(FGF), 혈소판 기원한 성장 인자(PDGF), 상피 성장 인자(EGF), 연결 조직 활성화된 펩타이드(CTAP), 골원성 인 자, 및 이러한 성장 인자의 생물학적으로 활성인 유사체, 단편 및 유도체, B/T-세포 분화 인자, B/T-세포 성장 인자, 유사분열촉진성 사이토카인, 화학주성 사이토카인, 콜로니 자극 인자, 혈관형성 인자, IFN-α, IFN-β, IFN-γ, IL1, IL2, IL3, IL4, IL5, IL6, IL7, IL8, IL9, IL10, IL11, IL12, IL13, IL14, IL15, IL16, IL17, IL18 등, 렙틴, 마이오스타틴, 대식구 자극 단백질, 혈소판-기원한 성장 인자, TNF-α, TNF-β, NGF, CD40L, CD137L/4-1BBL, 사람 림프독소-β, G-CSF, M-CSF, GM-CSF, PDGF, IL-1α, IL1-β, IP-10, PF4, GRO, 9E3, 에리트로포이에틴, 엔도스타틴, 안지오스타틴, VEGF, 전환 성장 인자(TGF) 슈퍼유전자 계열, 예를 들면, 베터 전환 성장 인자(예를 들면, TGF-β1, TGF-β2, TGF-β3); 골 형태형성 단백질(예를 들면, BMP-1, BMP-2, BMP-3, BMP-4, BMP-5, BMP-6, BMP-7, BMP-8, BMP-9); 헤파린-결합 성장 인자(섬유아세포 성장 인자(FGF), 상피 성장 인자(EGF), 혈소판-기원 성장 인자(PDGF), 인슐린-유사 성장 인자(IGF)); 인히빈(예를 들면, 인히빈 A, 인히빈 B); 성장 분화 인자(예를 들면, GDF-1); 및 액티빈(예를 들면, 액티빈 A, 액티빈 B, 액티빈 AB)를 포함한다.
본 발명의 특징 및 장점을 보다 완전히 이해하기 위해서는, 첨부되는 도면과 함께 본 발명의 상세한 설명이 참조되어야 하며, 도면에서,
도 1은 동일한 조작된 사람화된 mAb(MATCHMAB)(하부 부위)와 동시에 복합체내에서 표적화된 다수의 항원의 예와 선행 기술의 것(상부 부위)을 비교한 도이다.
도 2는 이-특이적인 mAb를 형성하기 위한 본 발명의 용도를 나타낸다.
도 3은 SDS.PAGE 및 쿠마시 브릴리언트 블루(Coomassie Brilliant Blue) 염색을 환원시킴으로써 분석된 단백질 G 친화성 정제된 rAb 단백질을 나타낸다. 레인은 좌측에서 우측의 순서이다.
도 4A 및 도 4B는 각종 rAb.융합 단백질의 분비 수준의 항-사람 IgFc ELISA에 의한 측정을 나타낸다.
도 5는 분비된 항-LOX1_15C4 rAb(청색 기호) 및 항-LOX1_15C4.doc rAb(적색 기호) 단백질의 항-사람 IgFc ELISA(HRP 활성) 및 LOX-1.알칼린 포스파타제 결합(AP 활성)에 의한 측정을 나타낸다.
도 6은 mIgG 카파 발현 플라스미드로 공동-형질감염시킨 경우, rAB-pCMV(mIgG2bH-도커린) 플라스미드가 rAB-mIgG2b.도커린 융합 단백질의 효율적인 분비를 지시함을 나타낸다.
도 7A 및 도7B는 AP가 아닌 분비된 coh.알칼린 포스파타제(coh.AP)가 플라스틱상에서 고정화된 rAb.Doc에 효율적으로 및 특이적으로 결합함을 나타낸다.
도 8A 및 도 8B는 분비된 G.AP를 함유하는 상청액의 각종 희석물의 경우 고정화된 mIgG2a 및 mIgG2b에 결합하지만 rAb.doc에는 결합하지 않는 반면, coh.AP는 rAb.doc에 특이적으로 결합함을 나타낸다.
도 9는 미세-역가 플레이트 속에서 1시간 동안 항온처리에 의해 어셈블리된 고정량의 proG.AP 또는 coh.AP 또는 coh2.AP(0.1 ㎍) 및 고정화된 mIgG2b 또는 rAb.doc (0.25 ㎍)사이의 복합체의 차등적 안정성을 나타낸다.
도 10은 미세-역가 플레이트 속에서 1시간 동안 항온처리에 의해 어셈블리된 고정량의 proG.AP 또는 coh.AP (0.1 ㎍) 및 고정화된 mIgG2b 또는 rAb.doc (0.25 ㎍)사이의 복합체의 사람 혈청내 차등적 안정성을 나타낸다.
도 11은 rAb.doc 상청액 및 coh.AP 상청액을 동일한 단백질 G 친화성 컬럼에 순차적 적용함에 의해 생산된 rAb.doc:Coh2.AP 복합체의 환원된 대 비-환원된 SDS.PAGE 분석을 나타내는 겔이다.
도 12는 rAb.doc 상청액 및 coh.Flu HA5-1 상청액을 동일한 단백질 G 친화성 컬럼에 순차적 적용시킴으로써 생산된 rAb.doc:Coh.Flu HA5-1 복합체의 비-환원된 SDS.PAGE 분석이다.
도 13은 개개의 정제된 성분들을 혼합시킴에 의해 형성된 항-DC_rAb.doc:coh.Flu M1 복합체가 시험관내에서 Flu M1-특이적인 T 세포를 확장시키는데 있어서 효과적이었음을 나타내는 도이다.
도 14는 개개의 정제된 성분들을 혼합시킴에 의해 형성된 항-DC_rAb.doc:coh.Flu M1은 시험관내에서 Flu M1-특이적인 T 세포를 확장하는데 효과적이었지만 mIgG2b.doc:coh.Flu M1 복합체는 그렇지 않음을 나타내는 도이다.
도 15는, CD34+ 사람 DC가 CD1a+ 및 CD14+ 아형으로 분류되며 3 nM 항-DC_rAb.Flu M1 PEP 또는 항-DC_rAb의 존재 및 부재하에 배양됨을 나타낸다.
도 16은 coh.pep 단백질의 합성을 지시하는 발현 플라스미드를 지닌 이.콜라이가 성장하여 특이적인 단백질 생산을 유도함을 나타낸다. 세포를 수거하여 초음 파로 파괴하였다.
도 17은, DCIR.Doc rAb 단독으로는 DC의 생존에 효과를 가지지 않으나, DC-SIGN/L.Doc rAb는 이들의 생존을 향상시킴을 나타낸다.
도 18은, Coh.PE38 단독은 7-AAD 기록된 아폽토시스 세포(22.1 내지 29.8%)의 수를 약간 증가시키지만, DCIR 또는 DC-SIGN/L.Doc rAb에 연결되는 경우, Coh.PE38은 7-AAD 기록된 아폽토시스 세포의 수를 현저히 향상시킴을 나타낸다.
도 19는, 항-DC-SIGN/L 및 항-DC-ASPGR rAb.Coh 및 rAb.Doc의 발현물이 효율적으로 분비되었음을 나타낸다.
도 20은 사람 B 세포의 증식에 있어서 IL-21 및 Coh.IL-21의 효과를 나타낸다.
본 발명의 각종 양태의 제조 및 사용이 하기 상세히 논의되어 있다고 해도, 본 발명은 광범위한 특이적 내용내에서 구현될 수 있는 많은 적용가능한 발명적 개념을 제공함을 인지하여야 한다. 본원에 논의된 특이적인 양태는 본 발명을 제조하고 사용하기 위한 특정 방법의 단지 예이며 본 발명의 범위를 결정하지 않는다.
본 발명의 이해를 용이하게 하기 위하여, 다수의 용어들이 하기 정의되어 있다. 본원에 정의된 용어들은 본 발명과 관련된 영역내 통상의 기술자가 일반적으로 이해하는 의미를 지닌다. "a", "an" 및 "the"와 같은 용어는 단일체만을 말하는 것이 아니라, 예시에 사용될 수 있는 특정 예의 일반 부류를 포함하는 것으로 의도된다. 본원의 기술은 본 발명의 특정 양태를 기술하는데 사용되나 이의 용도는 청구의 범위에 요약된 것을 제외하고는, 본 발명을 결정하지 않는다.
현재, 단백질 조작 기술은 재조합 mAb(H 또는 L, 일반적으로 H의 C-말단이 흔히 사용된다)의 항원(또는 쇄 중 하나에 대한 상이한 항원)의 용이하고 조절된 부가를 가능하도록 한다. 상이한 항원 또는 상이한 항원 세트가 mAb에 연결되는 것이 요구되는 경우, mAb는 상이한 실체로서 재-조작, 발현 및 정제할 필요가 있다.
본 발명은 조절되고, 다가변성 양식으로, 하나의 단일의 주요 재조합 mAb에 대해 다수의 항원 또는 단백질(조작되고, 발현되며 주요 mAb와는 독립적으로 정제된)의 복합체화를 제공한다. 현재, 하나의 주요 mAb에 상이한 단백질(각각 조작되어 스트렙타비딘에 별개도 연결된)의 부가를 제공하는 부위-특이적인 비오티닐화 부위를 조작하는 방법이 존재한다. 그러나, 본 발명은 고정된 등몰비 및 위치에서 별개의 조작된 단백질의 다수의 조합의 주요 mAb에 대한 부가를 제공한다.
본원에 사용된 용어 "모듈러 rAb 운반체"는 단일 재조합 모노클로날 항체(mAb)에 대한 다양한 항원, 활성화 단백질 또는 다른 항체의 조절된 모듈러 부가를 제공하기 위해 조작된 재조합 항체 시스템을 기술하기 위해 사용된다. rAb는 표준 하이브리도마 기술, 재조합 항체 디스플레이, 사람화된 모노클로날 항체 등을 사용하여 제조된 모노클로날 항체일 수 있다. 모듈러 rAb 운반체는 예를 들면, 내부화된 수용체, 예를 들면, 사람 수지상 세포 수용체에 대한 하나의 주요 재조합 항체를 통해 다수의 항원 및/또는 항원과 활성화 사이토카인을 수지상 세포(DC)에 대해 표적화하는데 사용될 수 있다. 모듈러 rAb 운반체는 또한 조절되고 정의된 방식으로 2개의 상이한 재조합 mAb를 말단-대-말단으로 연결하는데 사용될 수 있다.
"모듈러 rAb 운반체"의 항원 결합은 하나 이상의 가변성 도메인, 하나 이상의 가변성 및 제1 불변 도메인, Fab 단편, Fab' 단편, F(ab)2 단편, 및 Fv 단편, 및 Fabc 단편 및/또는 유사한 모듈러 결합 부위가 아미노산 서열에 가해지고/지거나 결합된 Fc 도메인의 일부를 갖는 Fab 단편일 수 있다. 모듈러 rAb 운반체에서 사용하기 위한 항체는 임의의 동형 또는 부류, 아부류 또는 임의의 공급원(동물 및/또는 재조합체)일 수 있다.
하나의 비-제한적인 예에서, 모듈러 rAb 운반체는 조작된 재조합 mAb의 측면에서 특이적이고 정의된 단백질 복합체를 제조하기 위한 하나 이상의 모듈러 코헤신-도커린 단백질 도메인을 가지도록 조작된다. mAb는 mAb의 항원 결합 도메인으로부터 하나 이상의 모듈러 코헤신-도커린 단백질 도메인을 포함하는 융합 단백질의 일부이다. 코헤신-도커린 단백질 도메인은 심지어 예를 들면, 화학적 가교-결합제 및/또는 이황화 결합을 사용함으로써 해독후에 부착될 수 있다.
모듈러 rAb 운반체는 분리된 분자, 예를 들면, 펩타이드, 단백질, 지질, 탄수화물, 핵산(올리고뉴클레오타이드, 압타머, 염기 또는 골격 변형이 이루어지거나 또는 이루어지지 않는 벡터) 또는 이들의 조합을 코헤신-도커린 쌍의 상보적인 쌍에 대해 분자를 분리하는 결합에 의해 운반하는데 사용될 것이다. 예를 들면, 제조된 도커린 또는 코헤신은 융합 단백질로 제조되거나 항원, 펩타이드, 단백질, 독소, 사이토카인, 효소, 구조 단백질, 세포외 기질 단백질, 다른 항체, 세포 또는 이의 단편에 화학적으로 결합된다. 모듈러 rAb 운반체는 하나 이상의 코헤신, 도커린 또는 모듈러 rAb 운반체의 항원 인지 도메인을 통해 전달용의 하나 이상의 상보성 코헤신/도커린-분자와의 복합체를 형성하는 코헤신 및 도커린 도메인 둘다를 지닐 수 있다.
본원에 사용된 용어 "항원"은 항원의 수용체내에서 체액성 및/또는 세포성 면역 반응을 개시할 수 있는 분자를 말한다. 항원은 본 발명에서 2개의 상이한 측면에서 사용될 수 있다: rAb의 항체 또는 다른 항원 인지 도메인에 대한 표적물로서 또는 모듈러 rAb 운반체에 대해 도커린/코헤신-분자 상보체의 일부로서. 항원은 일반적으로 백신화가 유리한 치료일 수 있는 질병을 유발하는 물질이다. 항원이 MHC상에 존재하는 경우, 펩타이드는 흔히 약 8 내지 약 25개의 아미노산이다. 항원은 예를 들면, 단순한 중간 대사물, 당, 지질 및 호르몬, 및 복합체 탄수화물, 인지질, 핵산 및 단백질과 같은 거대 분자를 포함하는 임의의 유형의 생물학적 분자를 포함한다. 항원의 일반적인 범주는 바이러스 항원, 세균 항원, 진균 항원, 원생동물 및 기타 기생충 항원, 종양 항원, 자가면역 병, 알레르기 및 이식 거부에 관여된 항원 및 다른 각종 항원을 포함하나, 이에 한정되지 않는다.
모듈러 rAb 운반체는 임의의 수의 활성제, 예를 들면, 항생제, 항-감염제, 항바이러스제, 항-종양제, 항발열제, 진통제, 소염제, 골다공증용 치료제, 효소, 사이토카인, 항응고제, 다당류, 콜라겐, 세포 및 앞서의 활성제 2개 이상의 조합을 운반할 수 있다. 본 발명을 사용하여 전달하기 위한 항생제의 예는 테트라사이클린, 아미노글리코사이드, 페니실린, 세팔로스포린, 설폰아미드 약물, 클로람페니콜 나트륨 석시네이트, 에리트로마이신, 반코마이신, 린코마이신, 클린다마이신, 니스타틴, 암포테리신 B, 아만티딘, 이독스우리딘, p-아미노 살리사이클산, 이소니아지드, 리팜핀, 안티노마이신 D, 미트라마이신, 다우노마이신, 아드리아마이신, 블레오마이신, 빈블라스틴, 빈크리스틴, 프로카르바진, 이미다졸 카르복스아미드 등을 포함하나, 이에 한정되지 않는다.
본 발명을 사용하여 전달하기 위한 항-종양제의 예는 독소루비신, 다우노루비신, 탁솔, 메토트렉세이트 등을 포함하나, 이에 한정되지 않는다. 항발열제 및 진통제의 예는 아스피린, Motrin®, Ibuprofen®, 나프로신, 아세트아미노펜 등을 포함하나, 이에 한정되지 않는다.
본 발명을 사용하여 전달하기 위한 소염제의 예는 NSAIDS, 아스피린, 스테로이드, 덱사메타손, 하이드로코르티손, 프레드니솔론, 디클로페낙 Na 등을 포함하나, 이에 한정되지 않는다.
본 발명을 사용하여 전달하기 위한 골다공증을 치료하기 위한 치료제 및 골과 골격에 작용하는 기타 인자는 칼슘, 알렌드로네이트, 골 GLa 펩타이드, 파라티로이드 호르몬 및 이의 활성 단편, 히스톤 H4-관련 골 형성 및 증식 펩타이드 및 돌연변이, 이의 유도체 및 유사체를 포함하나, 이에 한정되지 않는다.
본 발명을 사용하여 전달하기 위한 효소 및 효소 보조인자의 예는 판크레아제, L-아스파라기나제, 히알루로니다제, 키모트립신, 트립신, tPA, 스트렙토키나제, 우로키나제, 판크레아틴, 콜라게나제, 트립시노겐, 키모트립시노겐, 플라스미노겐, 스트렙토키나제, 아데닐 사이클라제, 초과산화물 디스뮤타제(SOD) 등을 포함하나, 이에 한정되지 않는다.
본 발명을 사용하여 전달하기 위한 사이토카인의 예는 인터루킨, 전환 성장 인자(TGF), 섬유아세포 성장 인자(FGF), 혈소판 기원 성장 인자(PDGF), 상피 성장 인자(EGF), 연결 조직 활성화된 펩타이드(CTAP), 골형성 인자 및 생물학적으로 활성인 이러한 성장 인자의 유사체, 단편 및 유도체를 포함하나, 이에 한정되지 않는다. 사이토카인은 B/T-세포 분화 인자, B/T-세포 성장 인자, 유사분열촉진 사이토카인, 화학주성 사이토카인, 콜로니 자극 인자, 혈관형성 인자, IFN-α, IFN-β, IFN-γ, IL1, IL2, IL3, IL4, IL5, IL6, IL7, IL8, IL9, IL10, IL11, IL12, IL13, IL14, IL15, IL16, IL17, IL18 등, 렙틴, 마이오스타틴, 대식구 자극 단백질, 혈소판-기원 성장 인자, TNF-α, TNF-β, NGF, CD40L, CD137L/4-1BBL, 사람 림프독소-β, G-CSF, M-CSF, GM-CSF, PDGF, IL-1α, IL1-β, IP-10, PF4, GRO, 9E3, 에리트로포이에틴, 엔도스타틴, 안지오스타틴, VEGF 또는 이의 임의의 단편 또는 조합일 수 있다. 다른 사이토카인은 베타 전환 성장 인자(예를 들면, TGF-β1, TGF-β2, TGF-β3)를 포함하는 전환 성장 인자(TGF) 슈퍼유전자 계열의 구성원; 골 형태형성 단백질(예를 들면, BMP-1, BMP-2, BMP-3, BMP-4, BMP-5, BMP-6, BMP-7, BMP-8, BMP-9); 헤파린-결합 성장 인자(예를 들면, 섬유아세포 성장 인자(FGF), 상피 성장 인자(EGF), 혈소판-기원 성장 인자(PDGF), 인슐린-유사 성장 인자(IGF)); 인히빈(예를 들면, 인히빈 A, 인히빈 B); 성장 분화 인자(예를 들면, GDF-1); 및 액티빈(예를 들면, 액티빈 A, 액티빈 B, 액티빈 AB)을 포함한다.
본 발명을 사용하여 전달하기 위한 성장 인자의 예는 포유동물 세포로부터와 같은 자연 또는 천연의 공급원으로부터 분리할 수 있거나 재조합 DNA 기술 또는 각종 화학 과정에 의해서와 같이 화학적으로 합성할 수 있다. 또한, 이러한 인자의 유사체, 단편 또는 유도체를 사용할 수 있으나, 단, 이들은 천연 분자의 적어도 일부의 생물학적 활성을 나타낸다. 예를 들면, 유사체는 부위-지시된 돌연변이유발 또는 다른 유전 공학 기술에 의해 변경된 유전자의 발현으로 제조할 수 있다.
본 발명을 사용하여 전달하기 위한 항응고제의 예는 와파린, 헤파린, 히루딘 등을 포함하나, 이에 한정되지 않는다. 본 발명을 사용하여 전달하기 위한 면역 시스템에 작용하는 인자의 예는 염증 및 악성 신생물을 제어하는 인자, 및 화학주성 펩타이드 및 브래디키닌과 같이 감염성 미생물을 공격하는 인자를 포함하나, 이에 한정되지 않는다.
바이러스 항원 및/또는 바이러스 항원 표적의 예는 예를 들면, gag, pol 및 env 유전자의 유전자 생성물과 같은 사람 면역결핍성 바이러스(HIV) 항원으로부터의 항레트로바이러스 항원과 같은 레트로바이러스 항원, Nef 단백질, 역전사효소 및 다른 HIV 성분; B형 간염 바이러스의 S, M 및 L 단백질과 같은 간염 바이러스 항원, B형 간염 바이러스의 예비-S 항원, 및 기타 간염, 예를 들면, A, B 및 C형 간염, C형 간염 바이러스 RNA와 같은 바이러스 성분; 헤마글루티닌 및 뉴라미니다제와 같은 인플루엔자 바이러스 항원 및 기타 인플루엔자 바이러스 성분; 홍역 바이러스 융합 단백질과 같은 홍역 바이러스 항원 및 기타 홍역 바이러스 성분; 단백질 E1 및 E2와 같은 루벨라 바이러스 항원 및 기타 루벨라 바이러스 성분; VP7sc와 같은 로타바이러스 항원 및 기타 로타바이러스 성분; 외피 당단백질 B와 같은 사이토메갈로바이러스 항원 및 기타 사이토메갈로바이러스 항원 성분; RSV 융합 단백질, M2 단백질과 같은 호흡기 합포체 바이러스 항원 및 기타 호흡기 합포체 바이러스 항원 성분; 즉시 초기 단백질(immediate early protein)과 같은 단성 바이러스 항원, 당단백질 D 및 다른 간염 단성 바이러스 항원 성분; gpI, gpII와 같은 바리셀라 조스터 바이러스 항원, 및 기타 바리셀라 조스터 바이러스 항원 성분; 단백질 E, M-E, M-E-NS1, NS2, NS1-NS2A, 80% E와 같은 일본 뇌염 바이러스 항원, 및 기타 일본 뇌염 바이러스 항원 성분; 래비스 당단백질, 래비스 핵단백질과 같은 래비스 바이러스 항원 및 기타 래비스 바이러스 항원 성분을 포함하나, 이에 한정되지 않는다. 바이러스 항원의 추가의 예에 대해서는 문헌[참조: Fundamental Virology, Second Edition, eds. Fields, B. N. and Knipe, D. M. (Raven Press, New York, 1991)]을 참조한다.
본 발명의 rAb-DC/DC-항원 백신을 사용하여 전달할 수 있는 항원 및/또는 항원 표적은 바이러스 항원, 세균 항원, 진균 항원 또는 기생충 항원과 같은 항원을 암호화하는 유전자를 포함한다. 바이러스는 피코르나바이러스, 코로나바이러스, 토가바이러스, 플라비바이러스, 라브도바이러스, 파라믹소바이러스, 오르토믹소바이러스, 부니아바이러스, 아레나바이러스, 레오바이러스, 레트로바이러스, 파필로마바이러스, 파르보바이러스, 헤르페스바이러스, 폭스바이러스, 헤파드나바이러스 및 스폰지폼 바이러스를 포함한다. 기타 바이러스 표적은 인플루엔자, 헤르페스 단성 바이러스 1 및 2, 홍역, 뎅기열, 천연두, 소아마비 또는 HIV를 포함한다. 병원체는 파동편모충, 촌충, 회충, 연충, 말라리아를 포함한다. 태아 항원 또는 전립선 특이적인 항원과 같은 종양 마커를 이러한 방식으로 표적화할 수 있다. 다른 예는 HIV env 단백질 및 B형 간염 표면 항원을 포함한다. 백신화 목적을 위한 본 발명에 따른 벡터의 투여는, 벡터-관련 항원이 충분이 비-면역원성이어서, 강력한 면역 반응이 요구되는 트랜스유전자의 장기간 발현이 가능하도록 함이 요구되며, 이를 위해서는 강력한 면역 반응이 요구된다. 일부 경우에, 개체의 백신화는 단지 매년 또는 2년과 같이 드물게 요구될 수 있으며 감염성 제제에 대해 장기간의 면역원성 보호를 제공할 수 있다. 본 발명을 사용하여 벡터에서 및 궁극적으로 항원으로서 사용하기 위한 유기체, 알레르겐 및 핵산 및 아미노산 서열의 예는 본원에 관련 부분, 특히 본 발명과 함께 사용될 수 있는 유기체 및 특정 서열과 일치하는 표가 참조로 인용된 미국 특허 제6,541,011호에서 찾을 수 있다.
본원에 기술된 rAb 백신과 함께 사용하기 위한 세균 항원은 예를 들면, 백일해 독소, 섬유상 헤마글루티닌, 페르탁틴, FIM2, FIM3, 아데닐레이트 사이클라제와 같은 세균 항원 및 다른 백일해 세균 항원 성분; 디프테리아 독소 및 변성독소와 같은 디프테리아 세균 항원 및 기타 디프테리아 세균 항원 성분; 테타누스 독소 또는 변성독소와 같은 테타누스 세균 항원 및 기타 테타누스 세균 항원 성분; M 단백질과 같은 스트렙토코커스 세균 항원 및 기타 스트렙토코커스 세균 항원 성분; 리포폴리사카라이드와 같은 그람-음성 바실러스 세균 항원 및 기타 그람-음성 세균 항원 성분, 마이콜산, 열 쇼크 단백질 65(HSP65), 30kDa 주요 분비된 단백질, 항원 85A와 같은 마이코박테리움 투베르쿨로시스 세균 항원 및 기타 마이코박테리아 항원 성분; 헬리코박터 필로리 세균 항원 성분; 뉴몰라이신, 폐렴 협막 폴리사카라이드와 같은 폐렴 세균 항원 및 기타 페렴 세균 항원 성분; 협막 다당류와 같은 해모필루스 인플루엔자 세균 항원 및 기타 해모필루스 인플루엔자 세균 항원 성분; 안트락스 보호 항원과 같은 안트락스 세균 항원 및 기타 안트락스 세균 항원 성분; rompA와 같은 리케차 세균 항원 및 기타 리케차 세균 항원 성분을 포함하나, 이에 한정되지 않는다. 또한, 본원에 기술된 세균 항원에는 임의의 다른 세균, 마이코박테리아, 마이코플라스마, 리케차 또는 클라미디아(chlamydia) 항원이 포함된다. 부분 또는 전체 병원체는 또한 해모필루스 인플루엔자; 플라스모디움 팔시파룸; 네이세리아 메닌기티디스; 스트렙토코쿠스 뉴모니애; 네이세리아 고노레아; 살모넬라 혈청형 티피; 시겔라; 비브리오 콜레라에; 뎅기열; 뇌염; 일본 뇌염; 라임병(lyme disease); 예르시니아 페스티스; 서부 나일강 열 바이러스(west nile virus); 황색열(yellow fever); 야생토끼병(tularemia), 간염(바이러스; 세균); RSV(호흡기 합포체 바이러스); HPIV 1 및 HPIV 3; 아데노바이러스; 천연두; 알레르기 및 암이 포함된다.
본 발명의 조성물 및 방법과 함께 사용하기 위한 진균 항원은 예를 들면, 칸디다 진균 항원 성분; 열 쇼크 단백질 60(HSP60)과 같은 히스토플라스마 진균 항원 및 기타 히스토플라스마 진균 항원 성분; 협막 다당류와 같은 크립토코쿠스 진균 항원 및 기타 크립토코쿠스 진균 항원 성분; 스페룰(spherule) 항원과 같은 코키디오데스(coccidiodes) 진균 항원 및 기타 코키디오데스 진균 항원 성분; 및 트리코피틴과 같은 티네아(tinea) 진균 항원 및 기타 코키디오데스 진균 항원 성분들을 포함하나, 이에 한정되지 않는다.
원생동물 및 기타 기생충 항원의 예는 예를 들면, 메로조이테(merozoite) 표면 항원, 스포로조이테(sporozoite) 표면 항원, 키르쿰스포로조이테(circumsporozoite) 항원, 가메토사이트(gametocyte)/가메트(gamete) 표면 항원, 혈액-단계 항원 pf 155/RESA 및 기타 플라스모디움 항원 성분; SAG-1, p30과 같은 톡소플라스마 항원 및 기타 톡소플라스마 항원 성분; 글루타티온-S-트랜스퍼라제, 파라마이오신과 같은 스키스토조마에(schistosomae) 항원, 및 기타 스키스토소마에 항원 성분; gp63, 리포포스포글리칸 및 이의 관련 단백질과 같은 레슈마니아 주요 및 기타 레슈마니아 항원 및 다른 레슈마니아 항원 성분; 및 75-77 kDa 항원, 56kDa 항원과 같은 트리파노소마 크루지(trypanosoma cruzi) 항원 및 기타 트리파노소마 항원 성분들을 포함하나, 이에 한정되지 않는다.
본 발명의 rAb의 항체 부위의 항원 인지 부위를 사용하여 표적화할 수 있는 면역 세포 표면상의 표적 항원은 일반적으로 내부화 가능성, 면역 세포 특이성의 수준, 표적화된 면역 세포의 유형, 면역 세포 성숙도의 수준 및/또는 활성화 등을 기준으로 선택될 것이다. 수지상 세포에 대한 세포 표면 마커의 예는 MHC 클래스 I, MHC 클래스 II, CD1, CD2, CD3, CD4, CD8, CD11b, CD14, CD15, CD16, CD19, CD20, CD29, CD31, CD40, CD43, CD44, CD45, CD54, CD56, CD57, CD58, CD83, CD86, CMRF-44, CMRF-56, DCIR, DC-ASPGR, CLEC-6, CD40, BDCA-2, MARCO, DEC-205, 만노즈 수용체, 랑게린, DECTIN-1, B7-1, B7-2, IFN-γ 수용체 및 IL-2 수용체, ICAM-1, Fcγ 수용체 또는 항원 제시 세포에 의해 비교적 특이적으로 발현된 기타 수용체를 포함하나, 이에 한정되지 않는다. 항원 제시 세포에 대한 세포 표면 마커의 예는 MHC 클래스 I, MHC 클래스 II, CD1, CD2, CD3, CD4, CD8, CD11b, CD14, CD15, CD16, CD19, CD20, CD29, CD31, CD40,CD43, CD44, CD45, CD54, CD56, CD57, CD58, CD83, CD86, CMRF-44, CMRF-56, DCIR, DC-ASPGR, CLEC-6, CD40, BDCA-2, MARCO, DEC-205, 만노즈 수용체, 랑게린, DECTIN-1, B7-1, B7-2, IFN-γ 수용체 및 IL-2 수용체, ICAM-1, Fcγ 수용체 또는 항원 제시 세포에 의해 비교적 특이적으로 발현된 기타 수용체를 포함하나, 이에 한정되지 않는다. T 세포에 대한 세포 표면 마커의 예는 CD3, CD4, CD8, CD14, CD20, CD11b, CD16, CD45 및 HLA-DR을 포함하나, 이에 한정되지 않는다.
전달용 세포 표면상의 표적 항원은 종양 조직의 세포의 세포 표면, 세포질, 핵, 세포소기관 등으로부터 통상적으로 기원할 종양 항원의 특징적인 것들을 포함한다. 본 발명의 항체 부위에 대한 종양 표적의 예는 백혈구 및 림프구와 같은 혈액암, 별아교세포종 또는 아교모세포종과 같은 신경 종양, 흑색종, 유방암, 폐암, 두경부암, 위암 또는 결장암과 같은 위장관 종양, 간암, 췌장암, 자궁경부암, 자궁암, 난소암, 질암, 고환암, 전립선암 또는 음경암과 같은 비뇨생식기 종양, 골 종양, 혈관 종양, 또는 입술, 비인두, 인두 및 구강, 식도, 직장, 담낭, 담관, 후두, 폐 및 기관지, 방광, 신장, 뇌 및 신경계의 기타 부분, 갑상선의 암, 호지킨병(Hodgkin's disease), 비-호지킨 림프종, 다발성 골수종 및 백혈병을 포함하나, 이에 한정되지 않는다.
본 발명을 사용한 항원 제시용 면역 세포와 함께 또는 단독으로 전달될 수 있는 항원의 예는 종양 단백질, 예를 들면, 돌연변이된 종양유전자(oncogene); 종양과 관련된 바이러스 단백질; 및 종양 점액소 및 당지질을 포함한다. 항원은 위에서 나타낸 바이러스의 부류로부터의 것들일 수 있는 종양과 관련된 바이러스 단백질일 수 있다. 특정의 항원은 종양의 특징일 수 있거나(종양 전구체 세포에 의해 일반적으로 발현되지 않는 단백질인 하나의 서브세트), 종양 전구 세포내에서 일반적으로 발현되나 종양의 돌연변이 특징을 갖는 단백질일 수 있다. 다른 항원은 변경된 활성 또는 세포하 분포를 갖는 정상 단백질의 돌연변이 변이체(들), 예를 들면 종양 항원을 생성하는 유전자의 돌연변이를 포함한다.
종양 항원의 특이적인 비-제한적 예는 CEA, 전립선 특이적인 항원 (PSA), HER-2/neu, BAGE, GAGE, MAGE 1-4, 6 및 12, MUC(뮤신)(예를 들면, MUC-1, MUC-2 등), GM2 및 GD2 강글리오사이드, ras, myc, 타이로시나제, MART (흑색종 항원), Pmel 17(gp100), GnT-V 인트론 V 서열(N-아세틸글루코아미닐트랜스퍼라제 V 인트론 V 서열), 전립선 Ca psm, PRAME (흑색종 항원), β-카테닌, MUM-1-B(흑색종 유비퀴토스 돌연변이된 유전자 생성물), GAGE (흑색종 항원) 1, BAGE (흑색종 항원) 2-10, c-ERB2 (Her2/neu), EBNA[엡슈타인-바르(Epstein-Barr) 바이러스 핵 항원] 1-6, gp75, 사람 파필로마 바이러스(HPV) E6 및 E7, p53, 폐 내성 단백질(LRP), Bcl-2, 및 Ki-67을 포함한다. 또한, 면역원성 분자는 자가면역병의 개시 및/또는 전파에 관여된 자가항원일 수 있으며, 이의 병리학은 주로 관련된 표적 기관, 조직 또는 세포, 예를 들면, SLE 또는 MG에 의해 발현된 분자에 대해 특이적인 항체의 활성에 대부분 기인한다. 이러한 질병에서, 세포성(즉, Th1-유형) 면역 반응으로 관련 자가 항원에 대한 진행중인 항체-매개된(즉, Th2-유형) 면역 반응을 지시하는 것이 바람직할 수 있다. 달리는, 적절한 자가항원에 대해 Th1 반응을 예방학적으로 유도함으로써 관련 자가면역병을 가지지 않지만 이러한 질병에 걸릴 가능성이 있는 것으로 예상되는 대상체에서 자가항원에 대한 Th2 반응의 수준을 감소시키거나 발병을 예방하는 것이 바람직할 수 있다. 흥미있는 자가항원은 (a) SLE와 관련하여, 스미쓰(Smith) 단백질, RNP 리보뉴클레오단백질 및 SS-A 및 SS-B 단백질; 및 (b) MG와 관련하여, 아세틸콜린 수용체를 포함하나, 이에 한정되지 않는다. 하나 이상의 유형의 자가면역 반응에 관여된 다른 다양한 항원의 예는 황체형성 호르몬, 여포 자극 호르몬, 테스토스테론, 성장 호르몬, 프롤락틴 및 기타 호르몬과 같은 내인성 호르몬을 포함한다.
자가면역병, 알레르기 및 이식 거부에 관여된 항원도 본 발명의 조성물 및 방법에 사용될 수 있다. 예를 들면, 임의의 하나 이상의 다음 자가면역병 또는 질병에 관여된 항원도 본 발명에 사용될 수 있다: 당뇨병, 진성 당뇨병, 관절염(류마티스 관절염, 소아 류마티스 관절염, 골관절염, 건선 관절염 포함), 다발경화증, 중증 근육무력증, 전신홍반루푸스, 자가면역 갑상선염, 피부염(아토피성 피부염 및 습진성 피부염), 건선, 쇼그렌 증후군(Sjogren's Syndrome)에 대해 2차적인 건조각말결막염을 포함하는 쇼그렌 증후군, 원형탈모증, 절지동물 물림증 반응에 기인한 알레르기 반응, 크론병(Crohn's disease), 아프타 궤양, 홍채염, 결막염, 각막결막염, 궤양대장염, 천식, 알레르기 천식, 피부홍반성루푸스, 공피증, 질염, 직장염, 약물 발진, 나병 역 반응, 나병결절홍반, 자가면역 포도막염, 알레르기성 뇌척수염, 급성괴사출혈뇌척수염, 특발성 양쪽 진행형 감각신경성 난청, 재생불량빈혈, 순수 적혈구 빈혈, 특발성 혈소판감소증, 다발연골염, 베게너육아종증, 만성 활성 간염, 스티븐스-존슨 증후군(Stevens-Johnson syndrome), 특발스프루, 편평태선, 크론병(Crohn's disease), 그레이브스 눈병증(Graves ophthalmopathy), 사르코이드증(sarcoidosis), 원발쓸개관간경화증, 뒤포도막염(uveitis posterior), 및 사이질 폐 섬유증. 자가면역병에 관여된 항원의 예는 글루탐산 데카복실라제 65(GAD 65), 천연 DNA, 미엘린 염기성 단백질, 미엘린 단백질지질 단백질, 아세틸콜린 수용체 성분, 티로글로불린 및 티로이드 자극 호르몬(TSH) 수용체를 포함한다. 알레르기에 관여된 항원의 예는 일본 세다 폴렌 항원(Japanese cedar pollen antigen), 돼지풀 폴렌 항원(ragweed pollen antigen), 라이 그래스 폴렌 항원(rye grass pollen antigen)과 같은 폴렌 항원, 집먼지 진드기 항원 및 소포자균 항원과 같은 동물 기원한 항원, 조직적합성 항원 및 페니실린 및 기타 치료학적 약물을 포함한다. 이식 거부에 관여된 항원의 예는 심장, 폐, 간, 췌장, 신장 및 신경 이식체 성분과 같은 이식체 수용체내로 이식될 이식체의 항원 성분을 포함한다. 항원은 자가면역병을 치료하는데 유용한 변경된 펩타이드 리간드일 수 있다.
본원에 사용된 용어 "에피토프(들)"는 병원체 DNA 또는 RNA에 의해 암호화된 임의의 다수의 병원체 폴리펩타이드내에 위치한 에피토프와 유사한 일차, 이차 또는 삼차 구조를 포함하는 펩타이드 또는 단백질 항원을 말한다. 유사성의 수준은 일반적으로 이러한 폴리펩타이드에 대해 지시된 모노클로날 또는 폴리클로날 항체가 또한 펩타이드 또는 단백질 항원에 결합하거나, 반응하거나 또는 인지할 정도일 것이다. 각종 면역검정 방법을 예를 들면, 모두 당해 분야의 숙련가들에게 익히 공지된 웨스턴 블롯팅(Western blotting), ELISA, RIA 등과 함께 사용할 수 있다. 백신에서 사용하기에 적합한, 병원체 에피토프 및/또는 이들의 작용성 등가물의 확인은 본 발명의 일부이다. 일단 분리하여 확인되면, 작용성 등가물을 용이하게 수득할 수 있다. 예를 들면, 본원에서 참조로 인용한 것으로서, 친수성을 기초로 하여 아미노산 서열로부터 에피토프를 확인하고 제조하는 것을 교시하고 있는 미국 특허 제4,554,101호에서 교시하고 있는 바와 같은 호프(Hopp)의 방법을 사용할 수 있다. 몇몇 다른 논문에 기술된 방법, 및 이를 기초로 한 소프트웨어 프로그램을 또한 사용하여 에피토프 코어 서열을 확인할 수 있다(참조: 예를 들면, Jameson and Wolf, 1988; Wolf et al., 1988; 미국 특허 제4,554,101호). 이들 "에피토프 코어 서열"의 아미노산 서열은 이후에, 펩타이드 합성 또는 재조합 기술의 적용을 통해 펩타이드내로 용이하게 혼입시킬 수 있다.
본원에 사용된 용어 "프로모터"는 전사의 개시 및 전사율이 조절되는 핵산 서열의 영역인 조절 서열을 기술하고 있다. 이는, 조절 단백질 및 분자가 RNA 폴리머라제 및 기타 전사 인자와 같이 결합할 수 있는 유전 성분을 함유할 수 있다. 어절 "작동가능하게 위치한", "작동가능하게 연결된", "조절하에", 및 "전사 조절하에"는, 프로모터가 핵산 서열과 관련하여 정확한 작용 위치 및/또는 배향(즉, ORF)내에 있어 이러한 서열의 전사 개시 및/또는 발현을 조절하는 것을 의미한다. 프로모터는 핵산 서열의 전사 활성화에 관여된 시스-작용의 조절 서열을 언급하는 "인핸서"와 함께 사용되거나 사용되지 않을 수 있다. 본 발명과 함께 사용될 수 있는 프로모터 및/또는 인핸서의 목록은 예를 들면, 관련 기술 및 표가 본원에 참조로 인용된 미국 특허 제6,410,241호에 기술되어 있다.
본원에 사용된 용어 "세포", "세포주" 및 "세포 배양물"은 상호교환적으로 사용될 수 있다. 이들 용어 모두는 또한 생체내, 생체외 또는 시험관내에서 임의의 및 모든 후속 세대인 이들의 후대를 포함한다. 모든 후대는 고의적인 또는 비고의적인 돌연변이로 인하여 동일하지 않을 수 있다. 이종 핵산 서열의 발현과 관련하여, "숙주 세포"는 원핵 세포 또는 진핵 세포를 말하며, 이는 본 발명의 rAb 단백질 벡터를 사용하여 전달된 것으로서의 벡터에 의해 암호화된 이종 유전자를 발현할 수 있는 임의의 형질전환가능한 유기체를 포함한다. 숙주 세포는 벡터의 수용체로서 사용될 수 있고, 사용되어 왔다. 숙주 세포는 "형질감염"되거나 "형질전환"될 수 있으며, 이는, 본원에 기술된 것으로서 항원을 발현하는 외인성 핵산이 숙주 세포내로 이동되거나 도입되는 과정을 말한다. 형질전환된 세포는 주요 대상체 세포 및 이의 후대를 포함한다.
활성 성분으로서 본 발명의 항원을 암호화하는 핵산을 포함하는 백신 조성물의 제제는 액체 용액 또는 현탁액; 형질감염 전에 용액 또는 현탁액에 적합한 고체 형태로 제조될 수 있으며, 감염 전에 액체가 또한 제조될 수 있다. 제제는 유화되거나 리포좀 속에 봉입될 수 있다. 활성의 면역원성 성분은 흔히 약제학적으로 허용되며 활성 성분과 혼용성인 담체와 혼합된다.
용어 "약제학적으로 허용되는 담체"는 투여받는 대상체에서 알레르기 반응 또는 기타 원치않은 효과를 유발하지 않는 담체를 말한다. 적합한 약제학적으로 허용되는 담체는 예를 들면, 하나 이상의 물, 염수, 포스페이트 완충된 염수, 덱스트로즈, 글리세롤, 에탄올 등 및 이들의 조합을 포함한다. 또한, 경우에 따라, 백신은 습윤제 또는 유화제와 같은 소량의 보조 물질, pH 완충제 및/또는 백신의 효능을 향상시키는 애주번트를 함유할 수 있다. 효과적일 수 있는 애주번트의 예는 수산화알루미늄, N-아세틸-무라밀-L-트레오닐-D-이소글루타민(thr-MDP), N-아세틸-노르-무라밀-L-알라닐-D-이소글루타민, MTP-PE 및 2% 스쿠알렌/트윈 80 유액 속에 세균, 모노포스포릴 지질 A, 트레할로즈 디마이콜레이트 및 세포벽 골격(MPL+TDM+CWS)로부터 추출된 3개 성분을 함유하는 RIBI를 포함하나, 이에 한정되지 않는다. 애주번트의 다른 예는 DDA(디메틸디옥타데실암모늄 브로마이드), 프로인트 완전 및 불완전 애주번트 및 QuilA를 포함한다. 또한, 림포카인(예를 들면, IFN-γ, IL-2 및 IL-12) 또는 폴리 I:C와 같은 합성 IFN-γ 유도인자를 본원에 기술된 애주번트와 함께 사용할 수 있다.
약제학적 제품은 본 발명에 기술된 바와 같이 혈장 지단백질상에 존재하는 아포리포단백질의 특이적인 DNA-결합 부위에 결합한 특이적인 뉴클레오타이드 서열의 단일 또는 다수 카피를 지닌 네이키드(naked) 폴리뉴클레오타이드를 포함할 수 있다. 폴리뉴클레오타이드는 생물학적으로 활성인 펩타이드, 안티센스 RNA 또는 리보자임을 암호화할 수 있으며 생리학적으로 허용되는 투여가능한 형태로 제공될 것이다. 본 발명으로부터 도출될 수 있는 다른 약제학적 제품은 환자 혈액 또는 다른 공급원으로부터 본원에 기술된 방법에 따라 분리된 고도로 정제된 혈장 지단백질 분획, 및 생리학적으로 허용되는 투여가능한 형태로 정제된 지단백질에 예비결합된, 혈장 지단백질 상에 존재하는 아포지단백질의 특이적인 DNA-결합 부위에 결합한 특이적인 뉴클레오타이드 서열의 단일 또는 다수 카피를 함유하는 폴리뉴클레오타이드를 포함할 수 있다.
또 다른 약제학적 제품은 생리학적으로 허용되는 투여가능한 형태 속에 특이적인 뉴클에오타이드 서열의 단일 또는 다수 카피를 함유하는 폴리뉴클레오타이드에 예비결합된 특이적인 DNA-결합 모티프의 단일 또는 다수 카피를 함유하는 재조합 아포지단백질 단편을 함유하는 고도로 정제된 혈장 지단백질 분획을 포함할 수 있다. 또 다른 약제학적 제품은 생리학적으로 허용되는 투여가능한 형태 속에 특이적인 뉴클레오타이드 서열의 단일 또는 다수의 카피를 함유하는 폴리뉴클레오타이드에 예비결합된, 특이적인 DNA-결합 모티프의 단일 또는 다수의 카피를 함유하는 재조합 아포지단백질 단편을 함유하는 고도로 정제된 혈장 지단백질 분획을 포함할 수 있다.
투여될 용량은 치료하는 대상체의 체중 및 생리학적 상태, 및 투여 경로 및 치료 횟수에 크게 의존한다. 고도로 정제된 지단백질 분획에 예비결합된 네이키드 폴리뉴클레오타이드를 포함하는 약제학적 조성물은 1㎍ 내지 1 mg의 폴리뉴클레오타이드 및 1㎍ 내지 100 mg의 단백질 범위의 양으로 투여될 수 있다.
환자에 대한 치료학적 바이러스 입자의 투여는 경우에 따라, 벡터의 독성을 고려하여, 화학치료제의 투여를 위한 일반적인 프로토콜에 따를 것이다. 치료 주기는 경우에 따라 반복될 수 있는 것으로 기대된다. 각종의 표준 치료요법, 및 외과 수술도 기술된 유전자 치료요법과 함께 적용될 수 있는 것으로 또한 여겨진다.
유전자 치료요법의 임상적 적용이 고려되는 경우, 요구된 적용에 적절한 약제학적 조성물로서 복합체를 제조하는 것이 요구될 수 있다. 일반적으로 이는 병원체 및 사람 또는 동물에 유해할 수 있는 다른 임의의 불순물이 본질적으로 부재하는 약제학적 조성물을 제조하는 것을 포함할 것이다. 또한 일반적으로 표적 세포에 의해 복합체의 흡수를 허용하고 복합체가 안정하도록 하는 완충제와 적절한 염을 사용하는 것이 바람직할 것이다.
본 발명의 수성 조성물은 약제학적으로 허용되는 담체 또는 수성 매질 속에 용해되거나 분산된 유효량의 화합물을 포함할 수 있다. 이러한 조성물은 또한 접종물(inocula)로서 언급될 수 있다. 약제학적 활성 물질용의 이러한 매질 및 제제의 사용은 당해 분야에 잘 알려져 있다. 임의의 통상적인 매질 또는 제제가 활성 성분과 비혼화성인 경우를 제외하고, 치료학적 조성물 속에서 이의 용도가 고려된다. 보충적인 활성 성분을 또한 조성물내로 혼입시킬 수 있다. 본 발명의 조성물은 전통적인 약제학적 제제를 포함할 수 있다. 분산제는 또한 글리세롤, 액체 폴리에틸렌 글리콜 및 이의 혼합물 및 오일 속에서 제조할 수 있다. 저장 및 사용의 통상적인 조건하에서, 이들 제제는 미생물의 성장을 방지하기 위한 방부제를 함유한다.
질병 상태. 치료될 특정 질병에 따라, 본 발명에 따른 치료학적 조성물의 투여는, 표적 조직이 최대(또는 일부 경우에 최소) 면역 반응을 위한 부위로 항원의 전달을 최대화하기 위하여 이러한 경로를 통해 이용가능한 한 어떠한 통상의 경로를 통해서도 이루어질 수 있다. 투여는 일반적으로 동소이식, 피내, 피하, 근육내, 복강내 또는 정맥내 주사에 의해 이루어질 것이다. 전달을 위한 기타 부위는 경구, 비강, 볼내, 직장, 질내 또는 국소를 포함한다. 국소 투여는 피부암의 치료시 특히 유리할 수 있다. 이러한 조성물은 일반적으로 생리학적으로 허용되는 담체, 완충제 또는 기타 부형제를 포함하는 약제학적으로 허용되는 조성물로서 투여될 수 있다.
본 발명의 백신 또는 치료 조성물은 비경구적으로, 주사에 의해, 예를 들면, 피하 또는 근육내 투여될 수 있다. 다른 투여 유형에 적합한 추가의 제형은 좌제, 및 일부 경우에, 경구 제형 또는 에어로졸과 같이 분산에 적합한 제형을 포함한다. 경구 제형의 경우에, 애주번트를 사용하는 T-세포 서브세트의 조작, 항원 패키징 또는 개개의 사이토카인의 각종 제형으로의 첨가는 면역 반응이 최적화된 개선된 경구 백신을 생성한다. 좌제의 경우, 전통적인 결합제 및 담체는 예를 들면, 폴리알킬렌 글리콜 또는 트리글리세라이드를 포함할 수 있으며, 이러한 좌제는 0.5% 내지 10%, 바람직하게는 1% 내지 2% 범위의 활성 성분을 함유하는 혼합물로부터 형성될 수 있다. 경구 제형은 예를 들면, 약제학적 등급의 만니톨, 락토즈, 전분 마그네슘 스테아레이트, 나트륨 사카린, 셀룰로즈, 탄산마그네슘 등으로서 일반적으로 사용된 부형제를 포함한다. 이들 조성물은 용제, 현탁제, 좌제, 정제, 환제, 캅셀제, 서방성 제형 또는 산제의 형태를 취할 수 있으며 10% 내지 95%의 활성 성분, 바람직하게는 25 내지 70%를 함유한다.
본 발명의 핵산을 암호화하는 항원은 중성 또는 염 형태로서 백신 또는 치료 조성물로 제형화될 수 있다. 약제학적으로 허용되는 염은 산 부가 염(펩타이드의 유리 아미노 그룹과 함께 형성됨)을 포함하며, 이는 예를 들면, 염산 또는 인산과 같은 무기산, 또는 아세트산, 옥살산, 타르타르산, 말레산 등과 같은 유기산과 함게 형성된다. 유리 카복실 그룹과 함께 형성된 염은 또한 예를 들면, 나트륨, 칼륨, 암모늄, 칼슘 또는 철 하이드로이드(ferric hydroide)와 같은 무기 염기 및 이소프로필아민, 트리메틸아민, 2-에틸아미노 에탄올, 히스티딘, 프로카인 등과 같은 유기 염기로부터 기원할 수 있다.
백신 또는 치료 조성물은 용량 제형과 혼용성인 방식으로 및 예방학적으로 및/또는 치료학적으로 효과적일 양으로 투여된다. 투여될 양은 항체를 합성하기 위한 대상체의 면역 시스템의 능력, 및 목적한 보호 또는 치료 정도를 포함하는, 치료되는 대상체에 따른다. 적합한 용량 범위는 백신화당 활성 성분 수백 마이크로그램의 정도에서 약 1mg 내지 300mg의 범위 및 바람직하게는 약 10mg 내지 50mg의 범위와 같이 약 0.1mg 내지 1000mg의 범위이다. 초기 투여 및 부스터 투여(booster shot)에 적합한 방법은 또한 변할 수 있으나 초기 투여 후 후속적인 접종 또는 다른 투여로 전형화되어 있다. 투여되는 활성 성분의 정확한 양은 의료인의 판단에 따르며 각각의 대상체마다 특징적일 수 있다. 본 발명의 핵산 분자 또는 융합 폴리펩타이드의 치료학적 유효량은, 핵산 분자 또는 융합 폴리펩타이드가 다른 치료제와 함께 투여되는지에 상관없이, 특히 투여 스케줄, 투여된 항원의 단위 투여량, 수용자의 면역 상태 및 건강, 및 특정 핵산 분자 또는 융합 폴리펩타이드의 치료학적 활성에 의존할 것임은 당해 분야의 숙련가에게 익숙할 것이다.
조성물은 단일 투여량 스케줄 또는 다수 투여량 스케줄로 제공될 수 있다. 다수 투여량 스케줄은, 백신화의 주요 과정이 예를 들면 1 내지 10회의 별개 투여량에 이어, 면역 반응을 유지시기고/시키거나 보강하는데 요구되는 후속적인 시간 간격, 예를 들면, 2번째 투여량의 경우 1 내지 4개월 째에 제공된 다른 투여량, 및 경우에 따라 수개월 후 후속적인 투여량(들)인 스케줄이다. 1 내지 5년의 간격, 일반적으로 3년 간격의 주기적인 부스터가 보호 면역성의 바람직한 수준을 유지하는데 바람직할 수 있다. 면역화의 과정은 ESAT6 또는 ST-CF와 함께 공동-배양된 말초혈 림프구(PBL)의 시험관내 증식 검정에 의해서, 및 초회민감 림프구로부터 방출된 IFN-γ의 수준을 측정함으로써 수반될 수 있다. 이들 기술은 당해 분야의 숙련가에게 공지되어 있으며, 본원에 관련 부분이 참조로 인용된 미국 특허 제3,791,932호, 제4,174,384호 및 제3,949,064호에서 찾을 수 있다.
모듈러 rAb 운반체 및/또는 접합된 rAb 운반체-(코헤신/도커린 및/또는 도커린-코헤신)-항원 복합체(rAb-DC/DC-항원 백신)은, 핵산 벡터가 사용되고, 최종의 정제된 단백질 또는 최종 백신 형태가 사용되는지에 따라 하나 이상의 "단위 투여량"으로 제공될 수 있다. 단위 투여량은 이의 투여, 즉, 적절한 경로 및 치료 요법과 함께 바람직한 반응을 생산하도록 계산된 치료학적 조성물의 예정된-양을 함유하는 것으로 정의된다. 투여될 양, 및 특정 경로 및 제형은 임상 분야의 숙련가의 기술내에 있다. 치료될 대상체는 또한 특히, 대상체의 면역 시스템 및 바람직한 보호의 상태에 대해 평가될 수 있다. 단위 투여량은 1회 주입으로 투여될 필요는 없으나 일정 기간에 걸친 연속 주입을 포함할 수 있다. 본 발명의 단위 투여량은 편리하게는 체중 kg당 DNA(또는 단백질)의 측면에서 약 0.05, 0.10, 0.15, 0.20, 0.25, 0.5, 1, 10, 50, 100, 1,000 mg 이상/DNA 또는 단백질/kg체중의 범위로 투여된다. 유사하게, 전달된 rAb-DC/DC-항원 백신의 양은 약 0.2 내지 약 8.0 mg/kg의 체중으로 변할 수 있다. 따라서, 특정 양태에서, 0.4 mg, 0.5 mg, 0.8 mg, 1.0 mg, 1.5 mg, 2.0 mg, 2.5 mg, 3.0 mg, 4.0 mg, 5.0 mg, 5.5 mg, 6.0 mg, 6.5 mg, 7.0 mg 및 7.5 mg의 백신이 생체내에서 개체에게 전달될 수 있다. 투여될 rAb-DC/DC-항원 백신의 용량은 치료되는 대상체의 체중 및 생리학적 상태, 및 투여 경로 및 치료 횟수에 크게 의존한다. 리포좀 또는 바이러스 전달 벡터에 예비결합된 네이키드 폴리뉴클레오타이드를 포함하는 약제학적 조성물은 1㎍ 내지 1mg의 폴리뉴클레오타이드 내지 1㎍ 내지 100mg의 단백질의 범위의 양으로 투여될 수 있다. 따라서, 특정 조성물은 독립적으로 1㎍, 5㎍, 10㎍, 20㎍, 3.0㎍, 40㎍ 50㎍, 60㎍, 70㎍, 80㎍, 100㎍, 150㎍, 200㎍, 250㎍, 500㎍, 600㎍, 700㎍, 800㎍, 900㎍, 1 mg, 1.5 mg, 5 mg, 10 mg, 20 mg, 30 mg, 40 mg, 50 mg, 60 mg, 70 mg, 80 mg, 90 mg 또는 100 mg의 벡터에 결합된 약 1㎍, 5㎍, 10㎍, 20㎍, 30㎍, 40㎍, 50㎍, 60㎍, 70㎍, 80㎍, 100㎍, 150㎍, 200㎍, 250㎍, 500㎍, 600㎍, 700㎍, 800㎍, 900㎍ 또는 1,000㎍의 폴리뉴클레오타이드 또는 단백질을 포함할 수 있다.
본 발명은 Flu 항원이 표적화된 수지상 세포에 의해 사람 Flu-특이적인 T 세포의 면역 자극을 측정하는 시험관내 세포 시스템 속에서 시험되었다. 본원에 나타낸 결과는, 당해 시스템속에서 자체로는 효과적이지 않은 항원의 투여량에서 이러한 항원 특이적인 세포의 특이적 확장을 입증한다.
본 발명은 또한 예를 들면 리신, 안트락스 독소 및 스타필로코쿠스 B 장독소로부터의 보호성 항원과 복합체화된 재조합 사람 mAb(특이적인 사람 수지상 세포 수용체에 대해 지시된)인 모듈러 rAb 운반체를 제조하는데 사용될 수 있다. 당해 실체에 대한 잠재적인 시장은 이들 제제와 관련된 임의의 생물위협(biotreat)에 대한 반응시 거대 집단 중심에 투여하기 위해 저장기에 유지된 저장된 백신 및 모든 군인의 백신화이다. 본 발명은 일반적으로 사람 및 동물 용도 둘다에서 백신의 설계에 광범위하게 적용된다.
본 발명의 하나의 상업적인 적용은 Ab 중쇄를 통해 보호성 항원을 암호화하는 것으로 공지되어 있거나 예상되는 항원에 융합된 재조합 사람화된 mAb(특이적인 사람 수지상 세포 수용체 DCIR에 대해 지시된)이다. 이들은 각종 제제에 대한 백신화의 예로서- 인플루엔자 H5N1으로부터의 헤마글루티닌; 리신, 안트락스 독소 및 스타필로코쿠스 B 장독소로부터의 약독화된 독소로부터의 HIV gag; 흑색종 항원으로부터의 항원성 펩타이드의 '스트링(string)' 등을 포함한다. 이러한 실체에 대한 잠재적인 시장은 감염 위험이 있거나 감염된 사람의 예방학적 또는 치료학적 백신화이다. 본 발명은 사람 및 동물용 둘다로 많은 질병 및 암에 대한 백신화에 적용된다. 흥미있는 산업은 제약 및 생명공학이다. 또한, 본 발명은 재조합 항체의 분비를 향상시키기 위해 특히 우수한 서열을 확인하는 방법을 기술하고 있으므로 항-DCIR 적용을 능가하는 영향을 갖는다.
조작된 재조합 모노클로날 항체를 제조하기 위한 항-DCIR 결합 영역의 적용은 강력한 치료학적 또는 예방학적 백신화 제제로서 항원에 융합되었다. 이들을 찾기위한 동일한 결합 특이성에 대한 상이한 V-영역 서열의 사용은 H 쇄 C-말단 결합된 항원 또는 다른 단백질 서열의 효과적인 발현에 가장 적합하다.
실시예 1. 복합체 속에서 동일한 조작된 사람화된 mAb(MATCHMAB)과 동시에 표적화된 다수의 항원
예상된 치료학적(당해의 경우, 백신화) 실체의 하나의 유형은 사람화된 DC-표적화된 mAb-항원 융합 단백질이며, 여기서, 항체 가변성 영역 특이성은 내부화 사람 수지상 세포 수용체에 대해 지시된다. 당해 분야의 현재 상태는 목적한 항원의 mAb H 쇄의 C-말단에 대한 융합물을 조작하는 것이다. 이러한 사고는 상이한 항원(A1, A2, A3)이 동일한 입증된 표적화 mAb 골격(하기 도면에서 Y)에 대해 조작되도록 함으로써, 상이한 병원성 제제에 대해 면역화하는 하나의 mAb의 유용성을 확장시킨다. 이러한 개념은 예를 들면, IgGFc C-말단 암호화 영역에 말단-대-말단으로 융합된 A1, A2, A3 암호화 영역을 조작함으로써 추가로 확장시킬 수 있다.
본 발명은 표적화 mAb에 항원을 연결시키는 새로운 사고를 기술하고 있으며, 이러한 사고는 복합체 속에서 최초로 동일한 조작된 사람화된 mAb(MATCHMAB)와 동 시에 표적화된 다수의 항원에 대한 개념을 확장시킨다.
도 1은 복합체 속에서 동일한 조작된 사람화된 mAb (MATCHMAB)(하부 부위)와 동시에 표적화된 다수의 항원의 예와 선행 기술(상부 부위)을 비교한다. Y는 사람화된 항-DC 표적화 mAb를 나타내며; A1, A2, A3는 독립적인 보호성 항원 또는 임의의 다른 바람직한 단백질 도메인이고; C1, C2, C2는 각각 도킹 도메인(docking domain) D1, D2, D3에 대한 특이적인 고 친화성 포획 도메인이고; DnAn은 상응하는 도킹-항원 융합 단백질이다. 각종 도메인은 일정한 비율로 그려지지 않았음에 주목한다. mAb 자체는 약 150 kDa이고, C는 약 17 Da이며, D는 약 8 kDa이고 A는 변하나, 일반적으로 >20 kDa이다.
MATCHMAB는 모듈러 비-공유 표적화 mAb-항원 복합체를 형성하기 위한 셀룰로좀-어셈블리 코헤신-도커린 서열의 사용을 기초로 한다. 비교적 작고 특이적인 코헤신-도커린 단백질-단백질 상호작용 도메인은, 단순한 통상의 제형이 mAb-항원 복합체를 표적화하도록 할 수 있다. 따라서, 단일 제조된 사람화된 mAb(상기 표기에서 Y.C1.C2.C3.Cn)은, 다양하지만 엄격하게 정의된 조합으로 다수 항원을 전달하는 기준으로서 사용될 수 있다.
C1.C2.C3.Cn을 암호화하는 서열의 예는 셀룰로좀 앵커 스캐폴딘 B 전구체(cellulosomal anchoring scaffoldin B precursor)[박테로이데스 셀룰로솔벤스(Bacteroides cellulosolvens)]의 공지된 서열 >gi│50656899│gb│AAT79550.1│로부터 취해진다. 하기 청색 부분은 리더 분비 서열을 나타내고, 황색 및 회색은 각종 코헤신 도메인을 강조한다. 적색 영역은 코헤신 도메인의 일부를 띄우는 링 커이다.
코헤신 도메인(C)는 도커린(D)라고 불리는 소 도메인(예를 들면, 56개 잔기)와 상호작용한다. 2중 대칭을 갖는 Ca++ 함유 구조가 존재하며 이들은 상이한 친화성(예를 들면, 6E6M, 2E7M)으로 유사한 코헤신에 결합할 수 있다. 도커린과 다수의 코헤신[스캐폴딘(scaffoldin) 상에서 발견된 것으로서]사이의 친화성은 훨씬 클 수 있다(예를 들면, >E9 M). 상호작용은 비-공유결합성이며 적어도 하나의 C-D 쌍에 대해 구조 분석에 의해 잘 정의되어 있다. 도커린은 상이한 도메인(천연적으로 효소)에 연결된 도메인이 되도록 설계되며, 코헤신은 [직접 말단-대-말단으로, 또는 다양한 크기(예를 들면, 12, 17, 25, 28, 36)의 유연한 PT-풍부한 링커에 의해 결합된] 선형 배열로 작용하도록 설계된다. 특정 도커린은 특정 코헤신에 대해 특이성을 지닐 수 있음은 알려져 있다(예를 들면, 하나의 세균 종으로부터의 C-D 쌍은 상이한 종으로부터의 C-D 쌍과 상호교환가능하지 않을 수 있다). 이러한 특징은, 각종 D-항원 융합 단백질과 다양한 특이성의 코헤신 도메인을 함유하는 조작된 mAb의 특이적이고 정밀한 상호작용을 보장할 수 있다.
실제로, 본 발명은 문헌으로부터 공지되거나, 자연으로부터 새로이 발견되거나 파지 디스플레이 기술을 사용하여 새로운 특이성을 지니도록 개발된 C-D 쌍을 채택하는 것을 포함한다. 후자의 기술을 또한 사용하여 C-D 상호작용의 ('성숙한') 친화성을 향상시킬 수 있으며, 이것이 바람직하다. 또한, C-D 상호작용(공지된 C-D 구조로부터의 모델링을 기준으로)의 반대 면에서 시스테인 잔기의 조작을 사용하여 C-D사이에 공유 결합을 제조함으로써 상호작용을 강력하게 할 수 있다. 또한, mAb의 이량체성 특성(및 따라서 연결된 C-도메인)을 사용하여 친화성 향상 목적에 유리하게 할 수 있다. 당해 양태에서, 예를 들면, D-항원 융합 단백질은 제2의 동일한 도커린 도메인(D-항원-D, 또는 D-D-항원), 또는 동종이량체화 도메인을 사용하여 조작된다. 도메인 사이의 링커가 강제적이지 않았던 경우, 이러한 구성은 동일한 mAb에 대해 D 도메인 둘다의 바람직한 동시 결합을 생성시킬 것이고, 단일 상호작용과 비교하여 안정성을 현저히 향상시킬 것이다.
코헤신-도커린 복합체의 결정 구조를 기초로 하여(예를 들면, 문헌: PNAS 2003,13809-13814, Cellulosome assembly revealed by the crystal structure of the cohesin-dockerin complex. Ana L. Carvalho*, Fernando M. V. Dias, Jose A. M. Prates, Tibor Nagy, Harry J. Gilbert, Gideon J. Davies, Luis M. A. Ferreira, Maria J. Romao and Carlos M. G. A. Fonte), 하나의 양태는 항원-도커린 융합 단백질(즉, 도커린의 N-말단에 융합된 항원)임이 명백하다. 그러나, 구조로부터 및 스캐폴딘내 코헤신 도메인 조직화의 특성 둘다로 부터, 코헤신이 스페이서 서열의 부재하에서도 말단-대-말단으로 융합될 수 있음이 명백하다. 또한, 잘-기술된 기술이 코헤신 및 도커린 도메인의 소형화된 버젼을 조작하는데 유용함이 명백하다(참조: 예를 들면, Proc. Natl. Acad. Sci. USA Vol. 94, pp. 10080-10085, September 1997. Structural mimicry of a native protein by a minimized binding domain. Melissa A. Starovasnik, Andrew C. Braisted, And James A. Wells).
본원에서 링커 서열이 ST 풍부성으로부터 초래되는 O-연결된 글리코실화에 대한 경향성을 가짐은 인지되어 있다. 또한, C 및 D 도메인 둘다는 잠재적인 N-연결된 부위를 가질 수 있다. 이러한 특징은 탄수화물을 사용한 장식을 통해 포유동물 세포-발현된 조작된 mAb의 가용성을 향상시키는데 있어 유리할 수 있다. 물론, C 도메인의 글리코실화의 결과는 작용(유사한 D에 결합하는)에 의해 점검할 필요가 있으며, 경우에 따라 부위 지시된 돌연변이유발로 수정할 필요가 있다. 본 발명의 매력적인 특징은, D-A가 우수한 것으로 익히 공지된 어떠한 시스템에서도 발현될 수 있다는 것이다. 예를 들면, 종양 항원 MART1은 막 단백질이며 이.콜라이 봉입체를 통해 높은 수율로 잘 제조된다. mAb에 직접 융합된 항원을 사용한 설계는 포유동물-세포 발현에 적합한 항원으로 제한된다.
본 발명의 다른 양태는 테일-대-테일로 결합된 이-특이적인 mAb를 제조하기 위해 D-C 상호작용을 사용하는 것이다. 도 2는 이-특이적인 mAb를 형성하기 위한 본 발명의 용도를 나타낸다. mAb1(검은색)은 C-말단 C1으로 나타내며 mAb2(자홍색)는 C-말단 D1으로 나타낸다. 등몰의 mAb1 및 mAb2의 혼합으로 이-특이적인 1:1 복합체가 생성될 것이다. 각각의 mAb 분자는 2몰 당량의 C 또는 D를 함유하므로(mAb 자체는 이량체성 구조이다), 이-특이적인 mAb는 2개의 동시발생하는 C-D 상호작용에 의해 크게 안정화될 것이다. 특히 낮은 (mAb)에서, 이는 가장 안정한 배열일 것이다.
실시예 2. 항체 및 코헤신/도커린 도메인 및 항원의 조합
실시에 2는, 특정 코헤신과 도커린 도메인이 특이적이고 높은 친화성 코헤신-도커린 단백질-단백질 상호작용을 유지하면서, 융합 단백질로서 포유동물 세포로부터 성공적으로 효율적으로 분비될 수 있음을 나타낸다. 비록 심도있는 코헤신-도커린 문헌이, 이러한 융합 단백질이 이러한 작용성을 가져야 하는 예측을 교시하고 있다고 해도, 포유동물 분비 시스템에서 이러한 융합 단백질의 생산을 기술하고 있지 않다. 현 과학 지식의 상태는 발견을 예측할 수 없도록 하는데, 이는 성공적인 분비에 대한 규칙(시그날 펩타이드와 같은 특징외에)이 성공적으로 확립되어 있지 않기 때문이다. 또한, 코헤신 링커 영역은 자체의 천연 세균내에서 글리코실화되는 것으로 공지되어 있으며, 코헤신 및 도커린 도메인은 예측된 글리코실화 부위를 함유한다. 비록 이것이 실제로 포유동물 세포로부터의 분비를 선호한다고 해도, '인공적인' 글리코실화가 코헤신-도커린 상호작용을 파괴할지는 명백하지 않 다.
각종 상업적 적용을 위한 코헤신-도커린 상호작용이 공지되어 있지만, 본 발명은, 이러한 상호작용에 대한 앞서의 인지되지 않은 용도가 예측되고 조절된 어셈블리 효소 적용과 관련되지 않은 특이적인 단백질 복합체를 어셈블리하는 것을 중심으로 제조한다는 것에 기초한다.
본 발명은 다양한 셀룰로즈 분해 미생물로부터의 모든 코헤신-도커린 서열의 사용을 포함하나, 미생물 클로스트리디움 써모셀룸(Clostridium thermocellum)으로부터의 링커 서열 및 특이적인 코헤신 및 도커린의 적용을 기술한다. 예를 들면, 표 1에 기술된 서열은 클로스트리디움 써모셀룸 도커린 서열(rAb.doc로 명명)에 C-말단 코돈에서 연결된 사람 IgG4의 H쇄를 암호화한다. rAb.doc 단백질의 다른 양태는 표 2에서 유사하게 기술되어 있으며 이들은 상이한 H쇄 실체를 암호화하는 벡터에 DNA 단편으로 도커린 암호화 영역을 단순히 이전시킴에 의해 조작된다.
표 1은 rAB-pIRES2(hIgG4H-도커린) 또는 C52.DNA(전체 암호화 영역)의 핵산 및 아미노산 서열을 나타내며 사람 IgG4H.doc 융합 단백질의 아미노산 서열(예측된 분비된 생성물)이 하기 나타나 있다. 도커린 도메인(클로스트리디움 써모셀룸으로부터 취함) celD는 황색으로 강조되어 있고 H 쇄 및 도커린 결합 서열은 밑줄쳐져 있다. 도커린 도메인내 고도로 예측된 N-결합된 글리코실화 부위는 적색으로 강조되어 있다.
표 2는 rAB-pIRES2(mAnti-DCIR2C9H-LV-hIgG4H-C-도커린) 또는 C82에 대한 핵산 및 아미노산 서열을 나타낸다. DNA(전체 암호화 영역) 및 아미노산 서열(예측된 분비된 생성물)이 하기 나타나 있다. 도커린 도메인은 황색으로 강조되어 있고 H 쇄 및 도커린 결합 서열은 밑줄쳐져 있다. IgG 가변 영역은 청색으로 강조되어 있다. 도커린 도메인내 고도로 예측된 N-결합된 글리코실화 부위는 적색으로 강조되어 있다.
표 3은 rAB-(mAnti-ASGPR_49C11_7H-SLAML-V-hIgG4H-C-도커린) 또는 C153에 대한 핵산 및 아미노산 서열을 나타낸다. DNA(전체 암호화 영역) 및 아미노산 서열(예측된 분비된 생성물)은 하기 나타낸다. 도커린 도메인은 황색으로 강조되어 있고, H 쇄 및 도커린 결합 서열은 밑줄쳐져 있다. IgG 가변 영역은 청색으로 강조되어 있다. 도커린 도메인내 고도로 예측된 N-결합된 글리코실화 부위는 적색으로 강조되어 있다.
표 4는 rAB-pIRES2(mAnti-DC-SIGNL16E7H-LV-hIgG4H-C-도커린) 또는 C92에 대한 핵산 및 아미노산 서열을 나타낸다. DNA(전체 암호화 영역) 및 아미노산 서열(예측된 분비된 생성물)은 하기 나타낸다. 도커린 도메인은 황색으로 강조되어 있고, H 쇄 및 도커린 결합 서열은 밑줄쳐져 있다. IgG 가변 영역은 청색으로 강조되어 있다. 도커린 도메인내 고도로 예측된 N-결합된 글리코실화 부위는 적색으로 강조되어 있다.
이러한 rAb.doc IgG H 쇄 단백질을 암호화하는 포유동물 발현 플라스미드를 표준 분자 생물학 기술로 생성하여 pIRES2-DsRed2[제조원: 비디 바이오사이언시즈(BD Biosciences)]와 같은 시판되는 발현 플라스미드 벡터의 기초가 될 수 있다. 분비된 rAb.doc를 생산하기 위해, 포유동물 세포를 발현 플라스미드 및 상보성 IgG L 쇄를 암호화하는 발현 플라스미드(표 3에 예시)로 공동-형질감염시킨다. 표준 프로토콜(예를 들면, FreeStyleTM 293 발현 시스템, 제조원: 인비트로젠(Invitrogen))을 포유동물 세포, 형질감염 시약 및 배양 배지용으로서 사용한다. 형질감염된 세포를 3 내지 7일 동안 배양하고 배양 상청액을 원심분리로 수거하고, 여과로 정화하고, rAB.doc 단백질을 단백질 G 친화성 크로마토그래피에 의해 컬럼 제조업자[지이 파마시아(GE Pharmacia)]로부터의 프로토콜을 사용하여 정제한다.
도 3은 쿠마시 브릴리언트 블루로 염색하여 SDS.PAGE로 환원시킴에 의한 대표적인 분비된 rAb.doc 생성물의 분석을 나타낸다. 당해 분석은, rAb.doc가 분비된 H+L 쇄 이량체로서 효율적으로 생산됨을 나타낸다. H 쇄내 이종성은 도커린 서열내에서 고도로 예측된(가능성 0.6426, NetNGlyc 1.0 서버 - 덴마크의 테크니컬 유니버시티(Technical University)) 부위에서 N-연결된 글리코실화를 반영한다.
표 5는 rAB-pIRES2(mAnti-DC-SIGNL16E7K-LV-hIgGK-C) 또는 C73에 대한 핵산 및 아미노산 서열을 나타낸다. mAnti-DC-SIGNL16E7 하이브리도마(청색으로 강조)로부터의 V 영역이 사람 C 영역(황색으로 강조)에 융합된 IgG 카파 단백질의 DNA(전체 암호화 영역) 및 아미노산 서열(예측된 분비된 생성물).
도 3은 SDS.PAGE 및 쿠마시 브릴리언트 블루 염색으로 환원시킴으로써 분석한 단백질 G 친화성 정제된 분비된 rAb 단백질을 나타낸다.
본 발명은 글리코실화와 관련된 것으로 익히 공지된 바람직한 가용성 및 약력학적 특성을 포유동물 세포-분비된 도커린 융합 단백질상에 부여하는 당해 글리코실화 부위의 예측가능하지 않은 존재 및 용도를 구현한다. 도 2는, 동일한 IgG H 및 L 서열을 사용하는 rAb.항원 융합 단백질이 분비 효율에 있어서 현저히 상이할 수 있음을 나타낸다. 양쪽 측면의 예에서, rAb.doc 실체는 대표적으로 매우 불량하게 발현하는 인플루엔자 HA5 서열에 융합된 rAb와 비교하여 잘 발현된다. 본 발명은 또한 관련된 rAb 실체의 분비를 현저히 방해하지 않는 도커린 도메인의 예측치못한 능력을 구현한다. 또한, 본 발명은 rAb 특이적인 항원 결합 영역의 작용성을 방해하지 않은 도커린 도메인의 특성을 구현한다. 이러한 특성은 IgFc 반응성과, 항-LOX1_15C4 rAb 단백질 및 항-LOX1_15C4.doc사이의 LOX-1 반응성사이의 조화를 나타내는 도 5에서 예시된다.
도 4A 및 4B는 각종 rAb.융합 단백질의 분비 수준의 항-사람 IgFc ELISA에 의한 측정을 나타낸다. 2.5㎍의 각각의 H 및 L 쇄 발현 플라스미드를 293F 세포내로 형질감염시키고 상청액 샘플의 2배 희석물을 3일 배양 후에 시험하였다. Y 축 값은 임의의 HRP 활성이다.
도 5는 분비된 항-LOX1_15C4 rAb(청색 기호) 및 항-LOX1_15C.doc rAb(적색 기호) 단백질의 항-사람 IgFc ELISA(HRP 활성) 및 LOX-1.알칼린 포스파타제 결합(AP 활성)에 의한 측정을 나타낸다. 총 5㎍의 H 및 L 쇄 발현 플라스미드의 상이한 비를 293F 세포내로 형질감염시키고 상청액 샘플을 3일 배양 후에 시험하였다.
본 발명은 hIgG4 및 이의 밀접한 유도체외에 융합 단백질 측면에서 효율적으로 및 작용적으로 발현된 도커린 도메인의 특성을 구현한다. 예를 들면, 표 6은 마우스 IgG2b H 쇄 융합 단백질을 기초로 rAb.doc 실체의 서열을 나타낸다.
표 6은 rAB-pCMV(mIgG2bH-도커린) 또는 C19에 대한 핵산 및 아미노산 서열을 나타낸다. DNA(전체 암호화 영역) 및 아미노산 서열(예측된 분비된 생성물)이 나타나 있다. 도커린 도메인은 황색으로 강조되어 있고 H 쇄 및 도커린 결합 서열은 밑줄쳐져 있다. 도커린 도메인내 고도로 예측된 N-연결된 글리코실화 부위는 적색으로 강조되어 있다.
도 6은, mIgG 카파 발현 플라스미드로 공동-형질감염시키는 경우, rAB-pCMV(mIgG2bH-도커린) 플라스미드가 rAB-mIgG2b.도커린 융합 단백질의 효율적인 분비를 지시함을 나타낸다. 도 6에서, 단백질 G 친화성 정제된 rAb 단백질이 환원 SDS.PAGE 및 쿠마시 블루 염색에 의해 분석된 형질감염된 293 F 세포로부터 분비되었다. 레인 11 및 12는 mIgG2b.doc 생성물을 나타낸다.
상기 상세된 rAb.doc 발명의 용도는 도커린-코헤신 상호작용의 특이성 및 강인성을 통한 rAb-항원 또는 독소 또는 활성화제 또는 효소 복합체의 어셈블리이다. 표 5는 코헤신.알칼린 포스파타제 융합 단백질(coh.AP)의 형태인 본 발명의 하나의 양태를 나타낸다. 또한 2개의 코헤신 도메인(coh.coh.AP)을 함유하는 알칼린 포스파타제 융합 단백질과 같은 추가의 양태가 기술되어 있으며, 다른 단백질은 사람 전립선 특이적인 항원의 성숙한 서열과 같은 다른 서열에 융합된 단일 코헤신 도메인(coh.hPSA) 및 인플루엔자 A HA5의 HA1 도메인 융합된 단일 코헤신 도메인(coh.Flu HA5-1)과 같은 본 발명의 일반성의 예이다.
표 7은 Mam-pCDM8(코헤신-SLAML-AP-6xHis) 또는 C16에 대한 핵산 및 아미노산 서열을 나타낸다. DNA(전체 암호화 영역) 및 아미노산 서열(예측된 분비된 생성물)이 하기 나타나 있다. 코헤신 도메인은 황색으로 강조되어 있고 코헤신 및 알칼린 포스파타제 결합 서열은 밑줄쳐져 있다. 코헤신 도메인내 고도로 예측된(G-score > 0.5, NetOGlyc 3.1 서버 - 덴마크의 테크니컬 유니버시티) O-연결된 글리코실화 부위 및 코헤신 도메인에서 원거리에 있는 링커가 적색으로 강조되어 있다. 회색으로 강조된 잔기는 금속 친화성 크로마토그래피를 통해 정제를 촉진시키는 C-말단 His 태그이다.
표 8은 Mam-pCDM8(코헤신-코헤신-SLAML-AP-6xHis) 또는 C17에 대한 핵산 및 아미노산 서열을 나타낸다. DNA(전체 암호화 영역) 및 아미노산 서열(예측된 분비된 생성물)이 하기 나타나 있다. 코헤신 도메인은 황색으로 강조되어 있고 코헤신 및 알칼린 포스파타제 결합 서열은 밑줄쳐져 있다. 코헤신 도메인내 고도로 예측된 O-연결된 글리코실화 부위 및 코헤신 도메인에서 원거리에 있는 링커가 단일의 고도로 예측된 N-말단 글리코실화 부위(NPT)에서와 같이 적색으로 강조되어 있다. 회색으로 강조된 잔기는 금속 친화성 크로마토그래피를 통해 정제를 촉진시키는 C-말단 His 태그이다.
표 9는 Mam-pCDM8(SLAML-코헤신-hPSA) 또는 C149에 대한 핵산 및 아미노산 서열을 나타낸다. DNA(전체 암호화 영역) 및 아미노산 서열(예측된 분비된 생성물)이 하기 나타나 있다. 코헤신 도메인은 황색으로 강조되어 있고 코헤신 및 hPSA 결합 서열은 밑줄쳐져 있다. 코헤신 도메인에서 원거리에 있는 링커내 고도로 예측된 O-연결된 글리코실화 부위 및 코헤신 도메인내 단일의 고도로 예측된 N-연결된 글리코실화 부위가 적색으로 강조되어 있다.
표 10은 Mam-pCDM8(SLAML-코헤신-FluHA5-1-6xHis) 또는 C24에 대한 핵산 및 아미노산 서열을 나타낸다. DNA(전체 암호화 영역) 및 아미노산 서열(예측된 분비된 생성물)이 하기 나타나 있다. 코헤신 도메인은 황색으로 강조되어 있고 코헤신 및 Flu HA5-1 결합 서열은 밑줄쳐져 있다. 코헤신 도메인에서 원거리에 있는 링커내 고도로 예측된 O-연결된 글리코실화 부위 및 코헤신 도메인내 단일의 고도로 예측된 N-결합된 글리코실화 부위는 적색으로 강조되어 있다. 회색으로 강조된 잔기는 금속 친화성 크로마토그래피를 통해 정제를 촉진시키는 C-말단 His 태그이다.
위에서 언급한 rAb.doc 작제물과 유사하게, 본 발명은 작용성 코헤신 융합 단백질(본원에서 coh.융합체로 명명)의 포유동물 세포로부터의 효율적인 분비를 구현한다. 코헤신 도메인이 도커린-결합 작용을 유지하면서 성공적으로 분비될 수 있는지는 명백하지 않았다. 도 5는, 분비된 coh.알칼린 포스파타제(coh.AP)를 함유하는 상청액이 플라스틱 표면상에 고정된 rAb.doc 단백질에 특이적으로 결합함을 입증한다.
도 7A 및 7B는, 분비된 알칼린 포스파타제(AP) 또는 coh.AP를 암호화하는 발현 플라스미드가 형질감염된 293F 세포로부터 작용성 단백질의 분비를 지시하였음을 나타낸다. 3일 배양 후, 상청액을 수거하여 96웰 미세-역가 플레이트에 결합된 0.25㎍의 rAb.doc(상부 패널) 또는 rAb(하부 패널)에 결합하는 이들의 능력에 대해 시험하였다. 항온처리 1시간 후, 플레이트를 세척하고 발색성 AP 기질을 사용하여 발색시켰다.
본 발명은 코헤신.도커린 상호작용을 기초로 특이적인 단백질 복합체 어셈블리의 적용을 구현한다. 특이적인 항체.항원 복합체를 또한 단백질 A 또는 단백질 G IgFc 결합 도메인의 확립된 상호작용을 사용하여 어셈블리할 수 있다. 본 발명은 예를 들면 IgG와의 단백질 G 상호작용과 비교하여 현저히 우수한 복합체 형성을 생성하는 코헤신.도커린 상호작용의 고유 특성을 구현한다. 도 6 및 7에서 코헤신.AP (Coh.AP로 명명) 단백질의 상호작용은 rAb.Doc 단백질에 특이적임이 밝혀졌다.
도 8A 및 8B는, 분비된 G.AP를 함유하는 상청액의 각종 희석물을 0.25㎍의 고정화된 mIgG2a, mIgG2b, 또는 mIgG2b-계 rAb.doc을 함유하는 미세-역가 웰 속에서 1시간 동안 항온처리하였음을 나타낸다. 세척 후 결합된 AP 활성을 발색성 AP 기질을 사용하여 발색시켰다. proG.AP는 rAb.doc에 결합하지 않았는데, 이는 proG.AP 작제물에서 사용된 특정 단백질 G 도메인과 상호작용하지 않는 mIgG2b의 동형 변이체였기 때문이다.
도 8B는 동일한 연구를 나타내지만 분비된 Coh.AP를 함유하는 상청액의 희석물을 사용하였다. Coh.AP는 단지 rAb.doc에만 결합하며, coh.doc 상호작용의 특이적을 다시 입증한다.
도 9는 proG.IgGFc 상호작용과 비교하여 coh.doc 상호작용을 기초로 예비어셈블리된 복합체의 가장 우수한 안정성을 입증한다. 도 9는 고정된 양의 proG.AP 또는 coh.AP 또는 coh2.AP (0.1 ug) 및 고정화된 mIgG2b 또는 rAb.doc (0.25 ug)사이의 복합체의 형성이 미세-역가 플레이트 속에서 1시간 동안 항온처리함에 의해 어셈블리되었음을 나타낸다. 다양한 시각에, 20배 과량의 가용성 mIgG2b 또는 rAb.doc를 가하고 다양한 시간 동안 계속 항온처리하였다. 이후에, 플레이트를 세척하고 결합된 AP 활성을 발색성 AP 기질을 첨가하여 평가하였다.
당해 실시예는, 혈청(예를 들면, 조직 배양 배지 및 생체내 투여)을 함유하는 셋팅에서 이러한 coh.doc 복합체의 용도를 나타낸다. 도 10은 이러한 셋팅에서 proG.IgGFc 복합체와 비교하여 coh.doc 복합체의 현저한 우수성을 입증한다. 사용된 조건하에서, 약 15 ug/ml Ig는 결합된 proG.AP를 완전히 교체하는데 충분하였으나, coh.AP는 순수한 혈청(15 mg/ml Ig)의 존재하에서도 rAb.doc에 안정하게 결합된 채로 잔존하였다.
도 10은 고정량의 proG.AP 또는 coh.AP (0.1 ug) 및 고정화된 mIgG2b 또는 rAb.doc(0.25 ug) 사이의 복합체의 형성이 미세-역가 플레이트 속에서 1시간 동안 항온처리함에 의해 어셈블리되었음을 나타낸다. 사람 혈청의 다양한 희석물을 가하고 4시간 동안 계속 항온처리하였다. 이후에, 플레이트를 세척하고 결합된 AP 활성을 발색성 AP 기질을 첨가하여 평가하였다.
본 발명은 또한 완전한 복합체 형성을 보장하는 생산 과정을 허용하고 coh.융합 단백질 실체를 위한 정제 과정과 동시에 일어날 수 있는 coh.doc 상호작용의 특정 용도를 구현한다. 본 발명은 도 11 및 12에 예시되어 있으며, 이는 단백질 G 친화성 크로마토그래피에 이어 단백질 G:rAb.doc 컬럼에 의한 배양 상청액으로부터의 coh.항원의 포획에 의해 배양 상청액으로부터 rAb.doc의 연속적인 포획을 통한 당해 과정을 나타낸다. 이후 낮은 pH를 사용한 용출은 순수한 rAb.doc:coh.항원을 방출한다. rAb.doc에 걸쳐 과량의 coh.항원이 존재하는 경우, 충분하고 완벽한 복합체가 생성될 수 있다. 본 발명의 관련 양태는 과도하게 순수하거나 부분적으로 정제된coh.융합 단백질의 단백질 G 포획된 rAb.doc에 대한 적용일 수 있다.
도 11은 동일한 단백질 G 친화성 컬럼에 대한 rAb.doc 상청액 및 coh.AP 상청액의 연속적인 적용에 의해 생산된 rAb.doc:Coh2.AP 복합체의 환원된 SDS.PAGE 분석 대 환원되지 않은 SDS.PAGE 분석의 겔을 도시한다. 레인 2 및 4는, Coh2.AP가 rAb.doc와 함께 공동-정제됨을 나타낸다.
도 12는 동일한 단백질 G 친화성 컬럼에 대한 rAb.doc 상청액 및 coh.Flu HA5-1 상청액의 연속적인 적용으로 생산된 rAb.doc:Coh.Flu HA5-1 복합체의 환원되지 않은 SDS.PAGE 분석이다. 레인 1 내지 4는 좌측에서 우측으로, Coh.Flu HA5-1가 rAb.doc와 공동-정제됨을 나타낸다.
코헤신 도메인의 잘 기술된 특징은 표준 이.콜라이 세균 발현 시스템과의 이들의 혼용성이다. 본 발명은 포유동물 분비 시스템에서 도커린 융합 단백질의 발현의 신규 용도를 구현하며, 이는 또한 coh.doc 복합체의 형성을 포함하고, 여기서, 상이한 성분들(즉, coh 및 doc)은 상이한 시스템내에서 발현된다. 이는 각각의 성분에 대한 가장 우수한 발현 시스템의 사용 가능성을 제공하기 때문에 매우 유리하다. 예를 들면, coh.Flu M1 발현 작제물은 형질감염된 포유동물 세포로부터 분비된 생성물의 합성을 효율적으로 지시하지 못하였다. 그러나, coh.Flu M1은 이.콜라이내에서 가용성 단백질로서 매우 효율적으로 발현되었다. 표 6은 당해 실시예에서 사용된 coh.Flu M1의 서열을 나타낸다.
표 11은 하기 나타낸 이.콜라이-pET28(코헤신-FluM1-6xHis) 또는 C32에 대한 핵산 및 아미노산 서열을 나타낸다. 아미노산 서열에서, 코헤신 도메인은 황색으로 강조되어 있고 코헤신 및 인플루엔자 A M1 단백질사이의 융합 지점은 밑줄쳐져 있다. 회색으로 강조된 잔기는 금속 친화성 크로마토그래피를 통해 정제를 촉진시키는 C-말단 His 태그이다.
본 발명은 각종 치료학적 또는 백신화 목적을 위한 정돈되고 특이적인 복합체를 어셈블리하기 위한 도커린.코헤신 상호작용의 용도를 구현한다. 예는 coh.Flu M1 단백질과 복합체화된 내부화 사람 수지상 세포(DC) 수용체에 대한 결합 특이성을 갖는 rAb.doc의 용도이다. 도 11은 시험관내 연구에 의해 이의 용도를 입증한다. 항-DC_rAb.doc:coh.Flu M1와 함께 배양된 후, 자가 T 세포와 공동-배양된 DC는 Flu M1의 특이적인 기억을 갖는 T 세포의 확장을 지시하였다. 동등한 투여량의 coh.Flu M1만으로는 이러한 효과를 갖지 않았다. 당해 연구는, coh.Flu M1 단독과 비교하여 항-DC_rAb.doc:coh.Flu M1을 통한 Flu M1-특이적인 T 세포 확장의 적어도 50배 향상을 나타낸다.
도 13은, 작용성 항-DC_rAb.doc:coh.Flu M1 복합체가 개개의 정제된 성분들을 혼합함에 의해 형성되었음을 나타낸다. 다양한 양의 복합체 또는 coh.Flu M1 만을 배양 배지 속에서 5E4 사람 DC(HLA201 공여체로부터) 및 10E5 자가 T 세포와 함께 항온배양하였다. 24시간 후, DC를 CD40L로 활성화시키고 추가로 9일 동안 계속 항온배양하였다. 세포를 수거하고 PE-표지된 Flu M1 펩타이드 GILGFVFTL(서열번호 24) HLA-A2 4량체로 염색하고 항원-특이적인 CD8+ 세포의 빈도를 분석하였다.
도 14는 사람 DC에 결합하지 않은 동형-매치된 mAb.doc에 복합체화된 coh.Flu M1의 추가의 조절을 도입한 유사 실시예를 나타낸다. 도 12는, Flu M1 GILGFVFTL 에피토프에 걸치는 펩타이드 단편에의 H 쇄 융합을 통해 직접 연결된 항-DC_rAb가 Flu M1-특이적인 T 세포의 확장을 초래하는 DC 표적화된 항원 전달을 유발하는데 효과적임을 나타낸다. 그러나, 항-DC_rAb.Flu M1 PEP 실체는 포유동물 세포로부터 매우 불량하게 분비되어, 이러한 백신의 생산은 불가능한 것 같았다. 당해 문제는 (이 경우) 백신 항원에 적절한 발현 시스템을 사용함으로써 생산 문제가 해결되도록 하는 본 발명의 양태를 예시한다.
도 14는, 항-DC_rAb.doc:coh.Flu M1 또는 mIgG2b.doc:coh.Flu M1 복합체가 개개의 정제된 성분들을 혼합함에 의해 형성되었음을 나타낸다. 다양한 양의 복합체, 또는 coh.Flu M1 단독을 배양 배지 속에서 5E4 사람 DC(HLA201 공여체로부터) 및 10E5 자가 T 세포와 함께 항온배양하였다. 24시간 후, DC를 CD40L로 활성화시키고 추가로 9일 동안 계속 항온배양하였다. 세포를 수거하고 PE-표지된 Flu M1 펩타이드 GILGFVFTL(서열번호 24) HLA-A2 4량체로 염색하고 항원-특이적인 CD8+ 세포의 빈도에 대해 분석하였다. mIgG2.doc 복합체에 대한 농도는 항-DC_rAb 복합체에 대한 것과 동일하였다.
도 15는, CD34+ 사람 DC가 CD1a+ 및 CD14+ 아형으로 분류되며 3nM 항-DC_rAb.Flu M1 PEP 또는 항-DC_rAb의 존재 및 부재하에 항온배양됨을 나타낸다. 자가 T 세포를 1일 후에 가하고 추가로 8일 동안 계속 항온배양하였다. 분석은 위에서 기술한 바와 같이 수행하였다. CD1a+ 세포는 항-DC_rAb.Flu M1 PEP 처리만을 사용하여 Flu M1-특이적인 CD8+ 세포를 확장시키는데 매우 효과적이었다.
본 발명의 양태의 하나의 유형은 항-DC-rAb.doc:coh.항원 복합체로 구성된 백신이지만, 일부 경우에 바람직한 DC-표적화 백신은 항-DC-rAb.항원일 것이며, 여기서, 항원은 일련의 보호성 항원일 수 있다. 생산 시스템에서 효과적인 발현에 적합한 효율적인 조합에서 이러한 항원의 확인은 매우 문제가 있다. 본 발명의 하나의 양태는 이러한 백신의 개발을 위한 항원 에피토프 조합의 합리화된 시험에 대한 방법을 제공한다. 상세하게는, 본 발명은 목적한 항-DC-rAb.항원의 생산에 초점을 맞추기 위한 예비행위로서 유사 항원 에피토프 단독 또는 조합을 선별하는 방법을 교시한다. 예를 들면, 표 13은 이.콜라이 시스템을 통해 용이하게 발현될 수 있는 예시적인 코헤신.펩타이드 작제물의 서열을 나타낸다. 도 11에 기술된 것과 유사한 기술을 사용하여, coh.pep 단백질의 다양한 수거물을 단일의 항-DC_rAb.doc 실체와의 복합체로서의 효능에 대해 용이하게 시험할 수 있다. 가장 효율적인 coh.pep 화합물은 이후에 항-DC_rAb.펩타이드 융합 단백질로서 직접 조작될 수 있다. 도 16은 이.콜라이내에서 발현된 정제된 coh.PEP 단백질의 예를 나타낸다.
표 12는 흑색종-관련 항원 gp100의 아미노산 서열을 나타낸다. 익히 공지된 HLA-A201-제한된 우성 펩타이드는 음영처리되어 있고 하기에 서열이 상세히 기술되어 있다. M으로 표지된 펩타이드 서열은 HLA-A201에 대한 향상된 친화성을 지닌 변이체이다. C180은 하기 나타낸 서열을 암호화하는 이.콜라이 발현 작제물이며, 여기서, 코헤신 도메인은 청색으로 음영처리되어 있고 gp100 펩타이드는 회색으로 음영처리되어 있다. 펩타이드에 결합하는 밑줄친 잔기는 gp100에 대해 천연적인 것이다. C-말단 His 태그는 금속 친화성 크로마토그래피를 통해 정제를 촉진한다.
하기 나타낸 것은 상기 언급한 gp100 서열 및 관련 펩타이드이다.
HLA-A0201 제한된 펩타이드 서열은 다음과 같다:
GP100 WT: 154-162: KTWGQYWQV (서열번호 26)
GP100 M: 209-217 (2M): IMDQVPFSV (서열번호 27); 209-217 WT: ITDQVPFSV (서열번호 28)
GP100 M: 280-288 (9V): YLEPGPVTV (서열번호 29) 280-288 WT: YLEPGPVTA (서열번호 30)
C180은 이.콜라이-pET28(코헤신-hgp100-펩타이드A-6xHis)이다:
표 13은 흑색종 항원 MART-1의 아미노산 서열을 나타낸다. 익히 공지된 HLA-A201-제한된 우성 펩타이드는 음영처리되어 있고 하기에 서열을 상세히 나타낸다. M 펩타이드는 HLA-A201에 대해 친화성이 향상된 펩타이드 서열을 나타낸다. C181은 하기 나타낸 서열을 암호화하는 이.콜라이 발현 작제물이며, 여기서 코헤신 도메인은 황색으로, MART-1 펩타이드는 회색으로 음영처리되어 있다. 펩타이드에 결합하는 밑줄친 잔기는 MART-1에 대해 천연적이다. C172 및 C174는 항-DC_rAb.MART-1 펩타이드 및 매치하는 대조군 rAb.MART-1 펩타이드 H 쇄의 발현을 지시하는 2개의 작제물이다. C-말단 잔기에 확장된 서열만이 나타나 있다. C-말단 His 태그는 금속 친화성 크로마토그래피를 통해 정제를 촉진한다.
MART-1은 다음과 같다:
HLA-A0201 제한된 펩타이드 서열은 다음과 같다:
C181은 이.콜라이 - pET28(코헤신-hMART-1-펩타이드B-6xHis)이다:
C186은 이.콜라이-pET28(코헤신-Flex-hMART-1-펩타이드A-6xHis)이다:
C172는 rAB-pIRES2(mAnti-ASGPR_49C11_7H-LV-hIgG4H-hMART-1-펩타이드A)이다.
C174는 rAB-pIRES2(hIgG4H-hMART-1-펩타이드A)이다.
도 16은, coh.pep 단백질의 합성을 지시하는 발현 플라스미드를 지닌 이.콜라이가 성장되어 특이적인 단백질 생산을 유도함을 나타낸다. 세포를 수거하고 초음파로 파괴하였다. 상청액 분획을 금속 친화성 크로마토그래피에 적용하여 정제하였다. 분석은 쿠마시 브릴리언트 블루에 의해 염색된 SDS.PAGE 겔을 환원시켜 수행하였다. 도는 좌측에서 우측으로 표지된 대표적인 생성물 coh.pep 단백질을 나타낸다.
당해 실시예는 포유동물 세포로부터 분비된 코헤신 및 도커린 융합 단백질의 성공적인 용도를 나타낸다. 융합 파트너 둘다가 상이한 특이성(즉, rAb1.doc 및 rAb2.coh)을 가진 rAb인 경우, 단순한 혼합으로 이-특이적인 항체인 rAb1.doc:rAb2.coh가 생성된다. 이특이적인 항체는 많은 강력한 치료학적 및 기술적 적용을 갖는다. 본 발명은 doc:coh 상호작용을 통해 이러한 실체를 어셈블리하기 위한 단순하고 예측가능한 수단을 제공한다. 또는, rAb1.doc:rAb1.coh가 어셈블리된 경우, 이러한 실체는 잠재적으로 유일한 생물학적 특성을 갖는 조절되고 가교-결합된 mAb를 나타내었다.
코헤신.도커린 모듈은 다양한 셀룰로즈 분해 종에 존재한다. 이들이 서열 유사성을 가지지만, 이들은 종간 교차되지 않는 특이성을 가질 수 있다. 이는 상이한 특이성을 갖는 코헤신으로 구성된 신규한 스캐폴드를 구성하고 당해 스캐폴드를 사용하여 공간적으로 및 숫자적으로 조절된 방식으로 고 차수의 복합체를 어셈블리하는 기회를 제공한다. 생명공학 적용을 위해 이러한 개념을 사용하기 위한 핵심 기술이 기술되어 있다[참조: Fierobe, H.-P., Mechaly, A., Tardif, C., Belaich, A., Lamed, R., Shoham, Y., Belaich, J.-P., and Bayer, E. A. (2001) Design and production of active cellulosome chimeras: Selective incorporation of dockerin-containing enzymes into defined functional complexes. J. Biol. Chem. 276, 21257-21261.]. 본 발명은 rAb.(doc:coh.fusion)n 복합체(여기서, n은 독특한 특이성을 갖는 doc:coh 상호작용의 >1 쌍을 나타낸다)의 제조와 관련된 적용을 위한 당해 기술의 특이적 사용을 구현한다. 따라서, 본 발명은 rAb.doc1.doc2.doc3. 등 및 coh1.fusionA, coh2.fusionB, coh3.fusion3 등 사이에 부분적으로 정돈된 복합체의 어셈블리(성분들의 단순 혼합에 의해)를 고려한다. coh.fusion 단백질은 상이한 항원, 또는 항원과 사이토카인과 같은 활성화제의 조합을 나타낼 수 있다.
확장에 의해 다수의 coh:doc 특이성을 또한 사용하여 보다 높은 정렬된 항원 특이성을 가진 2가 rAb를 제조할 수 있다. 셀룰로즈 분해 세균 및 유사한 유기체는 또한 분해 기구를 조직화하기 위해 셀룰로즈 결합 도메인(CBD)을 사용한다. 클로스트리디움 써모셀룸으로부터의 CBD의 구조는, N 및 C-말단이 매우 근접하며 CBD 작용성 구조의 필수적인 부분이 아님을 나타낸다. 실제로, CBD는 cipA에서coh.CBD.coh와 같은 다른 도메인에 연결된다. 본 발명은 coh.CBD.coh와 같은 실체를 사용하여 항체 및 다중 서브유닛 수용체를 모방하는 부분적이고 숫적으로 정렬된 복합체를 어셈블리함을 포함한다. 예를 들면, doc1에 융합된 IgG 카파 쇄 v 영역 및 doc2에 연결된 IgG H 쇄 V 영역은 coh1.CBD.coh2과 함께 어셈블리하여 원래의 mAb와 유사한 친화성 및 결합 특이성을 갖는 실체를 수득하기 위한 VL.doc1:coh1.CBD.coh2:VH.doc2를 수득할 수 있다. 이러한 실체는, 예를 들면, 특히 VL 및 VH 성분이 독립적으로 성숙되어 각종 조합의 혼합에 의해 결합될 수 있기 때문에 돌연변이유발 과정을 통해 mAb 특이성을 규정하기 위한 도구를 스크리닝하는데 매우 유용할 수 있다. 위에서 기술한 바와 같이, 당해 기술은 다중 조절된 coh:V.doc 조합에 용이하게 연장시켜 매우 높은 특이성 및 친화성을 갖는 결합 실체를 수득할 수도 있다. 이러한 연장은 예를 들면, cytoR1.doc + cytoR2.doc + cytoR3.doc (여기서, cytoR은 복합체 사이토카인 수용체의 하나의 서브유닛의 외도메인(ectodomain)를 나타낸다)의 어셈블리를 위한 주형으로서 coh1.coh2.CBD.coh3을 사용할 수 있다. 이러한 실체는 복합체 상청액 속에서 사이토카인을 측정하기 위한 생명공학 및 치료요법을 위한 사이토카인 상호작용을 차단하기 위한 용도를 지닐 것이다.
실시예 3. 면역독소 치료요법을 위한 코헤신-도커린 기술의 이용
현재 120만명의 미국인들이 매년 암에 걸리며, 대부분의 암은 이들이 전이되면 치유될 수 없기 때문에, 당해 질병으로부터 약 500,000명이 사망한다. 전이 암에 대한 새로운 치료를 개발하기 위하여, 강력한 세균 독소인, 슈도모나스 외독소 A(PE)를 변형시키는데 유전 공학이 사용됨으로써 정상 세포를 사멸시키는 대신에 이는 암 세포를 선택적으로 사멸시킬 수 있다. PE는 613개의 아미노산으로 구성된 3개의 도메인 단백질이다. 항암제는 이의 결합 도메인(aa 1-252)을 결실시키고 이를 항체의 Fv 단편 또는 암 세포상에 존재하는 항원에 결합하는 성장 인자와 교체함으로써 생산된다. 이들 제제는 재조합 면역독소(RIT)로 불린다. 결장, 유방, 폐 및 기타 상피암(B3(Fv)-PE38) 상의 Ley를 표적하는 RIT, 교아세포종(TGF-alpha-PE38)상에서 과발현된 EGF 수용체를 표적화하는 RIT, 교아세포종(MR-1(Fv)-PE38KDEL) 상에 존재하는 돌연변이체 EGF 수용체를 표적화하는 RIT, 및 많은 T 및 B 세포 백혈병 및 림프종 LMB-2 또는 항-Tac(Fv)-PE38 상에 존재하는 IL-2 수용체를 표적화하는 RIT 및 B 세포 악성종양 상의 CD22를 표적화하는 RIT 및 BL22 또는 RFB4(dsFv)-PE38 난소암 및 중피종(SS1P)을 표적화하는 RIT가 제조되었다. 이들 제제는 다량이 용이하게 정제될 수 있고 독소 자체가 이를 발현하는 포유동물 세포를 사멸시킬 수 있으므로, 이.콜라이내에서 생산된다. 적절한 사람 암 이종이식체를 지닌 마우스에 투여되는 경우, 모든 이들 RIT는 완전한 종양 퇴행을 일으킨다. 대부분의 이들 제제는 현재 사람에게서 임상 시도중에 있으며 몇몇은 암 환자에서 완전한 완화 및 부분적 완화를 일으켰다.
이상적인 면역독소는 매우 활성이어서 소량만이 암 퇴행을 유발하는데 요구되고 안정적이어서 종양 내부에 이르는데 요구되는 5 내지 10시간 동안 작용성이고, 비면역원성이어서 반복적으로 제공될 수 있어야 한다. 초기에, 재조합 면역독소는 PE (도메인 II 및 III)의 아미노산 253-613을 함유하였다. 아미노산 364-395는 활성의 손실없이 제거될 수 있음이 측정되었다. 증가된 안정성은 전체 항체에 독소를 연결시키는 것에 의해 해결될 수 있으며, 이는 긴 반감기를 가지는 것으로 알려져 있고 본 발명에서의 기술은 이러한 해결점을 제공한다.
비록 rAb.Doc:Coh.독소 기술이 공지된 암 항원에 적용될 수 있다고 해도, 또한 면역 관리로부터 종양을 피할 수 있는 것으로 예측되는 종양내 DC를 사멸하기 위해 시험할 수 있다. 후자의 경우, 항-DC 독소 치료요법은, 투여된 독소 자체에 대한 면역성의 생성이 제어될 수 있기 때문에(즉 DC 자체는 항원의 흡수 및 프로세싱을 통해 면역 반응을 개시하는데 중요하다. 당해 치료요법에서, 항체를 흡수하는 DC는 사멸하며 항-독소 반응을 일으킬 수 없다), 두배로 유리하다.
프랑켈(Frankel)(참조: Clinical Cancer Research, 8, 942-944, 2002)은 면역독소의 광범위한 적용을 방해하는 문제를 기술하였다. 이는 미스폴딩(misfolding) 오염물이 문제가 되는 이.콜라이 봉입체 발현 물질의 리폴딩(refolding)이 흔히 요구되는 생산 문제를 포함한다. 또한, 이의 표적에 대한 면역독소의 친화성은 흔히 충분한 강도를 수득하기가 어렵다. 본 발명의 근본 기술은 이들 주제 둘다에 초점을 맞추고 있는데 - 첫째로, 본 발명자들은, 코헤신.PE38 융합 단백질이 완전한 작용성 상태(코헤신 및 독소 활성 둘다 완전)로 복합체 리폴딩없이 단순한 생화학 수단에 의해 정제될 수 있는 가용성 단백질로서 이.콜라이내에서 발현됨을 발견하였다. 둘째로, 표적 항원에 대한 고 친화성 모노클로날 항체는 당해 분야의 숙련가에 의해 통상적으로 수득될 수 있다. 어려운 것은 독소와 융합되어 표적 결합에 대해 완전히 작용성인 형태의 항체 가변 영역을 조작하는 것이다. 조작의 일반적 수단(예를 들면, sFv 형태)은 역으로 초기 모노클로날 항체와 비교하여 표적에 대해 친화성의 현저한 손실을 초래한다. rAb.Doc:Coh.독소 기술은 이러한 주제를 극복하여 초기 mAb의 고 친화성 결합 부위(높고 특이적인 결합 활성을 유지하는 마우스 mAb V 영역의 사람화는 당해 분야의 숙련가에게 통상적임을 주목하라), 및 완전한 재조합 hIgG 측면의 긴 반감기 및 비-항원성의 유리한 특성 둘다를 보존하기 위한 수단을 제공한다.
또한, 코헤신.독소는 독립적으로 생산되므로, 독소의 하나의 제형을 환자에게 주사하기 전 성분의 단순 혼합에 의해 임의의 수의 별도로 생산된 표적화 rAb.Doc 단백질에 접합할 수 있다. 이는 제조 및 조사자 개발 시간을 현저히 단순화시킨다. 본 발명에 기술된 기술은 어떠한 독성 및 어떠한 rAb 특이성에도 용이하게 적용가능하다.
rAb.Doc:Coh.독소 기술의 세부사항. pRB 391[파스탄(Pastan) 박사로부터, Pastan, Chief of the Laboratory of Molecular Biology, Division of Basic Sciences. NCI, NIH]을 프라이머 PE38-N3 (cacggtcaccgtctccaaagcttccggagctagcGAGGGCGGCAGCCTGGCCGCGCT (서열번호 39)) 및 PE38-C3 (GGCCGGCTCCTGCGAAGGGAGCCGGCCGGTCGCGGCCGCTTACTTCAGGTCCTCGCGCGGCGGTTTGCCG (서열번호 40))와 함께 PCR용 주형으로서 사용하였다.
앞서 확립된 작제물 C21 또는 이.콜라이-pET28(코헤신-6xHis)내로 클로닝하여 하기 나타낸 아미노산 서열(회색 잔기는 코헤신이고; 황색 잔기는 PE38이며, 코헤신 도메인에 대해 천연적인 링커 서열에 의해 분리되어 있다)에 상응하는 코헤신-PE38을 암호화하는 융합 단백질을 생성하였다.
재조합 Coh.PE38 단백질의 발현 및 정제 - 각각의 1L의 발효물로부터 이.콜라이 세포를 25 ml의 빙냉 50 mM Tris, 1 mM EDTA pH 8.0와 0.1 ml의 프로테아제 억제제 칵테일 II[제조원: 칼바이오켐(Calbiochem)] 속에 재현탁시켰다. 세포를 빙상에서 2x 5분 동안 18의 셋팅(Fisher Sonic Dismembrator 60)으로 5분의 휴식 기간과 함께 초음파처리한 후 17,000 r.p.m.(Sorvall SA-600)에서 20분 동안 4℃에서 회전시킨다. 상청액을 50 mM 트리스, 1mM EDTA pH 8.0 속에 평형화시킨 1 ml의 ANX 세파로즈 컬럼을 통과시키고 완충액 B 속에서 0-1M NaCl 구배로 용출시켰다. 코헤신.PE38을 함유하는 분획을 SDS.PAGE로 확인하고 혼주된 분획을 항-코헤신 mAb 친화성 크로마토그래피를 통해 0.1 M 글라이신 pH 2.7로 용출시키는 정제로 추가 정제하였다.
rAb.Doc 표적화된 Coh.PE38에 의한 사람 DC의 선택적인 사멸 - 사람 DC를 GM-CSF 및 IL-4과 함께 6일 동안 배양함으로써 혈액 단핵구로부터 제조하였다. 이후에, DC를 Coh.PE38 단독, 항-DC-SIGN/L 16E7 rAb.Doc 단독, 항-DCIR 24A5.Doc 단독, 또는 rAb.Docs와 Coh.PE38(1.25 ug/ml의 제제를 가하였다)와 함께 배양하였다. 48시간 후, 세포를 아폽토시스 세포를 검출하는 시약(7-AAD)으로 염색하고 전면 대 측면 스캐터(forward versus side scatter) 및 7-AAD 형광성을 기록하는 FACS에 의해 분석하였다.
도 17은, DCIR.Doc rAb만으로 DC의 생존에 효과가 없음을 나타낸다. 그러나, DC-SIGN/L 단독은 DC에 생존 향상 효과를 가진다(스캐터 분석 및 7-AAD 염색 둘다로 입증됨). 도 18은, Coh.PE38만으로는 7-AAD 기록된 아폽토시스 세포(22.1-29.8%)의 수를 약간 증가시킴을 나타낸다. 그러나, DCIR.Doc를 통한 Coh.PE38 독소의 표적화는 7-AAD 양성 집단을 55.3%까지 증가시켰다. 스캐터 분석은 보다 더 극적으로 생존 DC의 집단 특징의 거의 완전한 상실을 나타내었다. DC-SIGN/L.Doc를 통한 Coh.PE38 독소의 표적화는 7-AAD 양성 집단을 생존 DC 스캐너 집단의 유사한 상실과 함께 53.7%까지 증가시켰다. 그러나, 후자의 결과는 DC-SIGN/L.Doc rAb의 생존 효과 측면에서 고찰되어야 하며, 이는 사멸이 3.1-53.1% 7-AAD 양성으로서 고찰될 수 있음을 의미한다.
다가 항체를 제조하기 위한 코헤신-도커린 기술의 이용. 코헤신 도메인을, 주형으로서 C17 (Mam-pCDM8(코헤신-코헤신-SLAML-AP-6xHis))을 기초로 한 PCR을 사용하여 rAb H 쇄의 C-말단과 프레임내(in-frame)로 조작하였다. 수득되는 분비된 H 쇄 서열을 하기 나타낸다(코헤신 도메인은 회색으로 강조되어 있으며 C-말단 H 쇄 잔기는 굵은 글씨이다):
당해 발현 작제물을 적절한 rAb L 쇄를 사용하여 293F 세포내로 공동-형질감염시키고 분비된 rAb의 발현을 3일 째에 항-hIgGFc ELISA로 평가하였다. 도 19는, 항-DC-SIGN/L 및 항-DC-ASPGR rAb.Coh의 발현물이 효과적으로 분비되었음을 나타내다.
따라서, 코헤신 및 도커린 도메인은 rAb 융합 단백질로서 용이하게 발현된다. 이러한 특성은 2가 항체(즉, 하나의 단백질내에 2개의 상이한 결합 특이성을 갖는)로서 (rAb1.Coh:rAb2.Doc) 복합체의 용도에 필수적이다. 2가 항체는 산업적, 분석적 및 치료학적 적용에 적합한 많은 바람직한 특징을 갖는다. 그러나, 이들은 개발하기가 어렵고 이들을 조작하는데 사용된 분자 기구는 통상적으로 모 모노클로날 항체에 고유한 고 친화성 및 특이성의 바람직한 특성의 질의 떨어뜨린다. (rAb1.Coh:rAb2.Doc) 기술은 이러한 장애를 극복하며 더욱이, 본 출원에 또한 기술되어 있는 바와 같이 쌍 방식의 특이성을 갖는 다수의 코헤신 또는 도커린 스트링을 혼입시킴에 의해 보다 높은(2배 초과) 결합가의 결합력으로 확장가능하다. 또한, 당해 기술은 예를 들면 사이토카인의 사용에 연장시켜 추가의 결합가(즉, rAb1.Doc:Coh.사이토카인)를 제공할 수 있다.
예를 들면, 코헤신 도메인 및 IL-21사이의 융합 단백질을 발현 작제물로서 조작하고 Coh.IL-21 단백질을 일시적으로 형질감염된 293F 세포로부터 효율적으로 분비시키고 연속적인 Q 세파로즈 및 항-코헤신 친화성 크로마토그래피로 용이하게 정제하였다. 분비된 생성물의 서열은 하기 나타내며, 코헤신 도메인은 회색으로, IL-21 도메인은 황색으로 나타낸다. 당해 생성물은 사람 B 세포의 증식을 유지하는 효능에 의해 측정된 것으로서 완전히 작용성이었다.
Mam-pCDM8(SLAML-코헤신-hIL-21)
따라서, rAb.Doc:Coh.IL-21은 동시적 증식 및 활성화 시그날을 B 세포에 전달할 수 있다(즉, rAb 자체가 활성화 특성을 갖는 경우). 이러한 주목은 특정 세포 유형 및 동일한 세포 유형에 지시된 활성을 갖는 임의의 사이토카인에 지시된 생물학적 특성을 갖는 어떠한 rAb에도 연장시킬 수 있다. 도 20은 사람 B 세포의 증식에 미치는 IL-21 및 Coh.IL-21의 효과를 나타낸다.
본 명세서에서 논의된 어떠한 양태도 본 발명의 어떠한 방법, 키트, 시약 또는 조성물과 관련하여 실시될 수 있으며, 역으로도 가능함이 고려된다. 또한, 본 발명의 조성물은 본 발명의 방법을 달성하기 위해 사용될 수 있다.
본원에 기술된 특정 양태는 예시로서 나타낸 것이며 본 발명을 제한하는 것이 아님은 이해될 것이다. 본 발명의 근본 특징은 본 발명의 범위로부터 벗어남이 없이 각종 양태에서 사용될 수 있다. 당해 분야의 숙련가들은 본원에 기술된 특정 과정에 대해 통상의 수준을 벗어나지 않는 실험을 사용하여, 다수의 등가물을 인지하거나 확인할 수 있을 것이다. 이러한 증가물은 본 발명의 범위내에 속하는 것으로 고려되며 청구의 범위에 의해 포함된다.
명세서에서 언급된 모든 공보 및 특허원은 본 발명이 속한 당해 분야의 숙련가의 기술 수준의 지표이다. 모든 공보 및 특허원은 본원에서 각각의 개개 공보 또는 특허원이 참조에 의해 인용되는 것으로 구체적으로 및 개별적으로 나타내어진 것과 동일한 정도로 참조로 인용된다.
청구의 범위 및/또는 명세서에서 용어 "포함하는"과 함께 사용되는 경우, 단어 "a" 또는 "an"의 사용은 "하나"를 의미할 수 있으나, 이는 또한 "하나 이상", "적어도 하나" 및 "하나 또는 하나 이상"의 의미와 일치한다. 청구의 범위에서 용어 "또는"의 사용은, 비록 기술이 단지 대안 및 "및/또는"만을 언급하는 정의를 지지한다고 해도, 대안만을 또는 대안이 서로 배타적임을 명백하게 지적하지 않는 한, "및/또는"을 의미하기 위해 사용된다. 당해 명세서 전체를 통해, 용어 "약"은, 값이 장치, 당해 값을 측정하는데 사용되는 방법 또는 연구 대상체 중에 존재하는 변화에 대한 고유의 오차 변화를 포함함을 나타내기 위해 사용된다.
당해 명세서 및 청구의 범위에 사용된 용어 "포함하는"(및 포함하는의 임의의 형태, 예를 들면 "포함하다"), "갖는"(및 갖는의 임의의 형태, 예를 들면, "갖다"), "포함하는"(및 포함하는의 임의의 형태, 예를 들면, "포함하다") 또는 "함유하는"(및 함유하는의 임의의 형태, 예를 들면, "함유하다")는 포괄적이고 개방적이며 추가의, 인용하지 않은 요소 또는 방법 단계를 배제하지 않는다.
본원에 사용된 용어 "또는 이들의 조합(물)"은 용어 앞부분의 나열된 항목의 모든 순열 및 조합을 말한다. 예를 들면, "A, B, C, 또는 이들의 조합"은 A, B, C, AB, AC, BC, 또는 ABC 중 적어도 하나, 및 특정 문맥에서 순서가 중요한 경우, 또한 BA, CA, CB, CBA, BCA, ACB, BAC, 또는 CAB를 포함하는 것으로 의도된다. 당해 예와 연속하여 BB, AAA, MB, BBC, AAABCCCC, CBBAAA, CABABB 등과 같은 하나 이상의 항목 또는 용어의 반복을 함유하는 조합도 분명히 포함된다. 당해 분야의 숙련가들은, 내용으로부터 달리 명백하지 않는 한, 임의의 조합에서 항목 또는 용어들의 수에 제한이 없음을 이해할 것이다.
본원에 기술되고 청구된 조성물 및/또는 방법 모두는 본 기술의 측면에서 과도한 실험없이 제조되고 실행될 수 있다. 본 발명의 조성물 및 방법은 바람직한 양태의 특면에서 기술되어 있지만, 당해 분야의 숙련가에게는, 변형들이 본 발명의 개념, 취지 및 범위로부터 벗어남이 없이 본원에 기술된 조성물 및/또는 방법 및 방법의 단계 또는 단계들의 순서에 적용될 수 있음이 명백할 것이다. 당해 분야의 숙련가에게 명백한 모든 이러한 유사한 치환 및 변형은 첨부된 청구의 범위에 의해 정의되는 본 발명의 취지, 범위 및 개념내에 있는 것으로 고려된다.
<110> Baylor Research Institute
<120> Multivariable antigens complexed with targeting humanized
monoclonal antibody
<130> BHCS:2094
<150> US 60/888,029
<151> 2007-02-02
<160> 43
<170> KopatentIn 1.71
<210> 1
<211> 2299
<212> PRT
<213> Bacteroides cellulosolvens
<400> 1
Met Gln Ser Pro Arg Leu Lys Arg Lys Ile Leu Ser Val Ile Leu Ala
1 5 10 15
Val Cys Tyr Ile Ile Ser Ser Phe Ser Ile Gln Phe Ala Ala Thr Pro
20 25 30
Gln Val Asn Ile Ile Ile Gly Ser Ala Gln Gly Ile Pro Gly Ser Thr
35 40 45
Val Lys Val Pro Ile Asn Leu Gln Asn Val Pro Glu Ile Gly Ile Asn
50 55 60
Asn Cys Asp Phe Thr Ile Lys Phe Asp Ser Asp Ile Leu Asp Phe Asn
65 70 75 80
Ser Val Glu Ala Gly Asp Ile Val Pro Leu Pro Val Ala Ser Phe Ser
85 90 95
Ser Asn Asn Ser Lys Asp Ile Ile Lys Phe Leu Phe Ser Asp Ala Thr
100 105 110
Gln Gly Asn Met Pro Ile Asn Glu Asn Gly Leu Phe Ala Val Ile Ser
115 120 125
Phe Lys Ile Lys Asp Asn Ala Gln Lys Gly Ile Ser Asn Ile Lys Val
130 135 140
Ser Ser Tyr Gly Ser Phe Ser Gly Met Ser Gly Lys Glu Met Gln Ser
145 150 155 160
Leu Ser Pro Thr Phe Phe Ser Gly Ser Ile Asp Val Ser Asp Val Ser
165 170 175
Thr Ser Lys Leu Asp Val Lys Val Gly Asn Val Glu Gly Ile Ala Gly
180 185 190
Thr Glu Val Asn Val Pro Ile Thr Phe Glu Asn Val Pro Asp Asn Gly
195 200 205
Ile Asn Asn Cys Asn Phe Thr Leu Ser Tyr Asp Ser Asn Ala Leu Glu
210 215 220
Phe Leu Thr Thr Glu Ala Gly Asn Ile Ile Pro Leu Ala Ile Ala Asp
225 230 235 240
Tyr Ser Ser Tyr Arg Ser Met Glu Gly Lys Ile Lys Phe Leu Phe Ser
245 250 255
Asp Ser Ser Gln Gly Thr Arg Ser Ile Lys Asn Asp Gly Val Phe Ala
260 265 270
Asn Ile Lys Phe Lys Ile Lys Gly Asn Ala Ile Arg Asp Thr Tyr Arg
275 280 285
Ile Asp Leu Ser Glu Leu Gly Ser Phe Ser Ser Lys Gln Asn Asn Asn
290 295 300
Leu Lys Ser Ile Ala Thr Gln Phe Leu Ser Gly Ser Val Asn Val Lys
305 310 315 320
Asp Ile Glu Ser Ser Val Ser Pro Thr Thr Ser Val His Pro Thr Pro
325 330 335
Thr Ser Val Pro Pro Thr Pro Thr Lys Ser Ser Pro Gly Asn Lys Met
340 345 350
Lys Ile Gln Ile Gly Asp Val Lys Ala Asn Gln Gly Asp Thr Val Ile
355 360 365
Val Pro Ile Thr Phe Asn Glu Val Pro Val Met Gly Val Asn Asn Cys
370 375 380
Asn Phe Thr Leu Ala Tyr Asp Lys Asn Ile Met Glu Phe Ile Ser Ala
385 390 395 400
Asp Ala Gly Asp Ile Val Thr Leu Pro Met Ala Asn Tyr Ser Tyr Asn
405 410 415
Met Pro Ser Asp Gly Leu Val Lys Phe Leu Tyr Asn Asp Gln Ala Gln
420 425 430
Gly Ala Met Ser Ile Lys Glu Asp Gly Thr Phe Ala Asn Val Lys Phe
435 440 445
Lys Ile Lys Gln Ser Ala Ala Phe Gly Lys Tyr Ser Val Gly Ile Lys
450 455 460
Ala Ile Gly Ser Ile Ser Ala Leu Ser Asn Ser Lys Leu Ile Pro Ile
465 470 475 480
Glu Ser Ile Phe Lys Asp Gly Ser Ile Thr Val Thr Asn Lys Pro Ile
485 490 495
Val Asn Ile Glu Ile Gly Lys Val Lys Val Lys Ala Gly Asp Lys Ile
500 505 510
Lys Val Pro Val Glu Ile Lys Asp Ile Pro Ser Ile Gly Ile Asn Asn
515 520 525
Cys Asn Phe Thr Leu Lys Tyr Asn Ser Asn Val Leu Lys Tyr Val Ser
530 535 540
Asn Glu Ala Gly Thr Ile Val Pro Ala Pro Leu Ala Asn Leu Ser Ile
545 550 555 560
Asn Lys Pro Asp Glu Gly Ile Ile Lys Leu Leu Phe Ser Asp Ala Ser
565 570 575
Gln Gly Gly Met Pro Ile Lys Asp Asn Gly Ile Phe Val Asn Leu Glu
580 585 590
Phe Gln Ala Val Asn Asp Ala Asn Ile Gly Val Tyr Gly Leu Glu Leu
595 600 605
Asp Thr Ile Gly Ala Phe Ser Gly Ile Ser Ser Ala Lys Met Thr Ser
610 615 620
Ile Glu Pro Gln Phe Asn Asn Gly Ser Ile Glu Ile Phe Asn Ser Ala
625 630 635 640
Gln Thr Pro Val Pro Ser Asn Thr Glu Val Gln Thr Pro Thr Asn Thr
645 650 655
Ile Ser Val Thr Pro Thr Asn Asn Ser Thr Pro Thr Asn Asn Ser Thr
660 665 670
Pro Lys Pro Asn Pro Leu Tyr Asn Leu Asn Val Asn Ile Gly Glu Ile
675 680 685
Ser Gly Glu Ala Gly Gly Val Ile Glu Val Pro Ile Glu Phe Lys Asn
690 695 700
Val Pro Asp Phe Gly Ile Asn Asn Cys Asp Phe Ser Val Lys Tyr Asp
705 710 715 720
Lys Ser Ile Phe Glu Tyr Val Thr Tyr Glu Ala Gly Ser Ile Val Lys
725 730 735
Asp Ser Ile Val Asn Leu Ala Cys Met Glu Asn Ser Gly Ile Ile Asn
740 745 750
Leu Leu Phe Asn Asp Ala Thr Gln Ser Ser Ser Pro Ile Lys Asn Asn
755 760 765
Gly Val Phe Ala Lys Leu Lys Phe Lys Ile Asn Ser Asn Ala Ala Ser
770 775 780
Gly Thr Tyr Gln Ile Asn Ala Glu Gly Tyr Gly Lys Phe Ser Gly Asn
785 790 795 800
Leu Asn Gly Lys Leu Thr Ser Ile Asn Pro Ile Phe Glu Asn Gly Ile
805 810 815
Ile Asn Ile Gly Asn Val Thr Val Lys Pro Thr Ser Thr Pro Ala Asp
820 825 830
Ser Ser Thr Ile Thr Pro Thr Ala Thr Pro Thr Ala Thr Pro Thr Ile
835 840 845
Lys Gly Thr Pro Thr Val Thr Pro Ile Tyr Trp Met Asn Val Leu Ile
850 855 860
Gly Asn Met Asn Ala Ala Ile Gly Glu Glu Val Val Val Pro Ile Glu
865 870 875 880
Phe Lys Asn Val Pro Pro Phe Gly Ile Asn Asn Cys Asp Phe Lys Leu
885 890 895
Val Tyr Asp Ser Asn Ala Leu Glu Leu Lys Lys Val Glu Ala Gly Asp
900 905 910
Ile Val Pro Glu Pro Leu Ala Asn Leu Ser Ser Asn Lys Ser Glu Gly
915 920 925
Lys Ile Gln Phe Leu Phe Asn Asp Ala Ser Gln Gly Ser Met Gln Ile
930 935 940
Glu Asn Gly Gly Val Phe Ala Lys Ile Thr Phe Lys Val Lys Ser Thr
945 950 955 960
Ala Ala Ser Gly Ile Tyr Asn Ile Arg Lys Asp Ser Val Gly Ser Phe
965 970 975
Ser Gly Leu Ile Asp Asn Lys Met Thr Ser Ile Gly Pro Lys Phe Thr
980 985 990
Asp Gly Ser Ile Val Val Gly Thr Val Thr Pro Thr Ala Thr Ala Thr
995 1000 1005
Pro Ser Ala Ile Val Thr Thr Ile Thr Pro Thr Ala Thr Thr Lys
1010 1015 1020
Pro Ile Ala Thr Pro Thr Ile Lys Gly Thr Pro Thr Ala Thr Pro
1025 1030 1035
Met Tyr Trp Met Asn Val Val Ile Gly Lys Met Asn Ala Glu Val
1040 1045 1050
Gly Gly Glu Val Val Val Pro Ile Glu Phe Asn Asn Val Pro Ser
1055 1060 1065
Phe Gly Ile Asn Asn Cys Asp Phe Lys Leu Val Tyr Asp Ala Thr
1070 1075 1080
Ala Leu Glu Leu Lys Asn Val Glu Ala Gly Asp Ile Ile Lys Thr
1085 1090 1095
Pro Leu Ala Asn Phe Ser Asn Asn Lys Ser Glu Glu Gly Lys Ile
1100 1105 1110
Ser Phe Leu Phe Asn Asp Ala Ser Gln Gly Ser Met Gln Ile Glu
1115 1120 1125
Asn Gly Gly Val Phe Ala Lys Ile Thr Phe Lys Val Lys Ser Thr
1130 1135 1140
Thr Ala Thr Gly Val Tyr Asp Leu Arg Lys Asp Leu Val Gly Ser
1145 1150 1155
Phe Ser Gly Leu Lys Asp Asn Lys Met Thr Ser Ile Gly Ala Glu
1160 1165 1170
Phe Thr Asn Gly Ser Ile Thr Val Ala Ala Thr Ala Pro Thr Val
1175 1180 1185
Thr Pro Thr Val Asn Ala Thr Pro Ser Ala Ala Thr Pro Thr Val
1190 1195 1200
Thr Pro Thr Ala Thr Ala Thr Pro Ser Val Thr Ile Pro Thr Val
1205 1210 1215
Thr Pro Thr Ala Thr Ala Thr Pro Ser Val Thr Ile Pro Thr Val
1220 1225 1230
Thr Pro Thr Ala Thr Ala Thr Pro Ser Ala Ala Thr Pro Thr Val
1235 1240 1245
Thr Pro Thr Ala Thr Ala Thr Pro Ser Val Thr Ile Pro Thr Val
1250 1255 1260
Thr Pro Thr Val Thr Ala Thr Pro Ser Asp Thr Ile Pro Thr Val
1265 1270 1275
Thr Pro Thr Ala Thr Ala Thr Pro Ser Ala Ile Val Thr Thr Ile
1280 1285 1290
Thr Pro Thr Ala Thr Ala Lys Pro Ile Ala Thr Pro Thr Ile Lys
1295 1300 1305
Gly Thr Pro Thr Ala Thr Pro Met Tyr Trp Met Asn Val Val Ile
1310 1315 1320
Gly Lys Met Asn Ala Glu Val Gly Gly Glu Val Val Val Pro Ile
1325 1330 1335
Glu Phe Lys Asn Val Pro Ser Phe Gly Ile Asn Asn Cys Asp Phe
1340 1345 1350
Lys Leu Val Tyr Asp Ala Thr Ala Leu Glu Leu Lys Asn Val Glu
1355 1360 1365
Ala Gly Asp Ile Ile Lys Thr Pro Leu Ala Asn Phe Ser Asn Asn
1370 1375 1380
Lys Ser Glu Glu Gly Lys Ile Ser Phe Leu Phe Asn Asp Ala Ser
1385 1390 1395
Gln Gly Ser Met Gln Ile Glu Asn Gly Gly Val Ser Ala Lys Ile
1400 1405 1410
Thr Phe Lys Val Lys Ser Thr Thr Ala Ile Gly Val Tyr Asp Ile
1415 1420 1425
Arg Lys Asp Leu Ile Gly Ser Phe Ser Gly Leu Lys Asp Ser Lys
1430 1435 1440
Met Thr Ser Ile Gly Ala Glu Phe Thr Asn Gly Ser Ile Thr Val
1445 1450 1455
Ala Thr Thr Ala Pro Thr Val Thr Pro Thr Ala Thr Ala Thr Pro
1460 1465 1470
Ser Val Thr Ile Pro Thr Val Thr Pro Thr Ala Thr Ala Thr Pro
1475 1480 1485
Gly Thr Ala Thr Pro Gly Thr Ala Thr Pro Thr Ala Thr Ala Thr
1490 1495 1500
Pro Gly Ala Ala Thr Pro Thr Glu Thr Ala Thr Pro Ser Val Met
1505 1510 1515
Ile Pro Thr Val Thr Pro Thr Ala Thr Ala Thr Pro Thr Ala Thr
1520 1525 1530
Ala Thr Pro Thr Val Lys Gly Thr Pro Thr Ile Lys Pro Val Tyr
1535 1540 1545
Lys Met Asn Val Val Ile Gly Arg Val Asn Val Val Ala Gly Glu
1550 1555 1560
Glu Val Val Val Pro Val Glu Phe Lys Asn Ile Pro Ala Ile Gly
1565 1570 1575
Val Asn Asn Cys Asn Phe Val Leu Glu Tyr Asp Ala Asn Val Leu
1580 1585 1590
Glu Val Lys Lys Val Asp Ala Gly Glu Ile Val Pro Asp Ala Leu
1595 1600 1605
Ile Asn Phe Gly Ser Asn Asn Ser Asp Glu Gly Lys Val Tyr Phe
1610 1615 1620
Leu Phe Asn Asp Ala Leu Gln Gly Arg Met Gln Ile Ala Asn Asp
1625 1630 1635
Gly Ile Phe Ala Asn Ile Thr Phe Lys Val Lys Ser Ser Ala Ala
1640 1645 1650
Ala Gly Ile Tyr Asn Ile Arg Lys Asp Ser Val Gly Ala Phe Ser
1655 1660 1665
Gly Leu Val Asp Lys Leu Val Pro Ile Ser Ala Glu Phe Thr Asp
1670 1675 1680
Gly Ser Ile Ser Val Glu Ser Ala Lys Ser Thr Pro Thr Ala Thr
1685 1690 1695
Ala Thr Gly Thr Asn Val Thr Pro Thr Val Ala Ala Thr Val Thr
1700 1705 1710
Pro Thr Ala Thr Pro Ala Ser Thr Thr Pro Thr Ala Thr Pro Thr
1715 1720 1725
Ala Thr Ser Thr Val Lys Gly Thr Pro Thr Ala Thr Pro Leu Tyr
1730 1735 1740
Ser Met Asn Val Ile Ile Gly Lys Val Asn Ala Glu Ala Ser Gly
1745 1750 1755
Glu Val Val Val Pro Val Glu Phe Lys Asp Val Pro Ser Ile Gly
1760 1765 1770
Ile Asn Asn Cys Asn Phe Ile Leu Glu Tyr Asp Ala Ser Ala Leu
1775 1780 1785
Glu Leu Asp Ser Ala Glu Ala Gly Glu Ile Val Pro Val Pro Leu
1790 1795 1800
Gly Asn Phe Ser Ser Asn Asn Lys Asp Glu Gly Lys Ile Tyr Phe
1805 1810 1815
Leu Phe Ser Asp Gly Thr Gln Gly Arg Met Gln Ile Val Asn Asp
1820 1825 1830
Gly Ile Phe Ala Lys Ile Lys Phe Lys Val Lys Ser Thr Ala Ser
1835 1840 1845
Asp Gly Thr Tyr Tyr Ile Arg Lys Asp Ser Val Gly Ala Phe Ser
1850 1855 1860
Gly Leu Ile Glu Lys Lys Ile Ile Lys Ile Gly Ala Glu Phe Thr
1865 1870 1875
Asp Gly Ser Ile Thr Val Arg Ser Leu Thr Pro Thr Pro Thr Val
1880 1885 1890
Thr Pro Asn Val Ala Ser Pro Thr Pro Thr Lys Val Val Ala Glu
1895 1900 1905
Pro Thr Ser Asn Gln Pro Ala Gly Pro Gly Pro Ile Thr Gly Thr
1910 1915 1920
Ile Pro Thr Ala Thr Thr Thr Ala Thr Ala Thr Pro Thr Lys Ala
1925 1930 1935
Ser Val Ala Thr Ala Thr Pro Thr Ala Thr Pro Ile Val Val Val
1940 1945 1950
Glu Pro Thr Ile Val Arg Pro Gly Tyr Asn Lys Asp Ala Asp Leu
1955 1960 1965
Ala Val Phe Ile Ser Ser Asp Lys Ser Arg Tyr Glu Glu Ser Ser
1970 1975 1980
Ile Ile Thr Tyr Ser Ile Glu Tyr Lys Asn Ile Gly Lys Val Asn
1985 1990 1995
Ala Thr Asn Val Lys Ile Ala Ala Gln Ile Pro Lys Phe Thr Lys
2000 2005 2010
Val Tyr Asp Ala Ala Lys Gly Ala Val Lys Gly Ser Glu Ile Val
2015 2020 2025
Trp Met Ile Gly Asn Leu Ala Val Gly Glu Ser Tyr Thr Lys Glu
2030 2035 2040
Tyr Lys Val Lys Val Asp Ser Leu Thr Lys Ser Glu Glu Tyr Thr
2045 2050 2055
Asp Asn Thr Val Thr Ile Ser Ser Asp Gln Thr Val Asp Ile Pro
2060 2065 2070
Glu Asn Ile Thr Thr Gly Asn Asp Asp Lys Ser Thr Ile Arg Val
2075 2080 2085
Met Leu Tyr Ser Asn Arg Phe Thr Pro Gly Ser His Ser Ser Tyr
2090 2095 2100
Ile Leu Gly Tyr Lys Asp Lys Thr Phe Lys Pro Lys Gln Asn Val
2105 2110 2115
Thr Arg Ala Glu Val Ala Ala Met Phe Ala Arg Ile Met Gly Leu
2120 2125 2130
Thr Val Lys Asp Gly Ala Lys Ser Ser Tyr Lys Asp Val Ser Asn
2135 2140 2145
Lys His Trp Ala Leu Lys Tyr Ile Glu Ala Val Thr Lys Ser Gly
2150 2155 2160
Ile Phe Lys Gly Tyr Lys Asp Ser Thr Phe His Pro Asn Ala Pro
2165 2170 2175
Ile Thr Arg Ala Glu Leu Ser Thr Val Ile Phe Asn Tyr Leu His
2180 2185 2190
Leu Asn Asn Ile Ala Pro Ser Lys Val His Phe Thr Asp Ile Asn
2195 2200 2205
Lys His Trp Ala Lys Asn Tyr Ile Glu Glu Ile Tyr Arg Phe Lys
2210 2215 2220
Leu Ile Gln Gly Tyr Ser Asp Gly Ser Phe Lys Pro Asn Asn Asn
2225 2230 2235
Ile Thr Arg Ala Glu Val Val Thr Met Ile Asn Arg Met Leu Tyr
2240 2245 2250
Arg Gly Pro Leu Lys Val Lys Val Gly Ser Phe Pro Asp Val Ser
2255 2260 2265
Pro Lys Tyr Trp Ala Tyr Gly Asp Ile Glu Glu Ala Ser Arg Asn
2270 2275 2280
His Lys Tyr Thr Arg Asp Glu Lys Asp Gly Ser Glu Ile Leu Ile
2285 2290 2295
Glu
<210> 2
<211> 1653
<212> DNA
<213> Artificial
<220>
<223> Chemically synthesized oligonucleotide
<400> 2
atggacctcc tgtgcaagaa catgaagcac ctgtggttct tcctcctgct ggtggcggct 60
cccagatggg tcctgtcccg gctgcagctg caggagtcgg gcccaggcct gctgaagcct 120
tcggtgaccc tgtccctcac ctgcactgtc tcgggtgact ccgtcgccag tagttcttat 180
tactggggct gggtccgtca gcccccaggg aagggactcg agtggatagg gactatcaat 240
tttagtggca atatgtatta tagtccgtcc ctcaggagtc gagtgaccat gtcggcagac 300
atgtccgaga actccttcta tctgaaattg gactctgtga ccgcagcaga cacggccgtc 360
tattattgtg cggcaggaca cctcgttatg ggatttgggg cccactgggg acagggaaaa 420
ctggtctccg tctctccagc ttccaccaag ggcccatccg tcttccccct ggcgccctgc 480
tccaggagca cctccgagag cacagccgcc ctgggctgcc tggtcaagga ctacttcccc 540
gaaccggtga cggtgtcgtg gaactcaggc gccctgacca gcggcgtgca caccttcccg 600
gctgtcctac agtcctcagg actctactcc ctcagcagcg tggtgaccgt gccctccagc 660
agcttgggca cgaagaccta cacctgcaac gtagatcaca agcccagcaa caccaaggtg 720
gacaagagag ttgagtccaa atatggtccc ccatgcccac cctgcccagc acctgagttc 780
gaagggggac catcagtctt cctgttcccc ccaaaaccca aggacactct catgatctcc 840
cggacccctg aggtcacgtg cgtggtggtg gacgtgagcc aggaagaccc cgaggtccag 900
ttcaactggt acgtggatgg cgtggaggtg cataatgcca agacaaagcc gcgggaggag 960
cagttcaaca gcacgtaccg tgtggtcagc gtcctcaccg tcctgcacca ggactggctg 1020
aacggcaagg agtacaagtg caaggtctcc aacaaaggcc tcccgtcctc catcgagaaa 1080
accatctcca aagccaaagg gcagccccga gagccacagg tgtacaccct gcccccatcc 1140
caggaggaga tgaccaagaa ccaggtcagc ctgacctgcc tggtcaaagg cttctacccc 1200
agcgacatcg ccgtggagtg ggagagcaat gggcagccgg agaacaacta caagaccacg 1260
cctcccgtgc tggactccga cggctccttc ttcctctaca gcaggctaac cgtggacaag 1320
agcaggtggc aggaggggaa tgtcttctca tgctccgtga tgcatgaggc tctgcacaac 1380
cactacacac agaagagcct ctccctgtct ctgggtaaag ctagcaattc tcctcaaaat 1440
gaagtactgt acggagatgt gaatgatgac ggaaaagtaa actccactga cttgactttg 1500
ttaaaaagat atgttcttaa agccgtctca actctccctt cttccaaagc tgaaaagaac 1560
gcagatgtaa atcgtgacgg aagagttaat tccagtgatg tcacaatact ttcaagatat 1620
ttgataaggg taatcgagaa attaccaata taa 1653
<210> 3
<211> 524
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 3
Arg Leu Gln Leu Gln Glu Ser Gly Pro Gly Leu Leu Lys Pro Ser Val
1 5 10 15
Thr Leu Ser Leu Thr Cys Thr Val Ser Gly Asp Ser Val Ala Ser Ser
20 25 30
Ser Tyr Tyr Trp Gly Trp Val Arg Gln Pro Pro Gly Lys Gly Leu Glu
35 40 45
Trp Ile Gly Thr Ile Asn Phe Ser Gly Asn Met Tyr Tyr Ser Pro Ser
50 55 60
Leu Arg Ser Arg Val Thr Met Ser Ala Asp Met Ser Glu Asn Ser Phe
65 70 75 80
Tyr Leu Lys Leu Asp Ser Val Thr Ala Ala Asp Thr Ala Val Tyr Tyr
85 90 95
Cys Ala Ala Gly His Leu Val Met Gly Phe Gly Ala His Trp Gly Gln
100 105 110
Gly Lys Leu Val Ser Val Ser Pro Ala Ser Thr Lys Gly Pro Ser Val
115 120 125
Phe Pro Leu Ala Pro Cys Ser Arg Ser Thr Ser Glu Ser Thr Ala Ala
130 135 140
Leu Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser
145 150 155 160
Trp Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val
165 170 175
Leu Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro
180 185 190
Ser Ser Ser Leu Gly Thr Lys Thr Tyr Thr Cys Asn Val Asp His Lys
195 200 205
Pro Ser Asn Thr Lys Val Asp Lys Arg Val Glu Ser Lys Tyr Gly Pro
210 215 220
Pro Cys Pro Pro Cys Pro Ala Pro Glu Phe Glu Gly Gly Pro Ser Val
225 230 235 240
Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr
245 250 255
Pro Glu Val Thr Cys Val Val Val Asp Val Ser Gln Glu Asp Pro Glu
260 265 270
Val Gln Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys
275 280 285
Thr Lys Pro Arg Glu Glu Gln Phe Asn Ser Thr Tyr Arg Val Val Ser
290 295 300
Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys
305 310 315 320
Cys Lys Val Ser Asn Lys Gly Leu Pro Ser Ser Ile Glu Lys Thr Ile
325 330 335
Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro
340 345 350
Pro Ser Gln Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu
355 360 365
Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn
370 375 380
Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser
385 390 395 400
Asp Gly Ser Phe Phe Leu Tyr Ser Arg Leu Thr Val Asp Lys Ser Arg
405 410 415
Trp Gln Glu Gly Asn Val Phe Ser Cys Ser Val Met His Glu Ala Leu
420 425 430
His Asn His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Leu Gly Lys Ala
435 440 445
Ser Asn Ser Pro Gln Asn Glu Val Leu Tyr Gly Asp Val Asn Asp Asp
450 455 460
Gly Lys Val Asn Ser Thr Asp Leu Thr Leu Leu Lys Arg Tyr Val Leu
465 470 475 480
Lys Ala Val Ser Thr Leu Pro Ser Ser Lys Ala Glu Lys Asn Ala Asp
485 490 495
Val Asn Arg Asp Gly Arg Val Asn Ser Ser Asp Val Thr Ile Leu Ser
500 505 510
Arg Tyr Leu Ile Arg Val Ile Glu Lys Leu Pro Ile
515 520
<210> 4
<211> 1635
<212> DNA
<213> Artificial
<220>
<223> Chemically synthesized oligonucleotide
<400> 4
atgaaatgca gctgggtcat cttcttcctg atggcagtgg ttacaggggt caattcagag 60
gttcagctgc agcagtctgg ggctgagctt gtgaggccag gggccttagt caagttgtcc 120
tgcaaagctt ctggcttcaa cattaatgac tactatatcc actgggtgaa gcagcggcct 180
gaacagggcc tggagcggat tggatggatt gatcctgaca atggtaatac tatatatgac 240
ccgaagttcc agggcaaggc cagtataaca gcagacacat cccccaacac agcctacctg 300
cagctcagca gcctgacatc tgaggacact gccgtctatt actgtgctag aacccgatct 360
cctatggtta cgacggggtt tgtttactgg ggccaaggga ctgtggtcac tgtctctgca 420
gccaaaacga agggcccatc cgtcttcccc ctggcgccct gctccaggag cacctccgag 480
agcacagccg ccctgggctg cctggtcaag gactacttcc ccgaaccggt gacggtgtcg 540
tggaactcag gcgccctgac cagcggcgtg cacaccttcc cggctgtcct acagtcctca 600
ggactctact ccctcagcag cgtggtgacc gtgccctcca gcagcttggg cacgaagacc 660
tacacctgca acgtagatca caagcccagc aacaccaagg tggacaagag agttgagtcc 720
aaatatggtc ccccatgccc accctgccca gcacctgagt tcgaaggggg accatcagtc 780
ttcctgttcc ccccaaaacc caaggacact ctcatgatct cccggacccc tgaggtcacg 840
tgcgtggtgg tggacgtgag ccaggaagac cccgaggtcc agttcaactg gtacgtggat 900
ggcgtggagg tgcataatgc caagacraag ccgcgggagg agcagttcaa cagcacgtac 960
cgtgtggtca gcgtcctcac cgtcctgcac caggactggc tgaacggcaa ggagtacaag 1020
tgcaaggtct ccaacaaagg cctcccgtcc tccatcgaga aaaccatctc caaagccaaa 1080
gggcagcccc gagagccaca ggtgtacacc ctgcccccat cccaggagga gatgaccaag 1140
aaccaggtca gcctgacctg cctggtcaaa ggcttctacc ccagcgacat cgccgtggag 1200
tgggagagca atgggcagcc ggagaacaac tacaagacca cgcctcccgt gctggactcc 1260
gacggctcct tcttcctcta cagcaggcta accgtggaca agagcaggtg gcaggagggg 1320
aatgtcttct catgctccgt gatgcatgag gctctgcaca accactacac acagaagagc 1380
ctctccctgt ctctgggtaa agctagcaat tctcctcaaa atgaagtact gtacggagat 1440
gtgaatgatg acggaaaagt aaactccact gacttgactt tgttaaaaag atatgttctt 1500
aaagccgtct caactctccc ttcttccaaa gctgaaaaga acgcagatgt aaatcgtgac 1560
ggaagagtta attccagtga tgtcacaata ctttcaagat atttgataag ggtaatcgag 1620
aaattaccaa tataa 1635
<210> 5
<211> 525
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 5
Glu Val Gln Leu Gln Gln Ser Gly Ala Glu Leu Val Arg Pro Gly Ala
1 5 10 15
Leu Val Lys Leu Ser Cys Lys Ala Ser Gly Phe Asn Ile Asn Asp Tyr
20 25 30
Tyr Ile His Trp Val Lys Gln Arg Pro Glu Gln Gly Leu Glu Arg Ile
35 40 45
Gly Trp Ile Asp Pro Asp Asn Gly Asn Thr Ile Tyr Asp Pro Lys Phe
50 55 60
Gln Gly Lys Ala Ser Ile Thr Ala Asp Thr Ser Pro Asn Thr Ala Tyr
65 70 75 80
Leu Gln Leu Ser Ser Leu Thr Ser Glu Asp Thr Ala Val Tyr Tyr Cys
85 90 95
Ala Arg Thr Arg Ser Pro Met Val Thr Thr Gly Phe Val Tyr Trp Gly
100 105 110
Gln Gly Thr Val Val Thr Val Ser Ala Ala Lys Thr Lys Gly Pro Ser
115 120 125
Val Phe Pro Leu Ala Pro Cys Ser Arg Ser Thr Ser Glu Ser Thr Ala
130 135 140
Ala Leu Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val
145 150 155 160
Ser Trp Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala
165 170 175
Val Leu Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val
180 185 190
Pro Ser Ser Ser Leu Gly Thr Lys Thr Tyr Thr Cys Asn Val Asp His
195 200 205
Lys Pro Ser Asn Thr Lys Val Asp Lys Arg Val Glu Ser Lys Tyr Gly
210 215 220
Pro Pro Cys Pro Pro Cys Pro Ala Pro Glu Phe Glu Gly Gly Pro Ser
225 230 235 240
Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg
245 250 255
Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser Gln Glu Asp Pro
260 265 270
Glu Val Gln Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala
275 280 285
Lys Thr Lys Pro Arg Glu Glu Gln Phe Asn Ser Thr Tyr Arg Val Val
290 295 300
Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr
305 310 315 320
Lys Cys Lys Val Ser Asn Lys Gly Leu Pro Ser Ser Ile Glu Lys Thr
325 330 335
Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu
340 345 350
Pro Pro Ser Gln Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys
355 360 365
Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser
370 375 380
Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp
385 390 395 400
Ser Asp Gly Ser Phe Phe Leu Tyr Ser Arg Leu Thr Val Asp Lys Ser
405 410 415
Arg Trp Gln Glu Gly Asn Val Phe Ser Cys Ser Val Met His Glu Ala
420 425 430
Leu His Asn His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Leu Gly Lys
435 440 445
Ala Ser Asn Ser Pro Gln Asn Glu Val Leu Tyr Gly Asp Val Asn Asp
450 455 460
Asp Gly Lys Val Asn Ser Thr Asp Leu Thr Leu Leu Lys Arg Tyr Val
465 470 475 480
Leu Lys Ala Val Ser Thr Leu Pro Ser Ser Lys Ala Glu Lys Asn Ala
485 490 495
Asp Val Asn Arg Asp Gly Arg Val Asn Ser Ser Asp Val Thr Ile Leu
500 505 510
Ser Arg Tyr Leu Ile Arg Val Ile Glu Lys Leu Pro Ile
515 520 525
<210> 6
<211> 1638
<212> DNA
<213> Artificial
<220>
<223> Chemically synthesized oligonucleotide
<400> 6
atggacccca aaggctccct ttcctggaga atacttctgt ttctctccct ggcttttgag 60
ttgtcgtacg gagatgtgca gcttcaggag tcaggacctg acctggtgaa accttctcag 120
tcactttcac tcacctgcac tgtcactggc tactccatca ccagtggtta tagctggcac 180
tggatccggc agtttccagg aaacaaactg gaatggatgg gctacatact cttcagtggt 240
agcactaact acaacccatc tctgaaaagt cgaatctcta tcactcgaga cacatccaag 300
aaccagttct tcctgcagtt gaattctgtg actactgagg acacagccac atatttctgt 360
gcaagatcta actatggttc ctttgcttcc tggggccaag ggactctggt cactgtctct 420
gcagccaaaa caaagggccc atccgtcttc cccctggcgc cctgctccag gagcacctcc 480
gagagcacag ccgccctggg ctgcctggtc aaggactact tccccgaacc ggtgacggtg 540
tcgtggaact caggcgccct gaccagcggc gtgcacacct tcccggctgt cctacagtcc 600
tcaggactct actccctcag cagcgtggtg accgtgccct ccagcagctt gggcacgaag 660
acctacacct gcaacgtaga tcacaagccc agcaacacca aggtggacaa gagagttgag 720
tccaaatatg gtcccccatg cccaccctgc ccagcacctg agttcgaagg gggaccatca 780
gtcttcctgt tccccccaaa acccaaggac actctcatga tctcccggac ccctgaggtc 840
acgtgcgtgg tggtggacgt gagccaggaa gaccccgagg tccagttcaa ctggtacgtg 900
gatggcgtgg aggtgcataa tgccaagaca aagccgcggg aggagcagtt caacagcacg 960
taccgtgtgg tcagcgtcct caccgtcctg caccaggact ggctgaacgg caaggagtac 1020
aagtgcaagg tctccaacaa aggcctcccg tcctccatcg agaaaaccat ctccaaagcc 1080
aaagggcagc cccgagagcc acaggtgtac accctgcccc catcccagga ggagatgacc 1140
aagaaccagg tcagcctgac ctgcctggtc aaaggcttct accccagcga catcgccgtg 1200
gagtgggaga gcaatgggca gccggagaac aactacaaga ccacgcctcc cgtgctggac 1260
tccgacggct ccttcttcct ctacagcagg ctaaccgtgg acaagagcag gtggcaggag 1320
gggaatgtct tctcatgctc cgtgatgcat gaggctctgc acaaccacta cacacagaag 1380
agcctctccc tgtctctggg taaagctagc aattctcctc aaaatgaagt actgtacgga 1440
gatgtgaatg atgacggaaa agtaaactcc actgacttga ctttgttaaa aagatatgtt 1500
cttaaagccg tctcaactct cccttcttcc aaagctgaaa agaacgcaga tgtaaatcgt 1560
gacggaagag ttaattccag tgatgtcaca atactttcaa gatatttgat aagggtaatc 1620
gagaaattac caatataa 1638
<210> 7
<211> 521
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 7
Asp Val Gln Leu Gln Glu Ser Gly Pro Asp Leu Val Lys Pro Ser Gln
1 5 10 15
Ser Leu Ser Leu Thr Cys Thr Val Thr Gly Tyr Ser Ile Thr Ser Gly
20 25 30
Tyr Ser Trp His Trp Ile Arg Gln Phe Pro Gly Asn Lys Leu Glu Trp
35 40 45
Met Gly Tyr Ile Leu Phe Ser Gly Ser Thr Asn Tyr Asn Pro Ser Leu
50 55 60
Lys Ser Arg Ile Ser Ile Thr Arg Asp Thr Ser Lys Asn Gln Phe Phe
65 70 75 80
Leu Gln Leu Asn Ser Val Thr Thr Glu Asp Thr Ala Thr Tyr Phe Cys
85 90 95
Ala Arg Ser Asn Tyr Gly Ser Phe Ala Ser Trp Gly Gln Gly Thr Leu
100 105 110
Val Thr Val Ser Ala Ala Lys Thr Lys Gly Pro Ser Val Phe Pro Leu
115 120 125
Ala Pro Cys Ser Arg Ser Thr Ser Glu Ser Thr Ala Ala Leu Gly Cys
130 135 140
Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser
145 150 155 160
Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser
165 170 175
Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser
180 185 190
Leu Gly Thr Lys Thr Tyr Thr Cys Asn Val Asp His Lys Pro Ser Asn
195 200 205
Thr Lys Val Asp Lys Arg Val Glu Ser Lys Tyr Gly Pro Pro Cys Pro
210 215 220
Pro Cys Pro Ala Pro Glu Phe Glu Gly Gly Pro Ser Val Phe Leu Phe
225 230 235 240
Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr Pro Glu Val
245 250 255
Thr Cys Val Val Val Asp Val Ser Gln Glu Asp Pro Glu Val Gln Phe
260 265 270
Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys Thr Lys Pro
275 280 285
Arg Glu Glu Gln Phe Asn Ser Thr Tyr Arg Val Val Ser Val Leu Thr
290 295 300
Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys Cys Lys Val
305 310 315 320
Ser Asn Lys Gly Leu Pro Ser Ser Ile Glu Lys Thr Ile Ser Lys Ala
325 330 335
Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro Pro Ser Gln
340 345 350
Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu Val Lys Gly
355 360 365
Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn Gly Gln Pro
370 375 380
Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser Asp Gly Ser
385 390 395 400
Phe Phe Leu Tyr Ser Arg Leu Thr Val Asp Lys Ser Arg Trp Gln Glu
405 410 415
Gly Asn Val Phe Ser Cys Ser Val Met His Glu Ala Leu His Asn His
420 425 430
Tyr Thr Gln Lys Ser Leu Ser Leu Ser Leu Gly Lys Ala Ser Asn Ser
435 440 445
Pro Gln Asn Glu Val Leu Tyr Gly Asp Val Asn Asp Asp Gly Lys Val
450 455 460
Asn Ser Thr Asp Leu Thr Leu Leu Lys Arg Tyr Val Leu Lys Ala Val
465 470 475 480
Ser Thr Leu Pro Ser Ser Lys Ala Glu Lys Asn Ala Asp Val Asn Arg
485 490 495
Asp Gly Arg Val Asn Ser Ser Asp Val Thr Ile Leu Ser Arg Tyr Leu
500 505 510
Ile Arg Val Ile Glu Lys Leu Pro Ile
515 520
<210> 8
<211> 1623
<212> DNA
<213> Artificial
<220>
<223> Chemically synthesized oligonucleotide
<400> 8
atggaaaggc actggatctt tctcttcctg ttttcagtaa ctgcaggtgt ccactcccag 60
gtccagcttc agcagtctgg ggctgagctg gcaaaacctg gggcctcagt gaagatgtcc 120
tgcaaggctt ctggctacac ctttactacc tactggatgc actgggtaaa acagaggcct 180
ggacagggtc tggaatggat tggatacatt aatcctatca ctggttatac tgagtacaat 240
cagaagttca aggacaaggc caccttgact gcagacaaat cctccagcac agcctacatg 300
caactgagca gcctgacatc tgaggactct gcagtctatt actgtgcaag agagggttta 360
agtgctatgg actattgggg tcagggaacc tcagtcaccg tcacctcagc caaaacaacg 420
ggcccatccg tcttccccct ggcgccctgc tccaggagca cctccgagag cacagccgcc 480
ctgggctgcc tggtcaagga ctacttcccc gaaccggtga cggtgtcgtg gaactcaggc 540
gccctgacca gcggcgtgca caccttcccg gctgtcctac agtcctcagg actctactcc 600
ctcagcagcg tggtgaccgt gccctccagc agcttgggca cgaagaccta cacctgcaac 660
gtagatcaca agcccagcaa caccaaggtg gacaagagag ttgagtccaa atatggtccc 720
ccatgcccac cctgcccagc acctgagttc gaagggggac catcagtctt cctgttcccc 780
ccaaaaccca aggacactct catgatctcc cggacccctg aggtcacgtg cgtggtggtg 840
gacgtgagcc aggaagaccc cgaggtccag ttcaactggt acgtggatgg cgtggaggtg 900
cataatgcca agacaaagcc gcgggaggag cagttcaaca gcacgtaccg tgtggtcagc 960
gtcctcaccg tcctgcacca ggactggctg aacggcaagg agtacaagtg caaggtctcc 1020
aacaaaggcc tcccgtcctc catcgagaaa accatctcca aagccaaagg gcagccccga 1080
gagccacagg tgtacaccct gcccccatcc caggaggaga tgaccaagaa ccaggtcagc 1140
ctgacctgcc tggtcaaagg cttctacccc agcgacatcg ccgtggagtg ggagagcaat 1200
gggcagccgg agaacaacta caagaccacg cctcccgtgc tggactccga cggctccttc 1260
ttcctctaca gcaggctaac cgtggacaag agcaggtggc aggaggggaa tgtcttctca 1320
tgctccgtga tgcatgaggc tctgcacaac cactacacac agaagagcct ctccctgtct 1380
ctgggtaaag ctagcaattc tcctcaaaat gaagtactgt acggagatgt gaatgatgac 1440
ggaaaagtaa actccactga cttgactttg ttaaaaagat atgttcttaa agccgtctca 1500
actctccctt cttccaaagc tgaaaagaac gcagatgtaa atcgtgacgg aagagttaat 1560
tccagtgatg tcacaatact ttcaagatat ttgataaggg taatcgagaa attaccaata 1620
taa 1623
<210> 9
<211> 521
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 9
Gln Val Gln Leu Gln Gln Ser Gly Ala Glu Leu Ala Lys Pro Gly Ala
1 5 10 15
Ser Val Lys Met Ser Cys Lys Ala Ser Gly Tyr Thr Phe Thr Thr Tyr
20 25 30
Trp Met His Trp Val Lys Gln Arg Pro Gly Gln Gly Leu Glu Trp Ile
35 40 45
Gly Tyr Ile Asn Pro Ile Thr Gly Tyr Thr Glu Tyr Asn Gln Lys Phe
50 55 60
Lys Asp Lys Ala Thr Leu Thr Ala Asp Lys Ser Ser Ser Thr Ala Tyr
65 70 75 80
Met Gln Leu Ser Ser Leu Thr Ser Glu Asp Ser Ala Val Tyr Tyr Cys
85 90 95
Ala Arg Glu Gly Leu Ser Ala Met Asp Tyr Trp Gly Gln Gly Thr Ser
100 105 110
Val Thr Val Thr Ser Ala Lys Thr Thr Gly Pro Ser Val Phe Pro Leu
115 120 125
Ala Pro Cys Ser Arg Ser Thr Ser Glu Ser Thr Ala Ala Leu Gly Cys
130 135 140
Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser
145 150 155 160
Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser
165 170 175
Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser
180 185 190
Leu Gly Thr Lys Thr Tyr Thr Cys Asn Val Asp His Lys Pro Ser Asn
195 200 205
Thr Lys Val Asp Lys Arg Val Glu Ser Lys Tyr Gly Pro Pro Cys Pro
210 215 220
Pro Cys Pro Ala Pro Glu Phe Glu Gly Gly Pro Ser Val Phe Leu Phe
225 230 235 240
Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr Pro Glu Val
245 250 255
Thr Cys Val Val Val Asp Val Ser Gln Glu Asp Pro Glu Val Gln Phe
260 265 270
Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys Thr Lys Pro
275 280 285
Arg Glu Glu Gln Phe Asn Ser Thr Tyr Arg Val Val Ser Val Leu Thr
290 295 300
Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys Cys Lys Val
305 310 315 320
Ser Asn Lys Gly Leu Pro Ser Ser Ile Glu Lys Thr Ile Ser Lys Ala
325 330 335
Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro Pro Ser Gln
340 345 350
Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu Val Lys Gly
355 360 365
Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn Gly Gln Pro
370 375 380
Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser Asp Gly Ser
385 390 395 400
Phe Phe Leu Tyr Ser Arg Leu Thr Val Asp Lys Ser Arg Trp Gln Glu
405 410 415
Gly Asn Val Phe Ser Cys Ser Val Met His Glu Ala Leu His Asn His
420 425 430
Tyr Thr Gln Lys Ser Leu Ser Leu Ser Leu Gly Lys Ala Ser Asn Ser
435 440 445
Pro Gln Asn Glu Val Leu Tyr Gly Asp Val Asn Asp Asp Gly Lys Val
450 455 460
Asn Ser Thr Asp Leu Thr Leu Leu Lys Arg Tyr Val Leu Lys Ala Val
465 470 475 480
Ser Thr Leu Pro Ser Ser Lys Ala Glu Lys Asn Ala Asp Val Asn Arg
485 490 495
Asp Gly Arg Val Asn Ser Ser Asp Val Thr Ile Leu Ser Arg Tyr Leu
500 505 510
Ile Arg Val Ile Glu Lys Leu Pro Ile
515 520
<210> 10
<211> 732
<212> DNA
<213> Artificial
<220>
<223> Chemically synthesized oligonucleotide
<400> 10
atgcatcgca ccagcatggg catcaagatg gagtcacaga ttcaggcatt tgtattcgtg 60
tttctctggt tgtctggtgt tggcggagac attgtgatga cccagtctca caaattcatg 120
tccacatcag taggagacag ggtcagcgtc acctgcaagg ccagtcagga tgtgacttct 180
gctgtagcct ggtatcaaca aaaaccaggg caatctccta aactactgat ttactgggca 240
tccacccggc acactggagt ccctgatcgc ttcacaggca gtggatctgg gacagattat 300
actctcacca tcagcagtgg gcaggctgaa gacctggcac tttattactg tcaccaatat 360
tatagcgctc ctcggacgtt cggtggaggc accaagctcg agatcaaacg aactgtggct 420
gcaccatctg tcttcatctt cccgccatct gatgagcagt tgaaatctgg aactgcctct 480
gttgtgtgcc tgctgaataa cttctatccc agagaggcca aagtacagtg gaaggtggat 540
aacgccctcc aatcgggtaa ctcccaggag agtgtcacag agcaggacag caaggacagc 600
acctacagcc tcagcagcac cctgacgctg agcaaagcag actacgagaa acacaaagtc 660
tatgcctgcg aagtcaccca tcagggcctg agctcgcccg tcacaaagag cttcaacagg 720
ggagagtgtt ag 732
<210> 11
<211> 214
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 11
Asp Ile Val Met Thr Gln Ser His Lys Phe Met Ser Thr Ser Val Gly
1 5 10 15
Asp Arg Val Ser Val Thr Cys Lys Ala Ser Gln Asp Val Thr Ser Ala
20 25 30
Val Ala Trp Tyr Gln Gln Lys Pro Gly Gln Ser Pro Lys Leu Leu Ile
35 40 45
Tyr Trp Ala Ser Thr Arg His Thr Gly Val Pro Asp Arg Phe Thr Gly
50 55 60
Ser Gly Ser Gly Thr Asp Tyr Thr Leu Thr Ile Ser Ser Gly Gln Ala
65 70 75 80
Glu Asp Leu Ala Leu Tyr Tyr Cys His Gln Tyr Tyr Ser Ala Pro Arg
85 90 95
Thr Phe Gly Gly Gly Thr Lys Leu Glu Ile Lys Arg Thr Val Ala Ala
100 105 110
Pro Ser Val Phe Ile Phe Pro Pro Ser Asp Glu Gln Leu Lys Ser Gly
115 120 125
Thr Ala Ser Val Val Cys Leu Leu Asn Asn Phe Tyr Pro Arg Glu Ala
130 135 140
Lys Val Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly Asn Ser Gln
145 150 155 160
Glu Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr Ser Leu Ser
165 170 175
Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His Lys Val Tyr
180 185 190
Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val Thr Lys Ser
195 200 205
Phe Asn Arg Gly Glu Cys
210
<210> 12
<211> 1644
<212> DNA
<213> Artificial
<220>
<223> Chemically synthesized oligonucleotide
<400> 12
atgggatggt catgtatcat cctttttcta gtagcaactg caactggagt acattcacag 60
gtccaactgc agcagcctgg ggctgagctg gtgaggcctg ggacttcagt gaagttgtcc 120
tgcaaggctt ctggttacat ctttaccagc tactggatgc actgggtaaa gcagaggcct 180
ggacaaggcc ttgagtggat cggactgatt gatccttctg atagttatag taagtacaat 240
caaaagttca agggcaaggc cacattgact gtagacacat cctccagcac agcctacatg 300
cagctcagca gcctgacatc tgaggactct gcggtctatt actgtgcaag aggggagctc 360
agtgacttct ggggccaagg caccactctc acagtctcct cagccaaaac aacaccccca 420
tcagtctatc cactggcccc tgggtgtgga gatacaactg gttcctctgt gactctggga 480
tgcctggtca agggctactt ccctgagtca gtgactgtga cttggaactc tggatccctg 540
tccagcagtg tgcacacctt cccagctctc ctgcagtctg gactctacac tatgagcagc 600
tcagtgactg tcccctccag cacctggcca agtcagaccg tcacctgcag cgttgctcac 660
ccagccagca gcaccacggt ggacaaaaaa cttgagccca gcgggcccat ttcaacaatc 720
aacccctgtc ctccatgcaa ggagtgtcac aaatgcccag ctcctaacct cgagggtgga 780
ccatccgtct tcatcttccc tccaaatatc aaggatgtac tcatgatctc cctgacaccc 840
aaggtcacgt gtgtggtggt ggatgtgagc gaggatgacc cagacgtccg gatcagctgg 900
tttgtgaaca acgtggaagt acacacagct cagacacaaa cccatagaga ggattacaac 960
agtactatcc gggtggtcag tgccctcccc atccagcacc aggactggat gagtggcaag 1020
gagttcaaat gcaaggtcaa caacaaagac ctcccatcac ccatcgagag aaccatctca 1080
aaaattaaag ggctagtcag agctccacaa gtatacatct tgccgccacc agcagagcag 1140
ttgtccagga aagatgtcag tctcacttgc ctggtcgtgg gcttcaaccc tggagacatc 1200
agtgtggagt ggaccagcaa tgggcataca gaggagaact acaaggacac cgcaccagtc 1260
ctggactctg acggttctta cttcatatac agcaagctcg atataaaaac aagcaagtgg 1320
gagaaaacag attccttctc atgcaacgtg agacacgagg gtctgaaaaa ttactacctg 1380
aagaagacca tctcccggtc tccgggtaaa gctagcaatt ctcctcaaaa tgaagtactg 1440
tacggagatg tgaatgatga cggaaaagta aactccactg acttgacttt gttaaaaaga 1500
tatgttctta aagccgtctc aactctgcct tcttccaaag ctgaaaagaa cgcagatgta 1560
aatcgtgacg gaagagttaa ttccagtgat gtcacaatac tttcaagata tttgataagg 1620
gtaatcgaga aattaccaat ataa 1644
<210> 13
<211> 528
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 13
Gln Val Gln Leu Gln Gln Pro Gly Ala Glu Leu Val Arg Pro Gly Thr
1 5 10 15
Ser Val Lys Leu Ser Cys Lys Ala Ser Gly Tyr Ile Phe Thr Ser Tyr
20 25 30
Trp Met His Trp Val Lys Gln Arg Pro Gly Gln Gly Leu Glu Trp Ile
35 40 45
Gly Leu Ile Asp Pro Ser Asp Ser Tyr Ser Lys Tyr Asn Gln Lys Phe
50 55 60
Lys Gly Lys Ala Thr Leu Thr Val Asp Thr Ser Ser Ser Thr Ala Tyr
65 70 75 80
Met Gln Leu Ser Ser Leu Thr Ser Glu Asp Ser Ala Val Tyr Tyr Cys
85 90 95
Ala Arg Gly Glu Leu Ser Asp Phe Trp Gly Gln Gly Thr Thr Leu Thr
100 105 110
Val Ser Ser Ala Lys Thr Thr Pro Pro Ser Val Tyr Pro Leu Ala Pro
115 120 125
Gly Cys Gly Asp Thr Thr Gly Ser Ser Val Thr Leu Gly Cys Leu Val
130 135 140
Lys Gly Tyr Phe Pro Glu Ser Val Thr Val Thr Trp Asn Ser Gly Ser
145 150 155 160
Leu Ser Ser Ser Val His Thr Phe Pro Ala Leu Leu Gln Ser Gly Leu
165 170 175
Tyr Thr Met Ser Ser Ser Val Thr Val Pro Ser Ser Thr Trp Pro Ser
180 185 190
Gln Thr Val Thr Cys Ser Val Ala His Pro Ala Ser Ser Thr Thr Val
195 200 205
Asp Lys Lys Leu Glu Pro Ser Gly Pro Ile Ser Thr Ile Asn Pro Cys
210 215 220
Pro Pro Cys Lys Glu Cys His Lys Cys Pro Ala Pro Asn Leu Glu Gly
225 230 235 240
Gly Pro Ser Val Phe Ile Phe Pro Pro Asn Ile Lys Asp Val Leu Met
245 250 255
Ile Ser Leu Thr Pro Lys Val Thr Cys Val Val Val Asp Val Ser Glu
260 265 270
Asp Asp Pro Asp Val Arg Ile Ser Trp Phe Val Asn Asn Val Glu Val
275 280 285
His Thr Ala Gln Thr Gln Thr His Arg Glu Asp Tyr Asn Ser Thr Ile
290 295 300
Arg Val Val Ser Ala Leu Pro Ile Gln His Gln Asp Trp Met Ser Gly
305 310 315 320
Lys Glu Phe Lys Cys Lys Val Asn Asn Lys Asp Leu Pro Ser Pro Ile
325 330 335
Glu Arg Thr Ile Ser Lys Ile Lys Gly Leu Val Arg Ala Pro Gln Val
340 345 350
Tyr Ile Leu Pro Pro Pro Ala Glu Gln Leu Ser Arg Lys Asp Val Ser
355 360 365
Leu Thr Cys Leu Val Val Gly Phe Asn Pro Gly Asp Ile Ser Val Glu
370 375 380
Trp Thr Ser Asn Gly His Thr Glu Glu Asn Tyr Lys Asp Thr Ala Pro
385 390 395 400
Val Leu Asp Ser Asp Gly Ser Tyr Phe Ile Tyr Ser Lys Leu Asp Ile
405 410 415
Lys Thr Ser Lys Trp Glu Lys Thr Asp Ser Phe Ser Cys Asn Val Arg
420 425 430
His Glu Gly Leu Lys Asn Tyr Tyr Leu Lys Lys Thr Ile Ser Arg Ser
435 440 445
Pro Gly Lys Ala Ser Asn Ser Pro Gln Asn Glu Val Leu Tyr Gly Asp
450 455 460
Val Asn Asp Asp Gly Lys Val Asn Ser Thr Asp Leu Thr Leu Leu Lys
465 470 475 480
Arg Tyr Val Leu Lys Ala Val Ser Thr Leu Pro Ser Ser Lys Ala Glu
485 490 495
Lys Asn Ala Asp Val Asn Arg Asp Gly Arg Val Asn Ser Ser Asp Val
500 505 510
Thr Ile Leu Ser Arg Tyr Leu Ile Arg Val Ile Glu Lys Leu Pro Ile
515 520 525
<210> 14
<211> 2061
<212> DNA
<213> Artificial
<220>
<223> Chemically synthesized oligonucleotide
<400> 14
atggatccca aaggatccct ttcctggaga atacttctgt ttctctccct ggcttttgag 60
ttgagctacg gactcgacga tctggatgca gtaaggatta aagtggacac agtaaatgca 120
aaaccgggag acacagtaag aatacctgta agattcagcg gtataccatc caagggaata 180
gcaaactgtg actttgtata cagctatgac ccgaatgtac ttgagataat agagatagaa 240
ccgggagaca taatagttga cccgaatcct gacaagagct ttgatactgc agtatatcct 300
gacagaaaga taatagtatt cctgtttgca gaagacagcg gaacaggagc gtatgcaata 360
actaaagacg gagtatttgc tacgatagta gcgaaagtaa aagaaggagc acctaacgga 420
ctcagtgtaa tcaaatttgt agaagtaggc ggatttgcga acaatgacct tgtagaacag 480
aagacacagt tctttgacgg tggagtaaat gttggagata caacagaacc tgcaacacct 540
acaacacctg taacaacacc gacaacaaca gatgatctgg atgcactcga gatcatccca 600
gttgaggagg agaacccgga cttctggaac cgcgaggcag ccgaggccct gggtgccgcc 660
aagaagctgc agcctgcaca gacagccgcc aagaacctca tcatcttcct gggcgatggg 720
atgggggtgt ctacggtgac agctgccagg atcctaaaag ggcagaagaa ggacaaactg 780
gggcctgagt tacccctggc catggaccgc ttcccatatg tggctctgtc caagacatac 840
aatgtagaca aacatgtgcc agacagtgga gccacagcca cggcctacct gtgcggggtc 900
aagggcaact tccagaccat tggcttgagt gcagccgccc gctttaacca gtgcaacacg 960
acacgcggca acgaggtcat ctccgtgatg aatcgggcca agaaagcagg gaagtcagtg 1020
ggagtggtaa ccaccacacg agtgcagcac gcctcgccag ccggcaccta cgcccacacg 1080
gtgaaccgca actggtactc ggacgccgac gtgcctgcct cggcccgcca ggaggggtgc 1140
caggacatcg ctacgcagct catctccaac atggacattg acgtgatcct aggtggaggc 1200
cgaaagtaca tgtttcgcat gggaacccca gaccctgagt acccagatga ctacagccaa 1260
ggtgggacca ggctggacgg gaagaatctg gtgcaggaat ggctggcgaa gcgccagggt 1320
gcccggtacg tgtggaaccg cactgagctc atgcaggctt ccctggaccc gtctgtgacc 1380
catctcatgg gtctctttga gcctggagac atgaaatacg agatccaccg agactccaca 1440
ctggacccct ccctgatgga gatgacagag gctgccctgc gcctgctgag caggaacccc 1500
cgcggcttct tcctcttcgt ggagggtggt cgcatcgacc atggtcatca tgaaagcagg 1560
gcttaccggg cactgactga gacgatcatg ttcgacgacg ccattgagag ggcgggccag 1620
ctcaccagcg aggaggacac gctgagcctc gtcactgccg accactccca cgtcttctcc 1680
ttcggaggct accccctgcg agggagctcc atcttcgggc tggcccctgg caaggcccgg 1740
gacaggaagg cctacacggt cctcctatac ggaaacggtc caggctatgt gctcaaggac 1800
ggcgcccggc cggatgttac cgagagcgag agcgggagcc ccgagtatcg gcagcagtca 1860
gcagtgcccc tggacgaaga gacccacgca ggcgaggacg tggcggtgtt cgcgcgcggc 1920
ccgcaggcgc acctggttca cggcgtgcag gagcagacct tcatagcgca cgtcatggcc 1980
ttcgccgcct gcctggagcc ctacaccgcc tgcgacctgg cgccccccgc cggcaccacc 2040
caccatcacc atcaccattg a 2061
<210> 15
<211> 662
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 15
Leu Asp Asp Leu Asp Ala Val Arg Ile Lys Val Asp Thr Val Asn Ala
1 5 10 15
Lys Pro Gly Asp Thr Val Arg Ile Pro Val Arg Phe Ser Gly Ile Pro
20 25 30
Ser Lys Gly Ile Ala Asn Cys Asp Phe Val Tyr Ser Tyr Asp Pro Asn
35 40 45
Val Leu Glu Ile Ile Glu Ile Glu Pro Gly Glu Leu Ile Val Asp Pro
50 55 60
Asn Pro Thr Lys Ser Phe Asp Thr Ala Val Tyr Pro Asp Arg Lys Met
65 70 75 80
Ile Val Phe Leu Phe Ala Glu Asp Ser Gly Thr Gly Ala Tyr Ala Ile
85 90 95
Thr Glu Asp Gly Val Phe Ala Thr Ile Val Ala Lys Val Lys Ser Gly
100 105 110
Ala Pro Asn Gly Leu Ser Val Ile Lys Phe Val Glu Val Gly Gly Phe
115 120 125
Ala Asn Asn Asp Leu Val Glu Gln Lys Thr Gln Phe Phe Asp Gly Gly
130 135 140
Val Asn Val Gly Asp Thr Thr Glu Pro Ala Thr Pro Thr Thr Pro Val
145 150 155 160
Thr Thr Pro Thr Thr Thr Asp Asp Leu Asp Ala Leu Glu Ile Ile Pro
165 170 175
Val Glu Glu Glu Asn Pro Asp Phe Trp Asn Arg Glu Ala Ala Glu Ala
180 185 190
Leu Gly Ala Ala Lys Lys Leu Gln Pro Ala Gln Thr Ala Ala Lys Asn
195 200 205
Leu Ile Ile Phe Leu Gly Asp Gly Met Gly Val Ser Thr Val Thr Ala
210 215 220
Ala Arg Ile Leu Lys Gly Gln Lys Lys Asp Lys Leu Gly Pro Glu Leu
225 230 235 240
Pro Leu Ala Met Asp Arg Phe Pro Tyr Val Ala Leu Ser Lys Thr Tyr
245 250 255
Asn Val Asp Lys His Val Pro Asp Ser Gly Ala Thr Ala Thr Ala Tyr
260 265 270
Leu Cys Gly Val Lys Gly Asn Phe Gln Thr Ile Gly Leu Ser Ala Ala
275 280 285
Ala Arg Phe Asn Gln Cys Asn Thr Thr Arg Gly Asn Glu Val Ile Ser
290 295 300
Val Met Asn Arg Ala Lys Lys Ala Gly Lys Ser Val Gly Val Val Thr
305 310 315 320
Thr Thr Arg Val Gln His Ala Ser Pro Ala Gly Thr Tyr Ala His Thr
325 330 335
Val Asn Arg Asn Trp Tyr Ser Asp Ala Asp Val Pro Ala Ser Ala Arg
340 345 350
Gln Glu Gly Cys Gln Asp Ile Ala Thr Gln Leu Ile Ser Asn Met Asp
355 360 365
Ile Asp Val Ile Leu Gly Gly Gly Arg Lys Tyr Met Phe Arg Met Gly
370 375 380
Thr Pro Asp Pro Glu Tyr Pro Asp Asp Tyr Ser Gln Gly Gly Thr Arg
385 390 395 400
Leu Asp Gly Lys Asn Leu Val Gln Glu Trp Leu Ala Lys Arg Gln Gly
405 410 415
Ala Arg Tyr Val Trp Asn Arg Thr Glu Leu Met Gln Ala Ser Leu Asp
420 425 430
Pro Ser Val Thr His Leu Met Gly Leu Phe Glu Pro Gly Asp Met Lys
435 440 445
Tyr Glu Ile His Arg Asp Ser Thr Leu Asp Pro Ser Leu Met Glu Met
450 455 460
Thr Glu Ala Ala Leu Arg Leu Leu Ser Arg Asn Pro Arg Gly Phe Phe
465 470 475 480
Leu Phe Val Glu Gly Gly Arg Ile Asp His Gly His His Glu Ser Arg
485 490 495
Ala Tyr Arg Ala Leu Thr Glu Thr Ile Met Phe Asp Asp Ala Ile Glu
500 505 510
Arg Ala Gly Gln Leu Thr Ser Glu Glu Asp Thr Leu Ser Leu Val Thr
515 520 525
Ala Asp His Ser His Val Phe Ser Phe Gly Gly Tyr Pro Leu Arg Gly
530 535 540
Ser Ser Ile Phe Gly Leu Ala Pro Gly Lys Ala Arg Asp Arg Lys Ala
545 550 555 560
Tyr Thr Val Leu Leu Tyr Gly Asn Gly Pro Gly Tyr Val Leu Lys Asp
565 570 575
Gly Ala Arg Pro Asp Val Thr Glu Ser Glu Ser Gly Ser Pro Glu Tyr
580 585 590
Arg Gln Gln Ser Ala Val Pro Leu Asp Glu Glu Thr His Ala Gly Glu
595 600 605
Asp Val Ala Val Phe Ala Arg Gly Pro Gln Ala His Leu Val His Gly
610 615 620
Val Gln Glu Gln Thr Phe Ile Ala His Val Met Ala Phe Ala Ala Cys
625 630 635 640
Leu Glu Pro Tyr Thr Ala Cys Asp Leu Ala Pro Pro Ala Gly Thr Thr
645 650 655
His His His His His His
660
<210> 16
<211> 2556
<212> DNA
<213> Artificial
<220>
<223> Chemically synthesized oligonucleotide
<400> 16
atggatccca aaggatccct ttcctggaga atacttctgt ttctctccct ggcttttgag 60
ttgagctacg gactcgacga tctggatgca gtaaggatta aagtggacac agtaaatgca 120
aaaccgggag acacagtaag aatacctgta agattcagcg gtataccatc caagggaata 180
gcaaactgtg actttgtata cagctatgac ccgaatgtac ttgagataat agagataaaa 240
ccgggagaat tgatagttga cccgaatcct gacaagagct ttgatactgc agtatatcct 300
gacagaaaga taatagtatt cctgtttgca gaagacagcg gaacaggagc gtatgcaata 360
actaaagacg gagtatttgc tacgatagta gcgaaagtaa aatccggagc acctaacgga 420
ctcagtgtaa tcaaatttgt agaagtaggc ggatttgcga ataatgacct tgtagaacag 480
aagacacagt tctttgacgg tggagtaaat gttggagata caacagaacc tgcaacacct 540
acaacacctg taacaacacc gacaacaaca gatgatctgg atgcagtaag gattaaagtg 600
gacacagtaa atgcaaaacc gggagacaca gtaaatatac ctgtaagatt cagtggtata 660
ccatccaagg gaatagcaaa ctgtgacttt gtatacagct atgacccgaa tgtacttgag 720
ataatagaga taaaaccggg agaattgata gttgacccga atcctaccaa gagctttgat 780
actgcagtat atcctgacag aaagatgata gtattcctgt ttgcggaaga cagcggaaca 840
ggagcgtatg caataactaa agacggagta tttgctacga tagtagcgaa agtaaaagaa 900
ggagcaccta acggactcag tgtaatcaaa tttgtagaag taggcggatt tgcgaacaat 960
gaccttgtag aacagaagac acagttcttt gacggtggag taaatgttgg agatacaaca 1020
gaacctgcaa cacctacaac acctgtaaca acaccgacaa caacagatga tctggatgca 1080
ctcgagatca tcccagttga ggaggagaac ccggacttct ggaaccgcga ggcagccgag 1140
gccctgggtg ccgccaagaa gctgcagcct gcacagacag ccgccaagaa cctcatcatc 1200
ttcctgggcg atgggatggg ggtgtctacg gtgacagctg ccaggatcct aaaagggcag 1260
aagaaggaca aactggggcc tgagttaccc ctggccatgg accgcttccc atatgtggct 1320
ctgtccaaga catacaatgt agacaaacat gtgccagaca gtggagccac agccacggcc 1380
tacctgtgcg gggtcaaggg caacttccag accattggct tgagtgcagc cgcccgcttt 1440
aaccagtgca acacgacacg cggcaacgag gtcatctccg tgatgaatcg ggccaagaaa 1500
gcagggaagt cagtgggagt ggtaaccacc acacgagtgc agcacgcctc gccagccggc 1560
acctacgccc acacggtgaa ccgcaactgg tactcggacg ccgacgtgcc tgcctcggcc 1620
cgccaggagg ggtgccagga catcgctacg cagctcatct ccaacatgga cattgacgtg 1680
atcctaggtg gaggccgaaa gtacatgttt cgcatgggaa ccccagaccc tgagtaccca 1740
gatgactaca gccaaggtgg gaccaggctg gacgggaaga atctggtgca ggaatggctg 1800
gcgaagcgcc agggtgcccg gtacgtgtgg aaccgcactg agctcatgca ggcttccctg 1860
gacccgtctg tgacccatct catgggtctc tttgagcctg gagacatgaa atacgagatc 1920
caccgagact ccacactgga cccctccctg atggagatga cagaggctgc cctgcgcctg 1980
ctgagcagga acccccgcgg cttcttcctc ttcgtggagg gtggtcgcat cgaccatggt 2040
catcatgaaa gcagggctta ccgggcactg actgagacga tcatgttcga cgacgccatt 2100
gagagggcgg gccagctcac cagcgaggag gacacgctga gcctcgtcac tgccgaccac 2160
tcccacgtct tctccttcgg aggctacccc ctgcgaggga gctccatctt cgggctggcc 2220
cctggcaagg cccgggacag gaaggcctac acggtcctcc tatacggaaa cggtccaggc 2280
tatgtgctca aggacggcgc ccggccggat gttaccgaga gcgagagcgg gagccccgag 2340
tatcggcagc agtcagcagt gcccctggac gaagagaccc acgcaggcga ggacgtggcg 2400
gtgttcgcgc gcggcccgca ggcgcacctg gttcacggcg tgcaggagca gaccttcata 2460
gcgcacgtca tggccttcgc cgcctgcctg gagccctaca ccgcctgcga cctggcgccc 2520
cccgccggca ccacccacca tcaccatcac cattga 2556
<210> 17
<211> 826
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized oligonucleotide
<400> 17
Leu Asp Leu Asp Ala Val Arg Ile Lys Val Asp Thr Val Asn Ala Lys
1 5 10 15
Pro Gly Asp Thr Val Arg Ile Pro Val Arg Phe Ser Gly Ile Pro Ser
20 25 30
Lys Gly Ile Ala Asn Cys Asp Phe Val Tyr Ser Tyr Asp Pro Asn Val
35 40 45
Leu Glu Ile Ile Glu Ile Lys Pro Gly Glu Leu Ile Val Asp Pro Asn
50 55 60
Pro Asp Lys Ser Phe Asp Thr Ala Val Tyr Pro Asp Arg Lys Ile Ile
65 70 75 80
Val Phe Leu Phe Ala Glu Asp Ser Gly Thr Gly Ala Tyr Ala Ile Thr
85 90 95
Lys Asp Gly Val Phe Ala Thr Ile Val Ala Lys Val Lys Ser Gly Ala
100 105 110
Pro Asn Gly Leu Ser Val Ile Lys Phe Val Glu Val Gly Gly Phe Ala
115 120 125
Asn Asn Asp Leu Val Glu Gln Lys Thr Gln Phe Phe Asp Gly Gly Val
130 135 140
Asn Val Gly Asp Thr Thr Glu Pro Ala Thr Pro Thr Thr Pro Val Thr
145 150 155 160
Thr Pro Thr Thr Thr Asp Asp Leu Asp Ala Val Arg Ile Lys Val Asp
165 170 175
Thr Val Asn Ala Lys Pro Gly Asp Thr Val Asn Ile Pro Val Arg Phe
180 185 190
Ser Gly Ile Pro Ser Lys Gly Ile Ala Asn Cys Asp Phe Val Tyr Ser
195 200 205
Tyr Asp Pro Asn Val Leu Glu Ile Ile Glu Ile Lys Pro Gly Glu Leu
210 215 220
Ile Val Asp Pro Asn Pro Thr Lys Ser Phe Asp Thr Ala Val Tyr Pro
225 230 235 240
Asp Arg Lys Met Ile Val Phe Leu Phe Ala Glu Asp Ser Gly Thr Gly
245 250 255
Ala Tyr Ala Ile Thr Lys Asp Gly Val Phe Ala Thr Ile Val Ala Lys
260 265 270
Val Lys Glu Gly Ala Pro Asn Gly Leu Ser Val Ile Lys Phe Val Glu
275 280 285
Val Gly Gly Phe Ala Asn Asn Asp Leu Val Glu Gln Lys Thr Gln Phe
290 295 300
Phe Asp Gly Gly Val Asn Val Gly Asp Thr Thr Glu Pro Ala Thr Pro
305 310 315 320
Thr Thr Pro Val Thr Thr Pro Thr Thr Thr Asp Asp Leu Asp Ala Leu
325 330 335
Glu Ile Ile Pro Val Glu Glu Glu Asn Pro Asp Phe Trp Asn Arg Glu
340 345 350
Ala Ala Glu Ala Leu Gly Ala Ala Lys Lys Leu Gln Pro Ala Gln Thr
355 360 365
Ala Ala Lys Asn Leu Ile Ile Phe Leu Gly Asp Gly Met Gly Val Ser
370 375 380
Thr Val Thr Ala Ala Arg Ile Leu Lys Gly Gln Lys Lys Asp Lys Leu
385 390 395 400
Gly Pro Glu Leu Pro Leu Ala Met Asp Arg Phe Pro Tyr Val Ala Leu
405 410 415
Ser Lys Thr Tyr Asn Val Asp Lys His Val Pro Asp Ser Gly Ala Thr
420 425 430
Ala Thr Ala Tyr Leu Cys Gly Val Lys Gly Asn Phe Gln Thr Ile Gly
435 440 445
Leu Ser Ala Ala Ala Arg Phe Asn Gln Cys Asn Thr Thr Arg Gly Asn
450 455 460
Glu Val Ile Ser Val Met Asn Arg Ala Lys Lys Ala Gly Lys Ser Val
465 470 475 480
Gly Val Val Thr Thr Thr Arg Val Gln His Ala Ser Pro Ala Gly Thr
485 490 495
Tyr Ala His Thr Val Asn Arg Asn Trp Tyr Ser Asp Ala Asp Val Pro
500 505 510
Ala Ser Ala Arg Gln Glu Gly Cys Gln Asp Ile Ala Thr Gln Leu Ile
515 520 525
Ser Asn Met Asp Ile Asp Val Ile Leu Gly Gly Gly Arg Lys Tyr Met
530 535 540
Phe Arg Met Gly Thr Pro Asp Pro Glu Tyr Pro Asp Asp Tyr Ser Gln
545 550 555 560
Gly Gly Thr Arg Leu Asp Gly Lys Asn Leu Val Gln Glu Trp Leu Ala
565 570 575
Lys Arg Gln Gly Ala Arg Tyr Val Trp Asn Arg Thr Glu Leu Met Gln
580 585 590
Ala Ser Leu Asp Pro Ser Val Thr His Leu Met Gly Leu Phe Glu Pro
595 600 605
Gly Asp Met Lys Tyr Glu Ile His Arg Asp Ser Thr Leu Asp Pro Ser
610 615 620
Leu Met Glu Met Thr Glu Ala Ala Leu Arg Leu Leu Ser Arg Asn Pro
625 630 635 640
Arg Gly Phe Phe Leu Phe Val Glu Gly Gly Arg Ile Asp His Gly His
645 650 655
His Glu Ser Arg Ala Tyr Arg Ala Leu Thr Glu Thr Ile Met Phe Asp
660 665 670
Asp Ala Ile Glu Arg Ala Gly Gln Leu Thr Ser Glu Glu Asp Thr Leu
675 680 685
Ser Leu Val Thr Ala Asp His Ser His Val Phe Ser Phe Gly Gly Tyr
690 695 700
Pro Leu Arg Gly Ser Ser Ile Phe Gly Leu Ala Pro Gly Lys Ala Arg
705 710 715 720
Asp Arg Lys Ala Tyr Thr Val Leu Leu Tyr Gly Asn Gly Pro Gly Tyr
725 730 735
Val Leu Lys Asp Gly Ala Arg Pro Asp Val Thr Glu Ser Glu Ser Gly
740 745 750
Ser Pro Glu Tyr Arg Gln Gln Ser Ala Val Pro Leu Asp Glu Glu Thr
755 760 765
His Ala Gly Glu Asp Val Ala Val Phe Ala Arg Gly Pro Gln Ala His
770 775 780
Leu Val His Gly Val Gln Glu Gln Thr Phe Ile Ala His Val Met Ala
785 790 795 800
Phe Ala Ala Cys Leu Glu Pro Tyr Thr Ala Cys Asp Leu Ala Pro Pro
805 810 815
Ala Gly Thr Thr His His His His His His
820 825
<210> 18
<211> 1326
<212> DNA
<213> Artificial
<220>
<223> Chemically synthesized oligonucleotide
<400> 18
atggatccca aaggatccct ttcctggaga atacttctgt ttctctccct ggcttttgag 60
ttgagctacg gactcgacga tctggatgca gtaaggatta aagtggacac agtaaatgca 120
aaaccgggag acacagtaag aatacctgta agattcagcg gtataccatc caagggaata 180
gcaaactgtg actttgtata cagctatgac ccgaatgtac ttgagataat agagatagaa 240
ccgggagaca taatagttga cccgaatcct gacaagagct ttgatactgc agtatatcct 300
gacagaaaga taatagtatt cctgtttgca gaagacagcg gaacaggagc gtatgcaata 360
actaaagacg gagtatttgc tacgatagta gcgaaagtaa aagaaggagc acctaacgga 420
ctcagtgtaa tcaaatttgt agaagtaggc ggatttgcga acaatgacct tgtagaacag 480
aagacacagt tctttgacgg tggagtaaat gttggagata caacagaacc tgcaacacct 540
acaacacctg taacaacacc gacaacaaca gatgatctgg atgcactcga ggcgcccctc 600
atcctgtctc ggattgtggg aggctgggag tgcgagaagc attcccaacc ctggcaggtg 660
cttgtggcct ctcgtggcag ggcagtctgc ggcggtgttc tggtgcaccc ccagtgggtc 720
ctcacagctg cccactgcat caggaacaaa agcgtgatct tgctgggtcg gcacagcctg 780
tttcatcctg aagacacagg ccaggtattt caggtcagcc acagcttccc acacccgctc 840
tacgatatga gcctcctgaa gaatcgattc ctcaggccag gtgatgactc cagccacgac 900
ctcatgctgc tccgcctgtc agagcctgcc gagctcacgg atgctgtgaa ggtcatggac 960
ctgcccaccc aggagccagc actggggacc acctgctacg cctcaggctg gggcagcatt 1020
gaaccagagg agttcttgac cccaaagaaa cttcagtgtg tggacctcca tgttatttcc 1080
aatgacgtgt gcgcgcaagt tcaccctcag aaggtgacca agttcatgct gtgtgctgga 1140
cgctggacag ggggcaaaag cacctgctcg ggtgattctg ggggcccact tgtctgtaat 1200
ggtgtgcttc aaggtatcac gtcatggggc agtgaaccat gtgccctgcc cgaaaggcct 1260
tccctgtaca ccaaggtggt gcattaccgg aagtggatca aggacaccat cgtggccaac 1320
ccctga 1326
<210> 19
<211> 417
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 19
Leu Asp Asp Leu Asp Ala Val Arg Ile Lys Val Asp Thr Val Asn Ala
1 5 10 15
Lys Pro Gly Asp Thr Val Arg Ile Pro Val Arg Phe Ser Gly Ile Pro
20 25 30
Ser Lys Gly Ile Ala Asn Cys Asp Phe Val Tyr Ser Tyr Asp Pro Asn
35 40 45
Val Leu Glu Ile Ile Glu Ile Glu Pro Gly Glu Leu Ile Val Asp Pro
50 55 60
Asn Pro Thr Lys Ser Phe Asp Thr Ala Val Tyr Pro Asp Arg Lys Met
65 70 75 80
Ile Val Phe Leu Phe Ala Glu Asp Ser Gly Thr Gly Ala Tyr Ala Ile
85 90 95
Thr Glu Asp Gly Val Phe Ala Thr Ile Val Ala Lys Val Lys Ser Gly
100 105 110
Ala Pro Asn Gly Leu Ser Val Ile Lys Phe Val Glu Val Gly Gly Phe
115 120 125
Ala Asn Asn Asp Leu Val Glu Gln Lys Thr Gln Phe Phe Asp Gly Gly
130 135 140
Val Asn Val Gly Asp Thr Thr Glu Pro Ala Thr Pro Thr Thr Pro Val
145 150 155 160
Thr Thr Pro Thr Thr Thr Asp Asp Leu Asp Ala Leu Glu Ala Pro Leu
165 170 175
Ile Leu Ser Arg Ile Val Gly Gly Trp Glu Cys Glu Lys His Ser Gln
180 185 190
Pro Trp Gln Val Leu Val Ala Ser Arg Gly Arg Ala Val Cys Gly Gly
195 200 205
Val Leu Val His Pro Gln Trp Val Leu Thr Ala Ala His Cys Ile Arg
210 215 220
Asn Lys Ser Val Ile Leu Leu Gly Arg His Ser Leu Phe His Pro Glu
225 230 235 240
Asp Thr Gly Gln Val Phe Gln Val Ser His Ser Phe Pro His Pro Leu
245 250 255
Tyr Asp Met Ser Leu Leu Lys Asn Arg Phe Leu Arg Pro Gly Asp Asp
260 265 270
Ser Ser His Asp Leu Met Leu Leu Arg Leu Ser Glu Pro Ala Glu Leu
275 280 285
Thr Asp Ala Val Lys Val Met Asp Leu Pro Thr Gln Glu Pro Ala Leu
290 295 300
Gly Thr Thr Cys Tyr Ala Ser Gly Trp Gly Ser Ile Glu Pro Glu Glu
305 310 315 320
Phe Leu Thr Pro Lys Lys Leu Gln Cys Val Asp Leu His Val Ile Ser
325 330 335
Asn Asp Val Cys Ala Gln Val His Pro Gln Lys Val Thr Lys Phe Met
340 345 350
Leu Cys Ala Gly Arg Trp Thr Gly Gly Lys Ser Thr Cys Ser Gly Asp
355 360 365
Ser Gly Gly Pro Leu Val Cys Asn Gly Val Leu Gln Gly Ile Thr Ser
370 375 380
Trp Gly Ser Glu Pro Cys Ala Leu Pro Glu Arg Pro Ser Leu Tyr Thr
385 390 395 400
Lys Val Val His Tyr Arg Lys Trp Ile Lys Asp Thr Ile Val Ala Asn
405 410 415
Pro
<210> 20
<211> 1554
<212> DNA
<213> Artificial
<220>
<223> Chemically synthesized oligonucleotide
<400> 20
atggatccca aaggatccct ttcctggaga atacttctgt ttctctccct ggcttttgag 60
ttgagctacg gactcgacga tctggatgca gtaaggatta aagtggacac agtaaatgca 120
aaaccgggag acacagtaag aatacctgta agattcagcg gtataccatc caagggaata 180
gcaaactgtg actttgtata cagctatgac ccgaatgtac ttgagataat agagatagaa 240
ccgggagaca taatagttga cccgaatcct gacaagagct ttgatactgc agtatatcct 300
gacagaaaga taatagtatt cctgtttgca gaagacagcg gaacaggagc gtatgcaata 360
actaaagacg gagtatttgc tacgatagta gcgaaagtaa aagaaggagc acctaacgga 420
ctcagtgtaa tcaaatttgt agaagtaggc ggatttgcga acaatgacct tgtagaacag 480
aagacacagt tctttgacgg tggagtaaat gttggagata caacagaacc tgcaacacct 540
acaacacctg taacaacacc gacaacaaca gatgatctgg atgcactcga ggatcagatt 600
tgcattggtt accatgcaaa caactcgaca gagcaggttg acacaataat ggaaaagaac 660
gttactgtta cacatgccca agacatactg gaaaagaaac acaacgggaa gctctgcgat 720
ctagatggag tgaagcctct aattttgaga gattgtagcg tagctggatg gctcctcgga 780
aacccaatgt gtgacgaatt catcaatgtg ccggaatggt cttacatagt ggagaaggcc 840
aatccagtca atgacctctg ttacccaggg gatttcaatg actatgaaaa attgaaacac 900
ctattgagca gaataaacca ttttgagaaa attcagatca tccccaaaag ttcttggtcc 960
agtcatgaag cctcattagg ggtgagctca gcatgtccat accagggaaa gtcctccttt 1020
ttcagaaatg tggtatggct tatcaaaaag aacagtacat acccaacaat aaagaggagc 1080
tacaataata ccaaccaaga agatcttttg gtactgtggg ggattcacca tcctaatgat 1140
gcggcagagc agacaaagct ctatcaaaac ccaaccacct atatttccgt tgggacatca 1200
acactaaacc agagattggt accaagaata gctactagat ccaaagtaaa cgggcaaagt 1260
ggaaggatgg agttcttctg gacaatttta aagccgaatg atgcaatcaa cttcgagagt 1320
aatggaaatt tcattgctcc agaatatgca tacaaaattg tcaagaaagg ggactcaaca 1380
attatgaaaa gtgaattgga atatggtaac tgcaacacca agtgtcaaac tccaatgggg 1440
gcgataaact ctagcatgcc attccacaat atacaccctc tcaccattgg ggaatgcccc 1500
aaatatgtga aatcaaacag attagtcctt gcgcaccatc accatcacca ttga 1554
<210> 21
<211> 493
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 21
Leu Asp Asp Leu Asp Ala Val Arg Ile Lys Val Asp Thr Val Asn Ala
1 5 10 15
Lys Pro Gly Asp Thr Val Arg Ile Pro Val Arg Phe Ser Gly Ile Pro
20 25 30
Ser Lys Gly Ile Ala Asn Cys Asp Phe Val Tyr Ser Tyr Asp Pro Asn
35 40 45
Val Leu Glu Ile Ile Glu Ile Glu Pro Gly Glu Leu Ile Val Asp Pro
50 55 60
Asn Pro Thr Lys Ser Phe Asp Thr Ala Val Tyr Pro Asp Arg Lys Met
65 70 75 80
Ile Val Phe Leu Phe Ala Glu Asp Ser Gly Thr Gly Ala Tyr Ala Ile
85 90 95
Thr Glu Asp Gly Val Phe Ala Thr Ile Val Ala Lys Val Lys Ser Gly
100 105 110
Ala Pro Asn Gly Leu Ser Val Ile Lys Phe Val Glu Val Gly Gly Phe
115 120 125
Ala Asn Asn Asp Leu Val Glu Gln Lys Thr Gln Phe Phe Asp Gly Gly
130 135 140
Val Asn Val Gly Asp Thr Thr Glu Pro Ala Thr Pro Thr Thr Pro Val
145 150 155 160
Thr Thr Pro Thr Thr Thr Asp Asp Leu Asp Ala Leu Glu Asp Gln Ile
165 170 175
Cys Ile Gly Tyr His Ala Asn Asn Ser Thr Glu Gln Val Asp Thr Ile
180 185 190
Met Glu Lys Asn Val Thr Val Thr His Ala Gln Asp Ile Leu Glu Lys
195 200 205
Lys His Asn Gly Lys Leu Cys Asp Leu Asp Gly Val Lys Pro Leu Ile
210 215 220
Leu Arg Asp Cys Ser Val Ala Gly Trp Leu Leu Gly Asn Pro Met Cys
225 230 235 240
Asp Glu Phe Ile Asn Val Pro Glu Trp Ser Tyr Ile Val Glu Lys Ala
245 250 255
Asn Pro Val Asn Asp Leu Cys Tyr Pro Gly Asp Phe Asn Asp Tyr Glu
260 265 270
Lys Leu Lys His Leu Leu Ser Arg Ile Asn His Phe Glu Lys Ile Gln
275 280 285
Ile Ile Pro Lys Ser Ser Trp Ser Ser His Glu Ala Ser Leu Gly Val
290 295 300
Ser Ser Ala Cys Pro Tyr Gln Gly Lys Ser Ser Phe Phe Arg Asn Val
305 310 315 320
Val Trp Leu Ile Lys Lys Asn Ser Thr Tyr Pro Thr Ile Lys Arg Ser
325 330 335
Tyr Asn Asn Thr Asn Gln Glu Asp Leu Leu Val Leu Trp Gly Ile His
340 345 350
His Pro Asn Asp Ala Ala Glu Gln Thr Lys Leu Tyr Gln Asn Pro Thr
355 360 365
Thr Tyr Ile Ser Val Gly Thr Ser Thr Leu Asn Gln Arg Leu Val Pro
370 375 380
Arg Ile Ala Thr Arg Ser Lys Val Asn Gly Gln Ser Gly Arg Met Glu
385 390 395 400
Phe Phe Trp Thr Ile Leu Lys Pro Asn Asp Ala Ile Asn Phe Glu Ser
405 410 415
Asn Gly Asn Phe Ile Ala Pro Glu Tyr Ala Tyr Lys Ile Val Lys Lys
420 425 430
Gly Asp Ser Thr Ile Met Lys Ser Glu Leu Glu Tyr Gly Asn Cys Asn
435 440 445
Thr Lys Cys Gln Thr Pro Met Gly Ala Ile Asn Ser Ser Met Pro Phe
450 455 460
His Asn Ile His Pro Leu Thr Ile Gly Glu Cys Pro Lys Tyr Val Lys
465 470 475 480
Ser Asn Arg Leu Val Leu Ala His His His His His His
485 490
<210> 22
<211> 1293
<212> DNA
<213> Artificial
<220>
<223> Chemically synthesized oligonucleotide
<400> 22
atggatctgg atgcagtaag gattaaagtg gacacagtaa atgcaaaacc gggagacaca 60
gtaaatatac ctgtaagatt cagtggtata ccatccaagg gaatagcaaa ctgtgacttt 120
gtatacagct atgacccgaa tgtacttgag ataatagaga taaaaccggg agaattgata 180
gttgacccga atcctaccaa gagctttgat actgcagtat atcctgacag aaagatgata 240
gtattcctgt ttgcggaaga cagcggaaca ggagcgtatg caataactaa agacggagta 300
tttgctacga tagtagcgaa agtaaaagaa ggagcaccta acgggctcag tgtaatcaaa 360
tttgtagaag taggcggatt tgcgaacaat gaccttgtag aacagaagac acagttcttt 420
gacggtggag taaatgttgg agatacaaca gaacctgcaa cacctacaac acctgtaaca 480
acaccgacaa caacagatga tctggatgca gctagccttc taaccgaggt cgaaacgtac 540
gttctctcta tcatcccgtc aggccccctc aaagccgaga tcgcacagag acttgaagat 600
gtctttgcag ggaagaacac cgatcttgag gttctcatgg aatggctaaa gacaagacca 660
atcctgtcac ctctgactaa ggggatttta ggatttgtgt tcacgctcac cgtgcccagt 720
gagcggggac tgcagcgtag acgctttgtc caaaatgctc ttaatgggaa cggagatcca 780
aataacatgg acaaagcagt taaactgtat aggaagctta agagggagat aacattccat 840
ggggccaaag aaatagcact cagttattct gctggtgcac ttgccagttg tatgggcctc 900
atatacaaca ggatgggggc tgtgaccact gaagtggcat ttggcctggt atgcgcaacc 960
tgtgaacaga ttgctgactc ccagcatcgg tctcataggc aaatggtgac aacaaccaat 1020
ccactaatca gacatgagaa cagaatggtt ctagccagca ctacagctaa ggctatggag 1080
caaatggctg gatcgagtga gcaagcagca gaggccatgg atattgctag tcaggccagg 1140
caaatggtgc aggcgatgag aaccattggg actcatccta gctccagtgc tggtctaaaa 1200
gatgatcttc ttgaaaattt gcaggcttac cagaaacgga tgggggtgca gatgcagcga 1260
ttcaagctcg agcaccacca ccaccaccac tga 1293
<210> 23
<211> 430
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 23
Met Asp Leu Asp Ala Val Arg Ile Lys Val Asp Thr Val Asn Ala Lys
1 5 10 15
Pro Gly Asp Thr Val Asn Ile Pro Val Arg Phe Ser Gly Ile Pro Ser
20 25 30
Lys Gly Ile Ala Asn Cys Asp Phe Val Tyr Ser Tyr Asp Pro Asn Val
35 40 45
Leu Glu Ile Ile Glu Ile Lys Pro Gly Glu Leu Ile Val Asp Pro Asn
50 55 60
Pro Thr Lys Ser Phe Asp Thr Ala Val Tyr Pro Asp Arg Lys Met Ile
65 70 75 80
Val Phe Leu Phe Ala Glu Asp Ser Gly Thr Gly Ala Tyr Ala Ile Thr
85 90 95
Lys Asp Gly Val Phe Ala Thr Ile Val Ala Lys Val Lys Glu Gly Ala
100 105 110
Pro Asn Gly Leu Ser Val Ile Lys Phe Val Glu Val Gly Gly Phe Ala
115 120 125
Asn Asn Asp Leu Val Glu Gln Lys Thr Gln Phe Phe Asp Gly Gly Val
130 135 140
Asn Val Gly Asp Thr Thr Glu Pro Ala Thr Pro Thr Thr Pro Val Thr
145 150 155 160
Thr Pro Thr Thr Thr Asp Asp Leu Asp Ala Ala Ser Leu Leu Thr Glu
165 170 175
Val Glu Thr Tyr Val Leu Ser Ile Ile Pro Ser Gly Pro Leu Lys Ala
180 185 190
Glu Ile Ala Gln Arg Leu Glu Asp Val Phe Ala Gly Lys Asn Thr Asp
195 200 205
Leu Glu Val Leu Met Glu Trp Leu Lys Thr Arg Pro Ile Leu Ser Pro
210 215 220
Leu Thr Lys Gly Ile Leu Gly Phe Val Phe Thr Leu Thr Val Pro Ser
225 230 235 240
Glu Arg Gly Leu Gln Arg Arg Arg Phe Val Gln Asn Ala Leu Asn Gly
245 250 255
Asn Gly Asp Pro Asn Asn Met Asp Lys Ala Val Lys Leu Tyr Arg Lys
260 265 270
Leu Lys Arg Glu Ile Thr Phe His Gly Ala Lys Glu Ile Ala Leu Ser
275 280 285
Tyr Ser Ala Gly Ala Leu Ala Ser Cys Met Gly Leu Ile Tyr Asn Arg
290 295 300
Met Gly Ala Val Thr Thr Glu Val Ala Phe Gly Leu Val Cys Ala Thr
305 310 315 320
Cys Glu Gln Ile Ala Asp Ser Gln His Arg Ser His Arg Gln Met Val
325 330 335
Thr Thr Thr Asn Pro Leu Ile Arg His Glu Asn Arg Met Val Leu Ala
340 345 350
Ser Thr Thr Ala Lys Ala Met Glu Gln Met Ala Gly Ser Ser Glu Gln
355 360 365
Ala Ala Glu Ala Met Asp Ile Ala Ser Gln Ala Arg Gln Met Val Gln
370 375 380
Ala Met Arg Thr Ile Gly Thr His Pro Ser Ser Ser Ala Gly Leu Lys
385 390 395 400
Asp Asp Leu Leu Glu Asn Leu Gln Ala Tyr Gln Lys Arg Met Gly Val
405 410 415
Gln Met Gln Arg Phe Lys Leu Glu His His His His His His
420 425 430
<210> 24
<211> 9
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 24
Gly Ile Leu Gly Phe Val Phe Thr Leu
1 5
<210> 25
<211> 661
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 25
Met Asp Leu Val Leu Lys Arg Cys Leu Leu His Leu Ala Val Ile Gly
1 5 10 15
Ala Leu Leu Ala Val Gly Ala Thr Lys Val Pro Arg Asn Gln Asp Trp
20 25 30
Leu Gly Val Ser Arg Gln Leu Arg Thr Lys Ala Trp Asn Arg Gln Leu
35 40 45
Tyr Pro Glu Trp Thr Glu Ala Gln Arg Leu Asp Cys Trp Arg Gly Gly
50 55 60
Gln Val Ser Leu Lys Val Ser Asn Asp Gly Pro Thr Leu Ile Gly Ala
65 70 75 80
Asn Ala Ser Phe Ser Ile Ala Leu Asn Phe Pro Gly Ser Gln Lys Val
85 90 95
Leu Pro Asp Gly Gln Val Ile Trp Val Asn Asn Thr Ile Ile Asn Gly
100 105 110
Ser Gln Val Trp Gly Gly Gln Pro Val Tyr Pro Gln Glu Thr Asp Asp
115 120 125
Ala Cys Ile Phe Pro Asp Gly Gly Pro Cys Pro Ser Gly Ser Trp Ser
130 135 140
Gln Lys Arg Ser Phe Val Tyr Val Trp Lys Thr Trp Gly Gln Tyr Trp
145 150 155 160
Gln Val Leu Gly Gly Pro Val Ser Gly Leu Ser Ile Gly Thr Gly Arg
165 170 175
Ala Met Leu Gly Thr His Thr Met Glu Val Thr Val Tyr His Arg Arg
180 185 190
Gly Ser Arg Ser Tyr Val Pro Leu Ala His Ser Ser Ser Ala Phe Thr
195 200 205
Ile Thr Asp Gln Val Pro Phe Ser Val Ser Val Ser Gln Leu Arg Ala
210 215 220
Leu Asp Gly Gly Asn Lys His Phe Leu Arg Asn Gln Pro Leu Thr Phe
225 230 235 240
Ala Leu Gln Leu His Asp Pro Ser Gly Tyr Leu Ala Glu Ala Asp Leu
245 250 255
Ser Tyr Thr Trp Asp Phe Gly Asp Ser Ser Gly Thr Leu Ile Ser Arg
260 265 270
Ala Leu Val Val Thr His Thr Tyr Leu Glu Pro Gly Pro Val Thr Ala
275 280 285
Gln Val Val Leu Gln Ala Ala Ile Pro Leu Thr Ser Cys Gly Ser Ser
290 295 300
Pro Val Pro Gly Thr Thr Asp Gly His Arg Pro Thr Ala Glu Ala Pro
305 310 315 320
Asn Thr Thr Ala Gly Gln Val Pro Thr Thr Glu Val Val Gly Thr Thr
325 330 335
Pro Gly Gln Ala Pro Thr Ala Glu Pro Ser Gly Thr Thr Ser Val Gln
340 345 350
Val Pro Thr Thr Glu Val Ile Ser Thr Ala Pro Val Gln Met Pro Thr
355 360 365
Ala Glu Ser Thr Gly Met Thr Pro Glu Lys Val Pro Val Ser Glu Val
370 375 380
Met Gly Thr Thr Leu Ala Glu Met Ser Thr Pro Glu Ala Thr Gly Met
385 390 395 400
Thr Pro Ala Glu Val Ser Ile Val Val Leu Ser Gly Thr Thr Ala Ala
405 410 415
Gln Val Thr Thr Thr Glu Trp Val Glu Thr Thr Ala Arg Glu Leu Pro
420 425 430
Ile Pro Glu Pro Glu Gly Pro Asp Ala Ser Ser Ile Met Ser Thr Glu
435 440 445
Ser Ile Thr Gly Ser Leu Gly Pro Leu Leu Asp Gly Thr Ala Thr Leu
450 455 460
Arg Leu Val Lys Arg Gln Val Pro Leu Asp Cys Val Leu Tyr Arg Tyr
465 470 475 480
Gly Ser Phe Ser Val Thr Leu Asp Ile Val Gln Gly Ile Glu Ser Ala
485 490 495
Glu Ile Leu Gln Ala Val Pro Ser Gly Glu Gly Asp Ala Phe Glu Leu
500 505 510
Thr Val Ser Cys Gln Gly Gly Leu Pro Lys Glu Ala Cys Met Glu Ile
515 520 525
Ser Ser Pro Gly Cys Gln Pro Pro Ala Gln Arg Leu Cys Gln Pro Val
530 535 540
Leu Pro Ser Pro Ala Cys Gln Leu Val Leu His Gln Ile Leu Lys Gly
545 550 555 560
Gly Ser Gly Thr Tyr Cys Leu Asn Val Ser Leu Ala Asp Thr Asn Ser
565 570 575
Leu Ala Val Val Ser Thr Gln Leu Ile Met Pro Gly Gln Glu Ala Gly
580 585 590
Leu Gly Gln Val Pro Leu Ile Val Gly Ile Leu Leu Val Leu Met Ala
595 600 605
Val Val Leu Ala Ser Leu Ile Tyr Arg Arg Arg Leu Met Lys Gln Asp
610 615 620
Phe Ser Val Pro Gln Leu Pro His Ser Ser Ser His Trp Leu Arg Leu
625 630 635 640
Pro Arg Ile Phe Cys Ser Cys Pro Ile Gly Glu Asn Ser Pro Leu Leu
645 650 655
Ser Gly Gln Gln Val
660
<210> 26
<211> 9
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 26
Lys Thr Trp Gly Gln Tyr Trp Gln Val
1 5
<210> 27
<211> 9
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 27
Ile Met Asp Gln Val Pro Phe Ser Val
1 5
<210> 28
<211> 9
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 28
Ile Thr Asp Gln Val Pro Phe Ser Val
1 5
<210> 29
<211> 9
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 29
Tyr Leu Glu Pro Gly Pro Val Thr Val
1 5
<210> 30
<211> 9
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 30
Tyr Leu Glu Pro Gly Pro Val Thr Ala
1 5
<210> 31
<211> 204
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 31
Met Asp Leu Asp Ala Val Arg Ile Lys Val Asp Thr Val Asn Ala Lys
1 5 10 15
Pro Gly Asp Thr Val Asn Ile Pro Val Arg Phe Ser Gly Ile Pro Ser
20 25 30
Lys Gly Ile Ala Asn Cys Asp Phe Val Tyr Ser Tyr Asp Pro Asn Val
35 40 45
Leu Glu Ile Ile Glu Ile Lys Pro Gly Glu Leu Ile Val Asp Pro Asn
50 55 60
Pro Thr Lys Ser Phe Asp Thr Ala Val Tyr Pro Asp Arg Lys Met Ile
65 70 75 80
Val Phe Leu Phe Ala Glu Asp Ser Gly Thr Gly Ala Tyr Ala Ile Thr
85 90 95
Lys Asp Gly Val Phe Ala Thr Ile Val Ala Lys Val Lys Glu Gly Ala
100 105 110
Pro Asn Gly Leu Ser Val Ile Lys Phe Val Glu Val Gly Gly Phe Ala
115 120 125
Asn Asn Asp Leu Val Glu Gln Lys Thr Gln Phe Phe Asp Gly Gly Val
130 135 140
Asn Val Gly Asp Thr Thr Glu Pro Ala Thr Pro Thr Thr Pro Val Thr
145 150 155 160
Thr Pro Thr Thr Thr Asp Asp Leu Asp Ala Ala Arg Ser Ala Phe Thr
165 170 175
Ile Met Asp Gln Val Pro Phe Ser Val Ser Val Ser Ala Ser Arg Lys
180 185 190
Gly Ala Ala Ala Leu Glu His His His His His His
195 200
<210> 32
<211> 118
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 32
Met Pro Arg Glu Asp Ala His Phe Ile Tyr Gly Tyr Pro Lys Lys Gly
1 5 10 15
His Gly His Ser Tyr Thr Thr Ala Glu Glu Ala Ala Gly Ile Gly Ile
20 25 30
Leu Thr Val Ile Leu Gly Val Leu Leu Leu Ile Gly Cys Trp Tyr Cys
35 40 45
Arg Arg Arg Asn Gly Tyr Arg Ala Leu Met Asp Lys Ser Leu His Val
50 55 60
Gly Thr Gln Cys Ala Leu Thr Arg Arg Cys Pro Gln Glu Gly Phe Asp
65 70 75 80
His Arg Asp Ser Lys Val Ser Leu Gln Glu Lys Asn Cys Glu Pro Val
85 90 95
Val Pro Asn Ala Pro Pro Ala Tyr Glu Lys Leu Ser Ala Glu Gln Ser
100 105 110
Pro Pro Pro Tyr Ser Pro
115
<210> 33
<211> 9
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 33
Ala Ala Gly Ile Gly Ile Leu Thr Val
1 5
<210> 34
<211> 10
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 34
Glu Ala Ala Gly Ile Gly Ile Leu Thr Val
1 5 10
<210> 35
<211> 10
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 35
Glu Leu Ala Gly Ile Gly Ile Leu Thr Val
1 5 10
<210> 36
<211> 204
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 36
Met Asp Leu Asp Ala Val Arg Ile Lys Val Asp Thr Val Asn Ala Lys
1 5 10 15
Pro Gly Asp Thr Val Asn Ile Pro Val Arg Phe Ser Gly Ile Pro Ser
20 25 30
Lys Gly Ile Ala Asn Cys Asp Phe Val Tyr Ser Tyr Asp Pro Asn Val
35 40 45
Leu Glu Ile Ile Glu Ile Lys Pro Gly Glu Leu Ile Val Asp Pro Asn
50 55 60
Pro Thr Lys Ser Phe Asp Thr Ala Val Tyr Pro Asp Arg Lys Met Ile
65 70 75 80
Val Phe Leu Phe Ala Glu Asp Ser Gly Thr Gly Ala Tyr Ala Ile Thr
85 90 95
Lys Asp Gly Val Phe Ala Thr Ile Val Ala Lys Val Lys Glu Gly Ala
100 105 110
Pro Asn Gly Leu Ser Val Ile Lys Phe Val Glu Val Gly Gly Phe Ala
115 120 125
Asn Asn Asp Leu Val Glu Gln Lys Thr Gln Phe Phe Asp Gly Gly Val
130 135 140
Asn Val Gly Asp Thr Thr Glu Pro Ala Thr Pro Thr Thr Pro Val Thr
145 150 155 160
Thr Pro Thr Thr Thr Asp Asp Leu Asp Ala Ala Arg Thr Ala Glu Glu
165 170 175
Leu Ala Gly Ile Gly Ile Leu Thr Val Ile Leu Gly Ala Ser Arg Lys
180 185 190
Gly Ala Ala Ala Leu Glu His His His His His His
195 200
<210> 37
<211> 241
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 37
Met Asp Leu Asp Ala Val Arg Ile Lys Val Asp Thr Val Asn Ala Lys
1 5 10 15
Pro Gly Asp Thr Val Asn Ile Pro Val Arg Phe Ser Gly Ile Pro Ser
20 25 30
Lys Gly Ile Ala Asn Cys Asp Phe Val Tyr Ser Tyr Asp Pro Asn Val
35 40 45
Leu Glu Ile Ile Glu Ile Lys Pro Gly Glu Leu Ile Val Asp Pro Asn
50 55 60
Pro Thr Lys Ser Phe Asp Thr Ala Val Tyr Pro Asp Arg Lys Met Ile
65 70 75 80
Val Phe Leu Phe Ala Glu Asp Ser Gly Thr Gly Ala Tyr Ala Ile Thr
85 90 95
Lys Asp Gly Val Phe Ala Thr Ile Val Ala Lys Val Lys Glu Gly Ala
100 105 110
Pro Asn Gly Leu Ser Val Ile Lys Phe Val Glu Val Gly Gly Phe Ala
115 120 125
Asn Asn Asp Leu Val Glu Gln Lys Thr Gln Phe Phe Asp Gly Gly Val
130 135 140
Asn Val Gly Asp Thr Thr Glu Pro Ala Thr Pro Thr Thr Pro Val Thr
145 150 155 160
Thr Pro Thr Thr Thr Asp Asp Leu Asp Ala Ala Ser Asp Thr Thr Glu
165 170 175
Ala Arg His Pro His Pro Pro Val Thr Thr Pro Thr Thr Asp Arg Lys
180 185 190
Gly Thr Thr Ala Glu Glu Leu Ala Gly Ile Gly Ile Leu Thr Val Ile
195 200 205
Leu Gly Gly Lys Arg Thr Asn Asn Ser Thr Pro Thr Lys Gly Glu Phe
210 215 220
Cys Arg Tyr Pro Ser His Trp Arg Pro Leu Glu His His His His His
225 230 235 240
His
<210> 38
<211> 66
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 38
Ala Ser Asp Thr Thr Glu Ala Arg His Pro His Pro Pro Val Thr Thr
1 5 10 15
Pro Thr Thr Thr Asp Arg Lys Gly Thr Thr Ala Glu Glu Leu Ala Gly
20 25 30
Ile Gly Ile Leu Thr Val Ile Leu Gly Gly Lys Arg Thr Asn Asn Ser
35 40 45
Thr Pro Thr Lys Gly Glu Phe Cys Arg Tyr Pro Ser His Trp Arg Pro
50 55 60
Arg Leu
65
<210> 39
<211> 57
<212> DNA
<213> Artificial
<220>
<223> Chemically synthesized oligonucleotide
<400> 39
cacggtcacc gtctccaaag cttccggagc tagcgagggc ggcagcctgg ccgcgct 57
<210> 40
<211> 70
<212> DNA
<213> Artificial
<220>
<223> Chemically synthesized oligonucleotide
<400> 40
ggccggctcc tgcgaaggga gccggccggt cgcggccgct tacttcaggt cctcgcgcgg 60
cggtttgccg 70
<210> 41
<211> 518
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 41
Met Asp Leu Asp Ala Val Arg Ile Lys Val Asp Thr Val Asn Ala Lys
1 5 10 15
Pro Gly Asp Thr Val Asn Ile Pro Val Arg Phe Ser Gly Ile Pro Ser
20 25 30
Lys Gly Ile Ala Asn Cys Asp Phe Val Tyr Ser Tyr Asp Pro Asn Val
35 40 45
Leu Glu Ile Ile Glu Ile Lys Pro Gly Glu Leu Ile Val Asp Pro Asn
50 55 60
Pro Thr Lys Ser Phe Asp Thr Ala Val Tyr Pro Asp Arg Lys Met Ile
65 70 75 80
Val Phe Leu Phe Ala Glu Asp Ser Gly Thr Gly Ala Tyr Ala Ile Thr
85 90 95
Lys Asp Gly Val Phe Ala Thr Ile Val Ala Lys Val Lys Glu Gly Ala
100 105 110
Pro Asn Gly Leu Ser Val Ile Lys Phe Val Glu Val Gly Gly Phe Ala
115 120 125
Asn Asn Asp Leu Val Glu Gln Lys Thr Gln Phe Phe Asp Gly Gly Val
130 135 140
Asn Val Gly Asp Thr Thr Glu Pro Ala Thr Pro Thr Thr Pro Val Thr
145 150 155 160
Thr Pro Thr Thr Thr Asp Asp Leu Asp Ala Ala Ser Glu Gly Gly Ser
165 170 175
Leu Ala Ala Leu Thr Ala His Gln Ala Cys His Leu Pro Leu Glu Thr
180 185 190
Phe Thr Arg His Arg Gln Pro Arg Gly Trp Glu Gln Leu Glu Gln Cys
195 200 205
Gly Tyr Pro Val Gln Arg Leu Val Ala Leu Tyr Leu Ala Ala Arg Leu
210 215 220
Ser Trp Asn Gln Val Asp Gln Val Ile Arg Asn Ala Leu Ala Ser Pro
225 230 235 240
Gly Ser Gly Gly Asp Leu Gly Glu Ala Ile Arg Glu Gln Pro Glu Gln
245 250 255
Ala Arg Leu Ala Leu Thr Leu Ala Ala Ala Glu Ser Glu Arg Phe Val
260 265 270
Arg Gln Gly Thr Gly Asn Asp Glu Ala Gly Ala Ala Asn Gly Pro Ala
275 280 285
Asp Ser Gly Asp Ala Leu Leu Glu Arg Asn Tyr Pro Thr Gly Ala Glu
290 295 300
Phe Leu Gly Asp Gly Gly Asp Val Ser Phe Ser Thr Arg Gly Thr Gln
305 310 315 320
Asn Trp Thr Val Glu Arg Leu Leu Gln Ala His Arg Gln Leu Glu Glu
325 330 335
Arg Gly Tyr Val Phe Val Gly Tyr His Gly Thr Phe Leu Glu Ala Ala
340 345 350
Gln Ser Ile Val Phe Gly Gly Val Arg Ala Arg Ser Gln Asp Leu Asp
355 360 365
Ala Ile Trp Arg Gly Phe Tyr Ile Ala Gly Asp Pro Ala Leu Ala Tyr
370 375 380
Gly Tyr Ala Gln Asp Gln Glu Pro Asp Ala Arg Gly Arg Ile Arg Asn
385 390 395 400
Gly Ala Leu Leu Arg Val Tyr Val Pro Arg Ser Ser Leu Pro Gly Phe
405 410 415
Tyr Arg Thr Ser Leu Thr Leu Ala Ala Pro Glu Ala Ala Gly Glu Val
420 425 430
Glu Arg Leu Ile Gly His Pro Leu Pro Leu Arg Leu Asp Ala Ile Thr
435 440 445
Gly Pro Glu Glu Glu Gly Gly Arg Leu Glu Thr Ile Leu Gly Trp Pro
450 455 460
Leu Ala Glu Arg Thr Val Val Ile Pro Ser Ala Ile Pro Thr Asp Pro
465 470 475 480
Arg Asn Val Gly Gly Asp Leu Asp Pro Ser Ser Ile Pro Asp Lys Glu
485 490 495
Gln Ala Ile Ser Ala Leu Pro Asp Tyr Ala Ser Gln Pro Gly Lys Pro
500 505 510
Pro Arg Glu Asp Leu Lys
515
<210> 42
<211> 614
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 42
Gln Ile Gln Leu Val Gln Ser Gly Pro Glu Leu Lys Lys Pro Gly Glu
1 5 10 15
Thr Val Lys Ile Ser Cys Lys Ala Ser Gly Tyr Ser Phe Thr Asn Tyr
20 25 30
Gly Met Asn Trp Val Lys Gln Ala Pro Gly Lys Gly Leu Lys Trp Met
35 40 45
Gly Trp Ile Asn Thr Tyr Thr Gly Glu Ser Thr Tyr Ala Asp Asp Phe
50 55 60
Lys Gly Arg Phe Ala Phe Ser Leu Glu Thr Ser Ala Ser Thr Ala Tyr
65 70 75 80
Leu Gln Ile Ser Asn Leu Lys Asn Glu Asp Met Ala Thr Tyr Phe Cys
85 90 95
Ala Arg Gly Asp Phe Arg Tyr Tyr Tyr Phe Asp Tyr Trp Gly Gln Gly
100 105 110
Thr Thr Leu Thr Gly Ser Ser Ala Lys Thr Lys Gly Pro Ser Val Phe
115 120 125
Pro Leu Ala Pro Cys Ser Arg Ser Thr Ser Glu Ser Thr Ala Ala Leu
130 135 140
Gly Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp
145 150 155 160
Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu
165 170 175
Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser
180 185 190
Ser Ser Leu Gly Thr Lys Thr Tyr Thr Cys Asn Val Asp His Lys Pro
195 200 205
Ser Asn Thr Lys Val Asp Lys Arg Val Glu Ser Lys Tyr Gly Pro Pro
210 215 220
Cys Pro Pro Cys Pro Ala Pro Glu Phe Glu Gly Gly Pro Ser Val Phe
225 230 235 240
Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr Pro
245 250 255
Glu Val Thr Cys Val Val Val Asp Val Ser Gln Glu Asp Pro Glu Val
260 265 270
Gln Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys Thr
275 280 285
Lys Pro Arg Glu Glu Gln Phe Asn Ser Thr Tyr Arg Val Val Ser Val
290 295 300
Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys Cys
305 310 315 320
Lys Val Ser Asn Lys Gly Leu Pro Ser Ser Ile Glu Lys Thr Ile Ser
325 330 335
Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro Pro
340 345 350
Ser Gln Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu Val
355 360 365
Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn Gly
370 375 380
Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser Asp
385 390 395 400
Gly Ser Phe Phe Leu Tyr Ser Arg Leu Thr Val Asp Lys Ser Arg Trp
405 410 415
Gln Glu Gly Asn Val Phe Ser Cys Ser Val Met His Glu Ala Leu His
420 425 430
Asn His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Leu Gly Lys Ala Ser
435 440 445
Thr Thr Glu Pro Ala Thr Pro Thr Thr Pro Val Thr Thr Pro Thr Thr
450 455 460
Thr Asp Asp Leu Asp Ala Val Arg Ile Lys Val Asp Thr Val Asn Ala
465 470 475 480
Lys Pro Gly Asp Thr Val Asn Ile Pro Val Arg Phe Ser Gly Ile Pro
485 490 495
Ser Lys Gly Ile Ala Asn Cys Asp Phe Val Tyr Ser Tyr Asp Pro Asn
500 505 510
Val Leu Glu Ile Ile Glu Ile Lys Pro Gly Glu Leu Ile Val Asp Pro
515 520 525
Asn Pro Thr Lys Ser Phe Asp Thr Ala Val Tyr Pro Asp Arg Lys Met
530 535 540
Ile Val Phe Leu Phe Ala Glu Asp Ser Gly Thr Gly Ala Tyr Ala Ile
545 550 555 560
Thr Lys Asp Gly Val Phe Ala Thr Ile Val Ala Lys Val Lys Glu Gly
565 570 575
Ala Pro Asn Gly Leu Ser Val Ile Lys Phe Val Glu Val Gly Gly Phe
580 585 590
Ala Asn Asn Asp Leu Val Glu Gln Lys Thr Gln Phe Phe Asp Gly Gly
595 600 605
Val Asn Val Gly Asp Thr
610
<210> 43
<211> 308
<212> PRT
<213> Artificial
<220>
<223> Chemically synthesized peptide
<400> 43
Leu Asp Asp Leu Asp Ala Val Arg Ile Lys Val Asp Thr Val Asn Ala
1 5 10 15
Lys Pro Gly Asp Thr Val Arg Ile Pro Val Arg Phe Ser Gly Ile Pro
20 25 30
Ser Lys Gly Ile Ala Asn Cys Asp Phe Val Tyr Ser Tyr Asp Pro Asn
35 40 45
Val Leu Glu Ile Ile Glu Ile Glu Pro Gly Asp Ile Ile Val Asp Pro
50 55 60
Asn Pro Asp Lys Ser Phe Asp Thr Ala Val Tyr Pro Asp Arg Lys Ile
65 70 75 80
Ile Val Phe Leu Phe Ala Glu Asp Ser Gly Thr Gly Ala Tyr Ala Ile
85 90 95
Thr Lys Asp Gly Val Phe Ala Thr Ile Val Ala Lys Val Lys Glu Gly
100 105 110
Ala Pro Asn Gly Leu Ser Val Ile Lys Phe Val Glu Val Gly Gly Phe
115 120 125
Ala Asn Asn Asp Leu Val Glu Gln Lys Thr Gln Phe Phe Asp Gly Gly
130 135 140
Val Asn Val Gly Asp Thr Thr Glu Pro Ala Thr Pro Thr Thr Pro Val
145 150 155 160
Thr Thr Pro Thr Thr Thr Asp Asp Leu Asp Ala Leu Glu Ala Asp Gln
165 170 175
Gly Gln Asp Arg His Met Ile Arg Met Arg Gln Leu Ile Asp Ile Val
180 185 190
Asp Gln Leu Lys Asn Tyr Val Asn Asp Leu Val Pro Glu Phe Leu Pro
195 200 205
Ala Pro Glu Asp Val Glu Thr Asn Cys Glu Trp Ser Ala Phe Ser Cys
210 215 220
Phe Gln Lys Ala Gln Leu Lys Ser Ala Asn Thr Gly Asn Asn Glu Arg
225 230 235 240
Ile Ile Asn Val Ser Ile Lys Lys Leu Lys Arg Lys Pro Pro Ser Thr
245 250 255
Asn Ala Gly Arg Arg Gln Lys His Arg Leu Thr Cys Pro Ser Cys Asp
260 265 270
Ser Tyr Glu Lys Lys Pro Pro Lys Glu Phe Leu Glu Arg Phe Lys Ser
275 280 285
Leu Leu Gln Lys Met Ile His Gln His Leu Ser Ser Arg Thr His Gly
290 295 300
Ser Glu Asp Ser
305
Claims (38)
- 코헤신(cohesin)-도커린(dockerin) 결합 쌍의 절반을 포함하는 하나 이상의 항원 운반체 도메인에 연결된 항원-특이적인 결합 도메인을 포함하는 모듈러(modular) rAb 운반체.
- 제1항에 있어서, 항원-특이적인 결합 도메인이 항체의 적어도 일부를 포함하는 rAb.
- 제1항에 있어서, 항원-특이적인 결합 도메인이 코헤신-도커린 결합 쌍의 절반과의 융합 단백질내 항체의 적어도 일부를 포함하는 rAb.
- 제1항에 있어서, 모듈러 rAb 운반체와 복합체를 형성하는 항원에 결합된 코헤신-도커린 결합 쌍의 상보적 절반을 추가로 포함하는 rAb.
- 제1항에 있어서, 항원과의 융합 단백질인 코헤신-도커린 결합 쌍의 상보적 절반을 추가로 포함하는 rAb.
- 제1항에 있어서, 항원 특이적인 도메인이 완전한 길이의 항체, 항체 가변 영역 도메인, Fab 단편, Fab' 단편, F(ab)2 단편, 및 Fv 단편, 및 Fabc 단편 및/또는 Fc 도메인의 일부를 갖는 Fab 단편을 포함하는 rAb.
- 제1항에 있어서, 코헤신-도커린이 클로스트리디움 써모셀룸(Clostridium thermocellum), 클로스트리디움 조수이(Clostridium josui), 클로스트리디움 셀룰로라이티쿰(Clostridium cellulolyticum) 및 박테로이데스 셀룰로솔벤스(Bacteroides cellulosolvens) 및 이들의 조합 중에서 선택되는 rAb.
- 제1항에 있어서, 항원-특이적인 결합 도메인이 MHC 클래스 I, MHC 클래스 II, CD1, CD2, CD3, CD4, CD8, CD11b, CD14, CD15, CD16, CD19, CD20, CD29, CD31, CD40, CD43, CD44, CD45, CD54, CD56, CD57, CD58, CD83, CD86, CMRF-44, CMRF-56, DCIR, DC-ASPGR, CLEC-6, CD40, BDCA-2, MARCO, DEC-205, 만노즈 수용체, 랑게린(Langerin), DECTIN-1, B7-1, B7-2, IFN-γ 수용체 및 IL-2 수용체, ICAM-1, Fcγ 수용체 또는 항원 제시 세포에 의해 비교적 특이적으로 발현된 다른 수용체 중에서 선택된 세포 표면 마커에 결합하는 rAb.
- 제1항에 있어서, rAb가 rAb.Doc; rAb.Coh; rAb.(Coh)x; rAb.(Doc)x; rAb.(Coh.Doc)x; 또는 rAb.(Coh)x(Doc)x(여기서, x는 1, 2, 3, 4, 5, 6, 7, 8, 9 또는 10이다)로 추가로 정의되는 rAb.
- 제1항에 있어서, rAb가 복합체:rAb.Doc:Coh.항원;rAb.Coh:Doc.항원;rAb.(Coh)x:(Doc.항원)x;rAb.(Doc)x:(Coh.항원)x;rAb.(Coh.Doc)x:(Doc.항원1)(Coh.항원2); 또는rAb.(Coh)x(Doc)x:(Doc.항원1)x(Coh.항원2)x(여기서, x는 1, 2, 3, 4, 5, 6, 7, 8, 9 또는 10이다)의 일부로서 추가로 정의되는 rAb.
- 항원에 결합된 코헤신-도커린 결합 쌍의 상보적 절반에 결합된 코헤신-도커린 결합 쌍의 절반을 포함하는 하나 이상의 도메인에 연결된 항원 특이적인 도메인을 포함하는 모듈러 rAb 운반체를 포함하는 백신.
- 제11항에 있어서, 항원 특이적인 도메인이 MHC 클래스 I, MHC 클래스 II, CD1, CD2, CD3, CD4, CD8, CD11b, CD14, CD15, CD16, CD19, CD20, CD29, CD31, CD40, CD43, CD44, CD45, CD54, CD56, CD57, CD58, CD83, CD86, CMRF-44, CMRF-56, DCIR, DC-ASPGR, CLEC-6, CD40, BDCA-2, MARCO, DEC-205, 만노즈 수용체, 랑게린, DECTIN-1, B7-1, B7-2, IFN-γ 수용체 및 IL-2 수용체, ICAM-1, Fcγ 수용체 또는 항원 제시 세포에 의해 비교적 특이적으로 발현된 다른 수용체 중에서 선택된 면역 세포 표면 단백질에 대해 특이적인 백신.
- 제11항에 있어서, 항원이 세균, 바이러스, 진균, 원생동물 또는 암 단백질을 포함하는 백신.
- 제11항에 있어서, 모듈러 rAb 운반체가rAb.Doc:Coh.항원;rAb.Coh:Doc.항원;rAb.(Coh)x:(Doc.항원)x;rAb.(Doc)x:(Coh.항원)x;rAb.(Coh.Doc)x:(Doc.항원1)(Coh.항원2); 또는rAb.(Coh)x(Doc)x:(Doc.항원1)x(Coh.항원2)x(여기서, x는 1, 2, 3, 4, 5, 6, 7, 8, 9 또는 10이다)로 추가로 정의되는 백신.
- 표적-특이적인 도메인 및 하나 이상의 도메인 및 코헤신-도커린 결합 쌍의 절반에 대한 암호화 단편을 포함하는 분리된 핵산.
- 제15항에 있어서, 표적이 항원이고, 특이적인 도메인이 항체의 적어도 일부를 암호화하는 핵산.
- 제15항에 있어서, 하나 이상의 도메인이 하나 이상의 코헤신 도메인, 하나 이상의 도커린 도메인 또는 하나 이상의 코헤신 및 도커린 도메인의 조합을 암호화하는 핵산.
- 제15항에 있어서, 표적 특이적인 도메인이 rAb.Doc; rAb.Coh; rAb.(Coh)x; rAb.(Doc)x; rAb.(Coh.Doc)x; 또는 rAb.(Coh)x(Doc)x(여기서, x는 1, 2, 3, 4, 5, 6, 7, 8, 9 또는 10이다)로 추가로 정의된 rAb를 포함하는 핵산.
- 항원 특이적인 도메인 및 코헤신-도커린 결합 쌍의 절반, 운반될 단백질 분자와의 코헤신-도커린 결합 쌍의 절반 및 이들의 조합을 포함하는 하나 이상의 도메인을 암호화하는 핵산을 포함하는 벡터.
- 제19항에 있어서, 코헤신-도커린 결합 쌍의 절반, 운반될 단백질 분자와의 코헤신-도커린 결합 쌍의 절반 및 이들의 조합이 동일한 프로모터, 상이한 프로모 터의 조절하에서, 동일한 방향으로 전사되거나 반대 방향으로 전사되는 벡터.
- 항원 특이적인 도메인 및 하나 이상의 도메인 및 코헤신-도커린 결합 쌍의 절반을 암호화하는 핵산을 포함하는 벡터를 포함하는 숙주 세포.
- 코헤신-도커린 결합 쌍의 절반을 포함하는 하나 이상의 도메인에 연결된 항원 특이적인 도메인을 조합시킴을 포함하여, 모듈러 rAb 운반체를 제조하는 방법.
- 제22항에 있어서, rAb가 rAb.Doc; rAb.Coh; rAb.(Coh)x; rAb.(Doc)x; rAb.(Coh.Doc)x; 또는 rAb.(Coh)x(Doc)x(여기서, x는 1, 2, 3, 4, 5, 6, 7, 8, 9 또는 10이다)로 추가로 정의되는 방법.
- 제22항에 있어서, rAb가, 항원에 결합된 코헤신:도커린 쌍의 상보적 절반과 복합체화되며,rAb.Doc:Coh.항원;rAb.Coh:Doc.항원;rAb.(Coh)x:(Doc.항원)x;rAb.(Doc)x:(Coh.항원)x;rAb.(Coh.Doc)x:(Doc.항원1)(Coh.항원2); 또는rAb.(Coh)x(Doc)x:(Doc.항원1)x(Coh.항원2)x(여기서, x는 1, 2, 3, 4, 5, 6, 7, 8, 9 또는 10이다) 중에서 선택되는 방법.
- rAb.Doc:Coh.독소 자가-어셈블리된 접합체(여기서, rAb는 세포 표적에 대해 특이적이다)를 포함하는 면역독소.
- 제25항에 있어서, 독소가 방사능 동위원소, 금속, 효소, 보툴린, 테타누스, 리신(ricin), 콜레라, 디프테리아, 아플라독소, 퍼프린젠스 독소, 마이코독소, 시가독소, 스타필로코쿠스 장독소 B, T2, 세구이독소, 삭시독소, 아브린, 시아노기노신, 알파독소, 테트로도독소, 아코노독소, 뱀독 및 거미 독으로 이루어진 그룹 중에서 선택되는 면역독소.
- 제25항에 있어서, 세포 표적이 혈액암, 백혈병, 림프종, 신경 종양, 별아교세포종 또는 아교모세포종, 흑색종, 유방암, 폐암, 두경부암, 위암 또는 결장암과 같은 위장관 종양, 간암, 췌장암, 자궁경부암, 자궁암, 난소암, 질암, 고환암, 전립선암 또는 음경암과 같은 비뇨생식기 종양, 골 종양, 혈관 종양 또는 입술, 비인두, 인두 및 구강, 식도, 직장, 담낭, 담관, 후두, 폐 및 기관지, 방광, 신장, 뇌 및 신경계의 다른 부분, 갑상선의 암, 호지킨병(Hodgkin's disease), 비-호지킨 림 프종(non-Hodgkin's lymphoma), 다발성 골수종 및 백혈병 중에서 선택된 암 세포를 포함하는 면역독소.
- 제25항에 있어서, 세포 표적이 세균, 원생동물, 연충, 바이러스-감염된 세포 또는 진균 중에서 선택된 병원체를 포함하는 면역독소.
- 코헤신 또는 도커린 융합 단백질을 기질에 결합된 상보성 코헤신 또는 도커린에 접합되는 rAb와 상호작용시킴으로써 상기 융합 단백질을 분리함을 포함하는, 단백질 정제 방법.
- 제29항에 있어서, 이식, 자가면역병, 감염성 질병 또는 암을 포함하는 치료학적 적용시 단백질을 투여하는 단계를 추가로 포함하는 방법.
- 활성 코헤신.독소 융합 단백질이 용이하게 정제되도록 하는 유리한 생화학적 특성을 부여하기 위한, 독소에 대한 융합 파트너로서의 코헤신의 용도.
- DC를 제거하는 치료학적 적용을 위해 DC를 표적화하기 위한 항-DC rAb.Doc의 용도.
- 수지상 세포의 생존을 향상시키기에 충분한 양으로 제공되는 항-DC-SIGN/L 항체로서, 성숙하여 면역화를 위해 수지상 세포를 활성화시키는 항-DC-SIGN/L 항체.
- 제33항에 있어서, 생체내에서 백신중 애주번트로서 수지상 세포로 표적화되는 항체.
- 치료제, 진단제 및 산업적 제제로서의 이가 및 다가 (rAb1.Doc:Coh.rAb2) 자가-어셈블리된 접합체.
- 치료제, 세포 증식제 또는 성숙제로서의 이가 및 다가 (rAb.Doc:Coh.사이토카인), (rAb.Coh:Doc.사이토카인) 또는 (사이토카인1.Coh:사이토카인2.Doc) 자가-어셈블리된 접합체.
- 표적 세포에 특이적으로 결합하여 사이토카인을 전달함으로써 표적 세포에 대해 효과를 발휘할 수 있는 하나 이상의 다가 rAb 및/또는 rAb.사이토카인 및/또는 사이토카인.사이토카인 조합을 스크리닝함을 포함하는, 모듈러 rAb의 제조 방법.
- 제37항에 있어서, 사이토카인이 인터루킨, 전환 성장 인자(TGF), 섬유아세포 성장 인자(FGF), 혈소판 기원한 성장 인자(PDGF), 상피 성장 인자(EGF), 연결 조직 활성화된 펩타이드(CTAP), 골원성 인자, 및 이러한 성장 인자의 생물학적으로 활성인 유사체, 단편 및 유도체, B/T-세포 분화 인자, B/T-세포 성장 인자, 유사분열촉진성 사이토카인, 화학주성 사이토카인, 콜로니 자극 인자, 혈관형성 인자, IFN-α IFN-β, IFN-γ, IL1, IL2, IL3, IL4, IL5, IL6, IL7, IL8, IL9, IL10, IL11, IL12, IL13, IL14, IL15, IL16, IL17, IL18 등, 렙틴, 마이오스타틴, 대식구 자극 단백질, 혈소판-기원한 성장 인자, TNF-α, TNF-β, NGF, CD40L, CD137L/4-1BBL, 사람 림프독소-β, G-CSF, M-CSF, GM-CSF, PDGF, IL-1α, IL1-β, IP-10, PF4, GRO, 9E3, 에리트로포이에틴, 엔도스타틴, 안지오스타틴, VEGF, 베타 전환 성장 인자(예를 들면, TGF-β1, TGF-β2, TGF-β3)를 포함하는 전환 성장 인자(TGF) 슈퍼유전자 계열; 골 형태형성 단백질(예를 들면, BMP-1, BMP-2, BMP-3, BMP-4, BMP-5, BMP-6, BMP-7, BMP-8, BMP-9); 헤파린-결합 성장 인자(섬유아세포 성장 인자(FGF), 상피 성장 인자(EGF), 혈소판-기원 성장 인자(PDGF), 인슐린-유사 성장 인자(IGF)); 인히빈(예를 들면, 인히빈 A, 인히빈 B); 성장 분화 인자(예를 들면, GDF-1); 및 액티빈(예를 들면, 액티빈 A, 액티빈 B, 액티빈 AB)를 포함하는 방법.
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| MX2022014943A (es) | 2020-05-26 | 2023-03-08 | Inst Nat Sante Rech Med | Polipéptidos de coronavirus 2 causante del síndrome respiratorio agudo severo (sars-cov-2) y usos de los mismos para propositos de vacuna. |
| WO2022101302A1 (en) | 2020-11-12 | 2022-05-19 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Antibodies conjugated or fused to the receptor-binding domain of the sars-cov-2 spike protein and uses thereof for vaccine purposes |
| EP4267176A1 (en) | 2020-12-23 | 2023-11-01 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Chlamydia vaccine based on targeting momp vs4 antigen to antigen presenting cells |
| US20240124532A1 (en) | 2021-01-29 | 2024-04-18 | Institut National De La Santé Et De La Recherche Médicale (Inserm) | Chlamydia trachomatis antigenic polypeptides and uses thereof for vaccine purposes |
| WO2023088968A1 (en) | 2021-11-17 | 2023-05-25 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Universal sarbecovirus vaccines |
| WO2024074571A1 (en) | 2022-10-05 | 2024-04-11 | Institut National de la Santé et de la Recherche Médicale | Dc-targeting vaccine against nipah virus infection |
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| US20040258688A1 (en) * | 1995-01-31 | 2004-12-23 | Daniel Hawiger | Enhanced antigen delivery and modulation of the immune response therefrom |
| WO1997014789A2 (en) * | 1995-10-17 | 1997-04-24 | Genencor International, Inc. | Enzymatic array and process of making same |
| FR2748479A1 (fr) * | 1996-05-10 | 1997-11-14 | Pasteur Institut | Polypeptide comportant un nouveau domaine cohesine de type ii, composition enzymatique en comportant et fragments d'adn codant pour ces polypeptides |
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| JP2000157282A (ja) * | 1998-11-30 | 2000-06-13 | Toyota Central Res & Dev Lab Inc | 酵素配列複合体及び固定化酵素配列複合体とそれらの製造方法、担体分子及び酵素 |
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| EP1046651A1 (en) * | 1999-04-19 | 2000-10-25 | Koninklijke Universiteit Nijmegen | Composition and method for modulating dendritic cell-T interaction |
| US7560534B2 (en) * | 2000-05-08 | 2009-07-14 | Celldex Research Corporation | Molecular conjugates comprising human monoclonal antibodies to dendritic cells |
| WO2001085204A2 (en) * | 2000-05-11 | 2001-11-15 | Altarex Corp. | Therapeutic method and composition utilizing antigen-antibody complexation and presentation by dendritic cells |
| WO2003018749A2 (en) * | 2001-08-22 | 2003-03-06 | Shengfeng Li | Compositions and methods for generating antigen-binding units |
| WO2003033695A1 (fr) * | 2001-10-11 | 2003-04-24 | Katakura Industries Co., Ltd. | Procede de purification de proteine fusionnee recombinee et procede de production de proteine utilisant ledit procede de purification |
| JP2004236504A (ja) * | 2003-02-03 | 2004-08-26 | Toyota Central Res & Dev Lab Inc | 酵素配列複合体及び固定化酵素配列複合体とそれらの製造方法、担体分子及び酵素 |
| US20050064509A1 (en) * | 2003-09-23 | 2005-03-24 | The Regents Of The University Of California | Use of templated self assembly to create novel multifunctional species |
| US20080025913A1 (en) * | 2003-12-15 | 2008-01-31 | Bowdish Katherine S | Novel Anti-Dc-Sign Antibodies |
| WO2006107617A2 (en) * | 2005-04-06 | 2006-10-12 | Ibc Pharmaceuticals, Inc. | Methods for generating stably linked complexes composed of homodimers, homotetramers or dimers of dimers and uses |
| AU2008214077B2 (en) * | 2007-02-02 | 2012-12-13 | Baylor Research Institute | Multivariable antigens complexed with targeting humanized monoclonal antibody |
| NZ578696A (en) * | 2007-02-02 | 2012-01-12 | Baylor Res Inst | Vaccines based on targeting antigen to dcir expressed an antigen-presenting cells |
| TWI422594B (zh) * | 2007-02-02 | 2014-01-11 | Baylor Res Inst | 經由樹狀細胞去唾液酸糖蛋白受體（ｄｃ-ａｓｇｐｒ）接合抗原呈現細胞之藥劑 |
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- 2008-01-31 EP EP13178012.4A patent/EP2684889A3/en not_active Withdrawn
- 2008-01-31 NZ NZ578657A patent/NZ578657A/en not_active IP Right Cessation
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| Publication number | Publication date |
|---|---|
| EP2114985A4 (en) | 2010-09-22 |
| EP2684889A2 (en) | 2014-01-15 |
| MX2009008143A (es) | 2009-10-20 |
| BRPI0807344A2 (pt) | 2014-05-20 |
| WO2008097817A2 (en) | 2008-08-14 |
| NZ592859A (en) | 2012-05-25 |
| ES2536900T3 (es) | 2015-05-29 |
| EP2114985B1 (en) | 2014-12-17 |
| US20160031988A1 (en) | 2016-02-04 |
| IL200092A0 (en) | 2010-04-15 |
| CA2715042A1 (en) | 2008-08-14 |
| EP2114985A2 (en) | 2009-11-11 |
| WO2008097817A3 (en) | 2008-10-30 |
| US20080254044A1 (en) | 2008-10-16 |
| TW200846371A (en) | 2008-12-01 |
| DK2114985T3 (en) | 2015-03-30 |
| ZA200905447B (en) | 2010-05-26 |
| JP2010518020A (ja) | 2010-05-27 |
| US20100330115A1 (en) | 2010-12-30 |
| JP5543785B2 (ja) | 2014-07-09 |
| EP2684889A3 (en) | 2014-03-05 |
| US7786267B2 (en) | 2010-08-31 |
| NZ578657A (en) | 2012-02-24 |
| CN101657464A (zh) | 2010-02-24 |
| AU2008214077A1 (en) | 2008-08-14 |
| CA2715042C (en) | 2021-02-02 |
| AU2008214077B2 (en) | 2012-12-13 |
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