KR20170121301A - 변형된 알파 바이러스 표면 당 단백질 및 종양-관련 항원을 포함하는 융합 단백질 및 이의 방법 - Google Patents
변형된 알파 바이러스 표면 당 단백질 및 종양-관련 항원을 포함하는 융합 단백질 및 이의 방법 Download PDFInfo
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Abstract
본 발명은 하나 이상의 변형된 알파 바이러스 표면 당 단백질 및 하나 이상의 종양 특이적 항원을 포함하는 융합 단백질에 관한 것이다. 또한, 본 발명은 하나 이상의 변형된 알파 바이러스 표면 당 단백질 및 하나 이상의 바이러스 특이적 항원을 포함하는 융합 단백질에 관한 것이다. 또한, 본 발명은 하나 이상의 변형된 알파 바이러스 표면 당 단백질을 포함하는 융합 단백질에 관한 것이다. 또한 본 발명은 종양 세포 또는 잠복 바이러스에 감염된 세포에 침투하고 사멸시키기 위해 암 환자에서 면역계를 활성화시키는 방법에 관한 것이다. 본 발명은 융합 단백질을 사용하여 보다 빠르고 광범위하고 강력한 면역 반응을 유도하는 플랫폼 기술을 제공한다.
Description
본 출원은 2015년 3월 18일에 출원된 미국 특허출원 제62/134,933호를 우선권으로 주장하고, 상기 명세서 전체는 본 출원의 참고문헌이다.
본 발명은 하나 이상의 변형된 알파 바이러스 표면 당 단백질 및 하나 이상의 종양 특이적 항원을 포함하는 융합 단백질에 관한 것이다. 또한, 본 발명은 하나 이상의 변형된 알파 바이러스 표면 당 단백질 및 하나 이상의 바이러스 특이적 항원을 포함하는 융합 단백질에 관한 것이다. 또한, 본 발명은 하나 이상의 변형된 알파 바이러스 표면 당 단백질을 포함하는 융합 단백질이 기재하였다. 또한, 본 발명은 종양 세포 또는 잠복 바이러스에 감염된 세포에 침투하고 사멸시키기 위해 암 환자에서 면역계를 활성화시키는 방법에 관한 것이다. 본 발명은 융합 단백질을 사용하여 보다 빠르고 광범위하고 강력한 면역 반응을 유도하는 플랫폼 기술을 제공한다.
난소암은 미국에서 부인과의 악성종양으로 인한 사망의 주요 원인이다(1). 불행하게도 대부분의 경우는 질병이 III 또는 IV 기까지 진행될 때까지 진단되지 않으며, 이 때에는 수술 및 화학 요법에 처음 성공적으로 반응 한 후에도 재발이 흔하다(2). 그러나 종양에 림프구가 침투한 환자는 그렇지 않은 환자보다 5년 생존율이 유의하게 높았는데(3), 이는 면역 체계가 종양 성장을 막는데 중요한 역할을 하고 면역 요법은 이 질병과 싸우기 위한 성공적인 전략이 될 수 있음을 시사한다, 또한, 많은 암이 바이러스 감염에 의해 유발된다는 것도 알려져 있다.
면역 체계는 “암 면역편집(cancer immunoediting)”으로 알려진 메커니즘을 통해 비-정상적인 종양 세포의 성장을 억제하고 조절하는데 중요한 역할을 한다(4). 세포독성 CD8 T세포 및 NK 세포(natural killer cell)는 이러한 세포들이 발생했을 때 이들 세포를 인식하고 파괴할 수 있다. 이러한 세포 유형이 결핍된 면역 결핍 마우스는 종양 형성에 대한 감수성이 증가한다는 것이 알려져있다(4). 그러나 종양 세포는 면역 시스템에 의한 검출을 피하는 돌연변이를 일으킬 수 있으며, 따라서 성숙한 종양은 종종 면역원성이 불충분하기 때문에 인간 환자에게 이러한 많은 치료법이 성공적으로 사용되지 못하고 있다(4). 또한, 종양은 림프구와의 직접 접촉을 막는 독특한 미세 환경을 형성할 수 있다.
그러나, 종양의 면역 억제 성질을 피해갈 수 있는 몇몇 발전이 이루어졌다. 최근에는 면역 요법 항체인 이필리무맙(Ipilimumab)과 니보루맙(Nivolumab)이 특정 암의 치료용으로 승인 받았다. 이들 체크포인트 억제제(checkpoint inhibitor)는 T세포에서 면역 억제 수용체인 CTLA-4(Ipilimumab) 및 PD-1(Nivolumab)의 활성을 표적으로 하여 억제한다. 이러한 면역 억제성 메카니즘은 잠재적으로 위험한 자가 면역 및 알레르기 반응을 조절하는 데 중요하기 때문에, 상기한 약물의 안전에 문제가 없는 것은 아니다. 키메라 항원 수용체(chimeric antigen receptor, CAR) T세포 치료법은 B 세포 급성 림프구성 백혈병(acute lymphoblastic leukemia, ALL)과 같은 혈액-기반 암 치료에 강력한 잠재력을 보여주었다. CAR T세포를 생성하기 위해, 환자 자신의 T세포를 수득한 후에 종양 세포상의 특정 표면 항원을 인식하는 수용체를 발현하기 위해 유전적으로 변형시켰다(5). 이 방법은 일반적으로 T세포와 항원-제시 종양 세포 사이에서 발생하는 신호 전달 경로를 피하여 면역 억제에 대해 내성을 만든다. 환자 자신의 세포의 유전 공학이 필요하고, 사이토카인-방출 증후군(cytokine-release syndrome)이 발생할 수 있는 잠재적인 위험한 부작용 때문에(6), CAR T세포 치료법은 전통적인 약물 치료법에서는 더 이상 필요하지 않은 밀접한 개별 모니터링을 필요로 한다. 난소암과 같은 고형 종양에 대항하는 CAR T세포의 능력은 여전히 평가중이다.
암에 대항하는 또 다른 잠재성을 가진 방법은 종양 용해 바이러스(oncolytic viruses) 또는 바이러스 벡터의 사용이다. 이러한 바이러스들은 암 세포를 특이적으로 감염시키고 사멸시키는 것으로 활성을 나타내는 것으로 생각된다. 암 세포가 용해되면, 수지상 세포(dendritic cell)는 분비된 종양 항원을 포착할 수 있고, 더 나은 항-종양 면역 반응을 생성할 수 있다. 그러나, 상기한 바이러스 및 바이러스 벡터는 림프절 또는 다른 기관 및 대상으로 하는 표적 종양 외의 위치에 축적되는 것으로 밝혀졌다. 따라서, 상기에 기재된 위험 및 문제점을 갖지 않는 안전하고 효과적인 암 치료 및 예방 방법을 제공할 필요가 있다.
본원에 기재된 것은 하나 이상의 종양-관련 항원 및 하나 이상의 변형된 알파 바이러스 표면 당단백질을 포함하는 융합 단백질이다. 또한, 본원에는 다중결합 복합체(multimeric complexes), 변형된 융합 단백질을 코딩하는 핵산, 융합 단백질의 아미노산 서열, 융합 단백질에 대한 항체 및 그의 용도가 기재되어 있다. 특정 실시양태에서, 알파 바이러스는 신드비스 알파 바이러스(Sidbis alpha virus) 또는 치쿤군야 바이러스(chikungunya virus)이다. 특정 실시양태에서, 상기 변형된 알파 바이러스 표면 당단백질은 E1, E2 또는 6K이다. 특정 실시양태에서, 상기 변형된 알파 바이러스 표면 당단백질은 E1 및 E2이다. 특정 실시양태에서, 본원은 변형된 알파 바이러스 폴리프로테인(polyprotein)을 제공한다. 특정 실시양태에서, 상기 폴리프로테인은 E3 또는 캡시드 단백질이다. 본원에서 하나 이상의 변형된 알파 바이러스 표면 당단백질 및 NCI Pilot Project to Prioritize Cancer Antigens과 관련하여 Clin Cancer Res 2009;15:5323-5337의 표 3에 기재된 기타의 단백질을 포함하는 융합 단백질을 제공한다. 또한 본원에 기재된 것은 변형된 알파 바이러스 표면 당단백질 및 하나 이상의 유전자 또는 유전자 단편을 포함하는 재조합 융합 단백질이다. 특정 실시양태에서, 상기 융합 단백질은 알파 바이러스 표면 당단백질의 유전자 단편의 내부 또는 말단에 삽입된 종양-관련 항원의 유전자 또는 유전자 단편을 포함하는 구조물에 의해 코딩된다. 특정 실시양태에서, 상기 유전자 또는 유전자 단편은 하나 이상의 종양-관련 항원이다. 특정 실시양태에서, 상기 융합 단백질은 단량체(monomer), 복합체(complex), 접합체(comjugate)이다. 특정 실시양태에서, 상기 융합 단백질은 이량체, 삼량체 또는 다량체를 형성 할 수 있다.
또한 본원에 기재된 것은 하나 이상의 바이러스 항원 및 하나 이상의 변형된 알파 바이러스 표면 당단백질을 포함하는 융합 단백질이다.
또한 본원에 기재된 것은 하나 이상의 종양-관련 항원 및 하나 이상의 변형된 알파 바이러스 표면 당단백질을 포함하는 융합 단백질의 투여에 의한 질병의 치료 또는 예방 방법이다. 특정 실시양태에서, 상기 본원에 기재된 방법은 억제된 면역 시스템을 활성화시키기 위한 개체의 치료에 관한 것이다. 특정 실시양태에서, 상기 치료는 암 환자에 대한 것이다. 특정 실시양태에서, 상기 치료는 종양 세포를 침윤 및 사멸시키는 단계를 포함한다. 특정 실시양태에서, 상기 치료는 잠복해 있는 바이러스 감염 세포를 사멸시키는 것을 포함한다.
하나의 실시양태에서는, 알파 바이러스 표면 당단백질 E1, E2 및 적어도 하나의 링커로 필수적으로 구성되는 융합 단백질을 이를 필요로 하는 개체에게 투여하는 것을 포함하는, 개체에서 암을 치료하는 방법이 기재되어 있는데, 상기 융합 단백질은 개체에 투여 될 때 면역 반응을 자극한다.
본 발명에 기재된 것은 질환의 예방 및 치료를 위한 상기 융합 단백질을 포함하는 키트이다.
상기 기재된 방법은 하나 이상의 종양-관련 항원 및 하나 이상의 변형된 알파 바이러스 표면 당단백질을 포함하는 융합 단백질의 투여를 포함한다. 특정 실시양태에서, 상기 변형된 알파 바이러스 표면 당 단백질은 단량체, 복합체, 융합체(fusion), 접합체이다. 특정 실시양태에서, 상기 융합 단백질은 이량체, 삼량체 또는 다량체를 형성 할 수 있다. 상기 하나 이상의 종양 관련 항원 및 하나 이상의 변형 된 알파 바이러스 표면 당 단백질을 포함하는 융합 단백질은 다음 중 하나 이상에 유용하다 : (i) 인간의 면역계를 여기(excite)/활성화; (ii) 인간 T세포의 성장을 자극/활성화; (iii) T세포, NK세포, B세포, 수지상 세포, 조절 T세포, 대식세포, 적혈구 등을 포함한 인간 조혈 세포를 여기/활성화; (iv) 아네르기(anergy)로부터 T세포를 분비; (v) T세포의 중단점(breakpoint) 억제 극복; (vi) 암 치료 또는 예방; 및 (vii) 잠복해 있는 바이러스 감염 세포. 특정 실시양태에서, 상기 방법은 하기 목적을 위해 종양-관련 항원 및 변형된 알파 바이러스 표면 당 단백질을 포함하는 융합 단백질을 이를 필요로 하는 대상에게 투여하는 단계를 포함한다 : (i) 인간의 면역계를 여기(excite)/활성화; (ii) 인간 T세포의 성장을 자극/활성화; (iii) T세포, NK세포, B세포, 수지상 세포, 조절 T세포, 대식세포, 적혈구 등을 포함한 인간 조혈 세포를 여기/활성화; (iv) 아네르기로부터 T세포를 분비; (v) T세포의 중단점 억제 극복; (vi) 암 치료 또는 예방; 및 (vii) 잠복해 있는 바이러스 감염 세포. 특정 실시양태에서, 상기 본원에 기재된 방법은 암 환자에서 억제된 면역 시스템을 활성화시켜 종양 세포를 침윤 및 사멸시키기 위한 개체의 치료에 관한 것이다. 다른 실시양태에서, 상기 융합 단백질은 잠복해 있는 바이러스 세포를 사멸하는데 유용한 하나 이상의 바이러스성 항원 및 하나 이상의 변형된 알파 바이러스 표면 당단백질을 포함한다.
정의
본 발명에서 사용된 바와 같이, 용어 "알파 바이러스(alpha virus)"는 당업계에서의 통상적인 의미를 가지며, VEE, SFV, 신드비스(Sindbis), 로스리버 바이러스(Ross River virus), 웨스턴 에퀸 바이러스(western equine encephalitis virus), 이스턴 에퀸 바이러스(Eastern Equine Encephalitis virus), 치쿤군야(Chikungunya), S.A. AR86, 에버글레이드 바이러스(Everglades virus), Mucambo, 바마 포리스트 바이러스(Barmah Forest virus), 미델부륵 바이러스(Middelburg virus), 픽수나 바이러스(Pixuna virus), O'nyong-nyong 바이러스, 게타 바이러스(Getah virus), 사기야마 바이러스(Sagiyama virus), 베바루 바이러스(Bebaru virus), 마야로 바이러스(Mayaro virus), 우나 바이러스(Una virus), 오라 바이러스(Aura virus), 와타로아 바이러스(Whataroa virus), 반반키 바이러스(Banbanki virus), 키지라가치 바이러스(Kyzylagach virus), 하이랜드 J 바이러스(Highlands J Virus), 포트 모간 바이러스(Fort Morgan virus), 엔두무 바이러스(Ndumu virus) 및 버기 크릭 바이러스(Buggy Creek virus)와 같은 바이러스 종을 포함한다. 특정 실시양태에서, 본 발명의 작제물 및 방법에 사용된 상기 알파바이러스는 VEE, S.AAR86, 신드비스(예; TR339, 미국 특허 제6,008,035호 참조) 및 SFV이다.
용어 “보조제(adjuvant)”는 투여된 면역원성 결정인자/항원/핵산 구조물과의 혼합물이 상기 결정 인자에 대한 면역 반응을 증가시키거나 그렇지 않으면 변경시키는 임의의 물질을 의미한다.
용어 “아미노산(amino acid)”은 생체 내에서 합성된 단백질 및 효소를 포함하는 펩티드 및 폴리펩티드에서 발생하는 아미노산을 포함하고, 아미노산의 변형을 포함하는, 합성 또는 자연적으로 존재하는 아미노 카르복실 산(amino carboxylic acid)를 의미한다. 상기 용어 “아미노산”은 본 발명에서 “아미노산 잔기”와 동의어로 사용되며, 이는 예를 들어 2 개, 예를 들어 3 개, 3개 이상의 다른 종과 같이 적어도 하나의 다른 종과 반응한 것으로 정해진 아미노산을 포함하는 것을 나타낸다. 상기 일반적인 용어 “아미노산”은 "D" 또는 "L" 이성질체 형태일 수 있는 천연 및 비-천연 아미노산 모두를 포함한다.
용어 “항체”는 면역글로불린 분자 및 면역글로불린 분자의 활성 부분을 나타낸다. 항체는 예를 들어 온전한(intact) 면역글로불린 분자 또는 면역학적 활성을 보유하는 이의 단편이다.
용어 “항원(antigen)”은 클론적으로 분포된 면역 수용체(T-세포 또는 B-세포 수용체)에 결합할 수 있는 임의의 물질을 의미한다. 보통 펩티드, 폴리펩티드 또는 다량체 폴리펩티드를 나타낸다. 바람직하게는 항원은 면역 반응을 유도할 수 있다.
부스트 샷 또는 용량을 증가시키는 것으로서 본 발명에서 사용된 용어 “부스트(boost)”는 같은 제제의 이전 투여량에 의해 유도된 면역 반응을 유지하기 위해 초기 투여 후 일정 시간 후에 주어진 백신과 같은 면역 제제의 추가 투여량을 제공하는 것이다.
용어 “캐리어(carrier)”는 면역 반응의 유도를 돕기 위해 항원에 결합되는 독립체(entity) 또는 화합물을 의미한다.
용어 “융합 단백질(fusion protein)”은 둘 이상의 완전 또는 부분 유전자 또는 일련의 핵산을 함께 결합시킴으로서 만들어진 뉴클레오티드 서열에 의해 코딩된 유전적으로 조작된 단백질을 의미한다. 대안적으로, 융합 단백질은 2개 이상의 이종 펩티드(heterologous peptide)를 함께 결합시킴으로서 제조될 수 있다.
용어 “사이토카인(cytokine)”은 성장 또는 분화 조절제를 의미하며, 이에 한정되는 것은 아니다. 사이토카인에 더하여, 부착(adhession) 또는 부속(accessary) 분자, 또는 이들의 임의의 조합이 단독 또는 사이토카인과 함께 사용될 수 있다.
용어 “세포독성 T 림프구(Cytotoxic T lymphocytes)”는 T-세포 수용체와 함께 CD8을 발현하는 T-세포의 하위 그룹을 나타내며, 따라서 클래스 I 분자에 의해 제시된 항원에 반응할 수 있음을 의미한다.
용어 “전달 비히클(delivery vehicle)”은 뉴클레오티드 서열 또는 폴리펩티드 또는 둘 모두가 적어도 하나의 배지(media)에서 다른 배지로 운반될 수 있게 하는 독립체(entity)를 의미한다.
용어 “단편(fragment)”은 핵산 또는 폴리펩티드의 전체 길이가 아닌 일부분을 의미한다.
용어 “개체(subject)”는 조류, 포유류, 인간, 비인간, 어류, 양서류 또는 파충류의 임의의 종 또는 아종을 의미한다.
핵산, 폴리펩티드 및 항체와 관련하여 사용되는 용어 “분리된(isolated)”은 이들의 천연, 전형적으로 세포성 환경의 성분으로부터 확인되고 분리 및/또는 회수된 것을 의미한다.
용어 “핵산(nucleic acid)”, “폴리펩티드(polypeptide)” 및 “항체(antibodies)”는 바람직하게는 분리된(isolated) 것이고, 본 발명의 백신 및 다른 조성물은 바람직하게 분리된 핵산, 폴리펩티드 또는 분리된 항체를 포함한다.
용어 “MHC(즉, 주요 조직 적합성 복합체(Major histocompatibility complex))는 MHC, 클래스 I 및 클래스 II의 두 가지 주요 하위 클래스를 의미한다.
용어 “핵산(nucleic acie)”은 유전 정보를 전달하는 뉴클레오티드의 사슬 또는 서열을 나타낸다. “핵산 작제물(nucleic acid construct)”는 유전적으로 조작된 핵산을 의미하며, 전형적으로 유전자 또는 그의 단편, 프로모터, 인핸서(enhancer), 종결자(terminators), 폴리 A 테일, 링커, 폴리링커, 작동 링커, 다중 클로닝 사이트(multiple cloning sites, MCS), 마커, STOP 코돈, 다른 조절 요소, 내부 리보솜 진입 사이트(internal ribosomal entry sites, IRES) 또는 다른 것들과 같은 몇몇 요소를 포함한다.
용어 “작동 링커(operative linker)”는 핵산 또는 폴리펩티드의 생물학적 과정을 확보하는 방식으로 핵산 작제물 또는 융합 폴리펩티드의 두 부분을 함께 결합시키는 뉴클레오타이드 또는 아미노산 잔기의 서열을 의미한다.
용어 “병원체(pathogen)”는 숙주에서 질환의 특정 원인 제제, 특히 바이러스, 박테리아, 프리온 또는 기생충과 같은 생물학적 제제(biological agent)를 나타내며, 감염성 제제라고도 한다.
용어 “암(cancer)” 또는 “종양(tumor)"은 비-정상적으로 통제되지 않은 세포 성장으로 인한 신생물 또는 종양을 의미한다. 상기 용어 ”암“은 전악성(pre-malignant) 및 악성(malignant) 암 세포를 함유하는 질환을 포함한다. 일부 실시양태에서, 암은 개체의 다른 부위에 퍼지지 않은 세포의 국부적인 과증식, 즉, 양성 종양을 나타낸다. 다른 실시양태에서, 암은 인접한 신체 구조를 침범하고 파괴하고 멀리 떨어진 지역으로 퍼지는 악성 종양을 나타낸다. 또 다른 실시양태에서, 상기 암은 특정 암 항원과 관련되어 있다.
본 발명에 사용된 용어 "유효량(effective amount)"은 다른 치료법의 예방 효과를 개선 또는 향상시키거나, 암의 중증도 및 암의 지속기간을 감소시키고, 암의 하나 이상의 증상을 개선하고, 암의 진행을 예방하고, 암의 퇴행을 야기하고, 및/또는 다른 치료제의 치료 효과를 개선 또는 향상시키기 위한, 암의 발병, 재발 또는 발달 및 하나 이상의 암 증상의 예방을 초래하기에 충분한 치료의 양을 의미한다. 하나의 실시양태에서, 치료의 양은 1, 2, 3 또는 그 이상의 치료법의 투여 후에 다음의 결과 중 하나, 둘, 셋 또는 그 이상을 달성하는데 효과적이다:(1) 암 줄기 세포 집단의 안정화, 감소 또는 제거; (2) 암세포 집단의 안정화, 감소 또는 제거; (3) 종양 또는 신생물의 성장의 안정화 또는 감소;(4) 종양의 형성 장애; (5) 원발성, 지역성 및/또는 전이성 암의 근절, 제거 또는 조절;(6) 사망률의 감소; (7) 무병 상태, 재발이 없는 상태, 무 진행 상태 및/또는 전체 생존 기간, 지속 기간 또는 비율의 증가; (8) 반응 속도, 반응의 지속성, 또는 반응하거나 완화되는 환자의 수의 증가; (9) 입원율의 감소; (10) 입원 기간 단축; (11) 종양의 크기가 유지되고 10 % 미만, 바람직하게는 5 % 미만, 바람직하게는 4 % 미만, 바람직하게는 2 % 미만으로 증가 또는 증가하지 않음; (12) 완화된 환자 수의 증가; (13) 완화 기간 또는 지속 기간의 증가; (14) 암의 재발률 감소; (15) 암의 재발까지의 시간의 증가; 및 (16) 암-관련 증상 및/또는 삶의 질의 개선.
용어 “펩티드(peptide)”는 서열로 정의하고 아미드 결합에 의해 연결되어 있는 다수의 공유 결합된 아미노산 잔기를 의미한다. 상기 용어는 “올리고펩티드” 및 “폴리펩티드”와 유사하게 사용된다. 천연 및/또는 비-천연 아미노산은 펩티드 결합 또는 비-펩티드 결합으로 연결될 수 있다. 또한 상기 용어 “펩티드”는 당업계에 공지된 바와 같이, 화학적 또는 효소-촉매 반응에 의해 도입된 번역 후 변형(post-translational modifications)을 포괄한다. 상기 용어는 폴리펩티드의 변이체 또는 단편을 의미할 수 있다.
용어 “약제 담체(pharmaceutical carriers)”, “부형제(excipients)” 또는 “안정화제(stabilizers)”는 사용된 투여량 및 농도에서 이에 노출되는 세포 또는 개인에 비-독성이다. 종종 생리학적으로 허용되는 담체는 수성 pH 완충 용액이다. 생리학적으로 허용가능한 담체의 예로는, 인산염, 시트르산 및 다른 유기산과 같은 완충제; 아스코르브 산을 포함하는 항산화제; 저분자량 (약 10 잔기 미만) 폴리펩티드; 혈청 알부민, 젤라틴 또는 면역 글로불린과 같은 단백질; 폴리비닐피롤리돈과 같은 친수성 중합체; 글리신, 글루타민, 아스파라긴, 아르기닌 또는 라이신과 같은 아미노산; 포도당, 만노오스 또는 덱스트린을 포함하는 단당류, 이당류 및 기타 탄수화물; EDTA와 같은 킬레이트 제제; 만니톨 또는 소르비톨과 같은 당 알콜; 나트륨과 같은 염-형성 카운터 이온(counterions); 및/또는 TWEEN ™, 폴리에틸렌 글리콜 (PEG) 및 PLURONICS ™와 같은 비-이온성 계면 활성제를 포함한다.
용어 “프로모터(promoter)”는 RNA 중합 효소가 결합하여 하나 이상의 인접한 구조 유전자에 의한 메신저 RNA(messenger RNA)의 전사를 개시하는 DNA 사슬의 결합 부위를 의미한다.
용어 “신호 펩티드(signal peptide)”는 정렬 펩티드(sorting peptide)라고도 하는 세포 내 단백질의 최종 위치를 결정하는 짧은 아미노산 서열을 의미한다.
용어 “계면 활성제(surfactant)”는 그것이 용해되는 액체의 표면 장력을 감소시킬 수 있는 계면 활성 제제를 의미한다. 계면 활성제는 친수성인 극성 그룹 및 소수성이고 종종 지방족 사슬로 구성된 비-극성 그룹을 포함하는 화합물이다.
용어 “백신(vaccine)”은 동물에서 면역 반응을 유도할 수 있는 물질 또는 조성물을 의미하며, 면역원성 조성물이라고 한다. 면역 반응(체액성/항체 및/또는 세포성)으로 유기체에서 기억을 유도하고, 감염성 제제를 야기하고, 일차성 반응 보다 이차성에 의해 일어나며 숙주 유기체에 영향을 감소시킨다. 백신은 예방약 및/또는 치료제로서 주어질 수 있다. 상기 조성물은 하기 중 하나 이상을 포함할 수 있다: 하나 이상의 종양-관련 항원(들)에 접합된 VGP, 하나 이상의 항원에 작동가능하게 연결된 VGP를 포함하는 핵산 작제물, 담체, 보조제 및 약제학적 담체.
용어 “변이체(variant)”는 주어진 기준(reference) 핵산 또는 폴리펩티드에 대해 일정 정도의 서열 상동성/동일성을 나타내는 핵산 또는 폴리펩티드를 의미하며, 상기 기준 핵산 또는 폴리펩티드와 동일하지는 않다.
1. 변형된 알파 바이러스 당단백질 및 항원을 포함하는 융합 단백질
모든 알파 바이러스와 마찬가지로, 신드비스 유전체는 RNA 복제를 담당하는 4 개의 비-구조 단백질(nsP1-4) 및 5 개의 구조 단백질(캡시드, E3, E2, 6K 및 E1)을 코딩한다. 상기 구조 단백질은 성숙한 단백질을 생성하기 위해 세포 프로테아제에 의해 절단되는 단일 폴리프로테인으로 발현된다(도 1 참조). 상기 캡시드 단백질은 바이러스 유전체를 둘러싼 내부 코어를 형성하고, E2 엔빌로프 당 단백질(envelope glycoprotein)의 세포질내 꼬리와 상호 작용한다(7). E3 단백질은 E3와 E2로 구성된 전구 단백질인 pE2에 대한 신호 서열(signal sequence)로 작용하고, 적절한 E2 폴딩을 매개하며, E1과 E2의 헤테로다이머화에 필요하다(7). 골지체에서 단백질 프로세싱 동안, E3는 푸린(furin)에 의해 절단되고, 세포로부터 바이러스가 나타나기 시작할 때 흘러나온다(7). 신드비스 바이러스("SINV") E2는 196 및 318에서 2 개의 N-연결 글리코실화 위치를 갖는 막 관통성(transmembrane) 당 단백질이다(8). 상기 6K 단백질은 E1에 대한 신호 서열로서 작용하고, 신호 펩티다아제에 의해 E1 및 E2로부터 절단되고, 성숙한 비리온(virion)에 최소한으로 존재한다. SINV E1은 139와 245에서 2 개의 N-연결 글리코실화 위치를 갖는 막 관통성 당 단백질이다(8). 바이러스가 세포에서 나타나기 시작하면, 캡시드는 숙주 세포 원형질막으로부터 유래된 바이러스 엔빌로프 내에 함유되어 있다. E2/E1 헤테로다이머는 바이러스 엔빌로프의 표면에 삼량체 스파이크(trimeric spike)로 존재한다. E2 영역은 표적 세포의 수용체와 상호 작용을 담당하는 반면, E1은 후기 엔도 좀 및 리소좀의 낮은 pH 조건에서 막 융합을 촉발시킨다(8).
본원에 기재된 변형된 바이러스 당 단백질(viral glycoproteins, VGP), E1 및 E2 단백질은 치료를 위한 융합 단백질 VGP-TAA를 형성하는 종양 특이적 항원에 접합된 단일 재조합 단백질(도 3 참조)로서 함께 발현되었다. 특정 실시양태에서, 상기 융합 단백질은 막관통 단백질, 6K 부위 및 비-구조 단백질을 포함하지 않는다. 특정 실시양태에서, 상기 융합 단백질을 발현하는 상기 발현 벡터는 바이러스 벡터가 아니다. 하나의 실시양태에서, 상기 융합 단백질은 서열번호 1의 아미노산 서열을 갖는다. 특정 실시양태에서, 상기 융합 단백질은 하기 변형을 갖는 서열번호 1의 아미노산 서열을 갖는다:(1) 하기 아미노산 잔기의 결실:1-65, 979-978. 상기 융합 단백질은 하나 이상의 종양-관련 항원에 작동 가능하게 연결된 바이러스 표면 막 당 단백질의 뉴클레오티드 서열을 갖는 뉴클레오티드에 의해 코딩되는 재조합 단백질이다. 특정 실시양태에서, 상기 하나 이상의 종양-관련 항원은 NCI Pilot Project to Prioritize Cancer Antigens Clin. Cancer Res 2009; 15:5323-5337.의 표 3에 기재되어 있다.
특정 실시양태에서, 융합 단백질의 상기 종양-관련 항원 부분은 서열번호 3 내지 11과 적어도 % 동일성을 갖는 아미노산 서열일 수 있다. 특정 실시양태에서, 융합 단백질의 상기 종양-관련 항원 부분은 아미노산 위치 877-978에서 서열 번호 1과 적어도 % 동일성을 갖는 아미노산 서열일 수 있다.
특정 실시양태에서, 상기 종양-관련 항원은 서열번호 3 내지 11의 적어도 7, 8, 9, 10, 12, 14, 16, 18, 20, 25, 30, 35, 40, 50, 60, 70, 80, 90, 100, 150, 200, 250 또는 그 이상의 연속적인 아미노산을 포함하며, 연속적인 아미노산은 면역원성이다.
특정 실시양태에서, 상기 종양-관련 항원은 서열번호 3 내지 11로부터 10-20, 20-30, 30-50, 50-150, 150-200, 200-400, 400-500 개의 아미노산을 포함한다. 특정 실시양태에서, 상기 종양 관련 항원은 서열번호 3 내지 11의 전장 단백질(full length protein)을 포함하지 않는다.
특정 실시양태에서, 상기 종양-관련 항원은 서열번호 3 내지 11의 단백질의 1200개 미만의 아미노산, 1100개 미만의 아미노산, 1000개 미만의 아미노산, 950개 미만의 아미노산, 900개 미만의 아미노산, 850개 미만의 아미노산, 800개 미만의 아미노산, 750개 미만의 아미노산, 700개 미만의 아미노산, 650개 미만의 아미노산, 600개 미만의 아미노산, 590개 미만의 아미노산 또는 580개 미만의 아미노산을 갖는다.
상기 기재된 서열번호 3 내지 11로부터의 종양-관련 항원 단편의 비-제한적인 예는 면역원성 단편으로서, 보조제(이에 제한되지는 않으나 하기의 “면역원성 조성물 및 의약품”부분에 열거되거나 논의된 보조제를 포함) 또는 상기 폴리펩티드에 결합된 적합한 단편을 포함할 수 있는 적합한 조성물로 개체에게 투여될 때, 단리된 전장 폴리펩티드 서열 번호 3-11 각각으로부터 유도된 면역원성 단편을 인식하는 항체 또는 T 세포-매개 면역 반응을 유도한다.
종양-관련 항원은, 서열 번호 3 내지 11 중 임의의 것과 비교하여, 보존적 치환(즉, 하나의 아미노산이 관련된 측쇄를 갖는 다른 아미노산으로 치환됨)과 같은 하나 이상(예를 들어, 1, 2, 3, 4, 5, 6, 7, 8, 9 등) 아미노산 치환을 포함한다. 유전자로 코딩된 아미노산은 일반적으로 4가지 계열로 나누어진다: (1) 산성 아미노산, 즉 아스파테이트, 글루타메이트; (2) 염기성 아미노산, 즉 리신, 아르기닌, 히스티딘; (3) 비극성 아미노산, 즉 알라닌, 발린, 류신, 이소류신, 프롤린, 페닐알라닌, 메티오닌, 트립토판; 및 (4) 비전하 극성 아미노산, 즉 글리신, 아스파라긴, 글루타민, 시스테인, 세린, 트레오닌, 티로신. 페닐알라닌, 트립토판 및 티로신은 때때로 방향족 아미노산으로 분류된다. 일반적으로, 이러한 계열 내에서 단일 아미노산의 치환은 생물학적 활성에 중요한 영향을 미치지 않는다.
폴리펩티드는 서열번호 3 내지 11 중 임의의 하나와 관련하여 하나 이상(예를 들어, 1, 2, 3, 4, 5, 6, 7, 8, 9 등) 단일 아미노산 결실을 포함할 수 있다. 유사하게, 폴리펩티드는 서열번호 3 내지 11 중 임의의 하나와 관련하여 하나 이상(예를 들어, 1, 2, 3, 4, 5, 6, 7, 8, 9 등) 삽입(예를 들어, 각각 1, 2, 3, 4 또는 5 개의 아미노산)을 포함할 수 있다.
결실 또는 치환은 N-말단 및/또는 C-말단에 존재할 수 있거나, 두 말단 사이에 존재할 수 있다. 그러므로, 절단(truncation)이 결실의 예다. 절단은 N-말단 및/또는 C-말단에서 최대 40 개(또는 그 이상)의 아미노산의 결실을 포함할 수 있다.
일반적으로, 본 발명의 폴리펩티드가 서열번호 3 내지 11의 완전한 서열과 동일하지 않은 서열을 포함하는 경우(예를 들어, 100% 미만의 서열 동일성을 갖는 서열 목록을 포함하는 경우 또는 그의 단편을 포함하는 경우), 폴리펩티드가 완전한 서열 번호로 이루어진 폴리펩티드를 인식하는 항체, 즉, 상기 서열번호 3 내지 11 중 하나 이상에 결합하는 항체를 유도할 수 있는 것이 바람직하다. 이러한 항체는 비-특이적 결합 표준으로서의 인간 혈청 알부민에 대한 항체의 비-특이적 친화도보다 상당히 높은 친화도를 갖는 상동체(homologs)가 아닌 다른 단백질에 결합하지 않으면서, 서열번호 3 내지 11에 각각 특이적으로 결합할 수 있다.
본 발명의 폴리펩티드는 금속 이온, 예를 들어, 폴리펩티드 사슬에서 하나 이상의 아미노산에 의해 조절되는 금속 이온을 포함할 수 있다. 예를 들어, 상기 폴리펩티드는 1가, 2가 또는 3가 금속 양이온을 포함할 수 있다. Mn2+, Fe2+, Co2+, Ni2+, Cu2+ 등과 같은 2가 양이온이 전형적이다. 상기 2가 양이온은 바람직하게는 Zn2+이다.
본원에 기재된 폴리펩티드는 다양한 형태(예를 들어, 천연, 융합, 글리코실화, 비-글리코실화, 지질화, 비-지질화, 인산화, 비-인산화, 미리스토일화, 비-미리스토일화, 단량체, 다량체, 미립자, 변성 등)를 가질 수 있다. 예를 들어, 본 발명의 폴리펩티드는 지질화된 N-말단 시스테인을 가질 수 있다.
본원에 기재된 폴리펩티드는 다양한 수단(예를 들어, 재조합 발현, 세포 배양으로부터의 정제, 화학적 합성 등)에 의해 제조 될 수 있다. 재조합-발현된 단백질이 바람직하다.
본원에 개시된 폴리펩티드는 바람직하게는 정제되거나 실질적으로 정제된 형태, 즉, 다른 폴리펩티드가 실질적으로 없는(예: 자연적으로 발생되는 폴리펩티드가 없는), 특히 다른 대장균 또는 숙주 세포 폴리펩티드가 없으며, 일반적으로 적어도 약 50 중량% 이상 순수하고, 통상적으로 약 90 중량%이상 순수하며, 즉, 조성물의 약 50 중량% 미만, 보다 바람직하게는 약 10 중량% 미만(예: 5 중량%)이 다른 발현된 폴리펩티드로 이루어진다. 따라서, 조성물 내의 상기 항원은 상기 분자가 발현되는 전체 유기체로부터 분리된다.
펩티드 단편으로부터의 종양-관련 항원 내의 에피토프는 B-세포 에피토프 및/또는 T-세포 에피토프일 수 있다. 상기한 에피토프는 경험적으로(예를 들어, PEPSCAN 또는 유사한 방법을 사용하여)확인될 수 있거나, 예측할 수 있다(예를 들어, Jameson-Wolf 항원 지수, 매트릭스-기재 접근법(matrix-based approach), MAPITOPE, TEPITOPE, 신경 네트워크, OptiMer & EpiMer, ADEPT, Tsites, 친수성, 항원 지수 등). 에피토프는 항체 또는 T 세포 수용체의 항원 결합 부위에 의해 인식되고 결합하는 항원의 일부이며, “항원 결정기 (antigenic determinants)”라고도 한다.
본원에 기재된 임의의 폴리펩티드는 백신의 성분으로서 유용성을 갖는다. 따라서, 또 다른 실시양태에서, 상기 단리된 또는 재조합 폴리펩티드는 보조제와 함께 존재할 것이다.
하나의 실시양태에서, 상기 융합 단백질은 하나 이상의 항원 단백질 또는 이외 펩티드 또는 단편을 포함하고, 상기 항원 단백질은 종양-관련 항원 단백질이다. 많은 단백질이 특정 유형의 암과 관련되어 있는 것을 확인하였다; 이를 종양-관련 항원이라고 한다. 일반적으로, 암 종양과 관련된 것으로 밝혀진 임의의 항원이 사용될 수 있다. 특정 실시양태에서 상기 종양 관련 항원은 WT1(UniProt Knowledgebase, MUC1(P15941), LMP2(P13285), HPV16 E6(P03126) 및 E7(P03129), HPV18(E6-P06463) 및 E7(P06788), RGL4(Q8IZJ4), EGFRvIII(P0533), HER-2/neu(P04626), MAGE A3(Q53EX0), PSMA(Q04609), CEA(P06731), MelanA/MART(Q16655), gp100(P40967), Proteinase3(PR1)(P24158), bcr-abl 융합, bcr(P11274), abl(P00519), 티로시나제(Tyrosinase, P14679), 서비빈(Survivin, O15392), PSA(P07288), hTERT(O14746), EphA2(P29317), PAP(P15309), ML-IAP(Q96CA5), AFP(P02771), EpCAM(P16422), TMPRSS2/ERG 융합, TMPRSS2(O15393), ERG(P11308), PAX3(P23760), ALK(Q9UM73), 안드로젠 수용체(Androgen receptor, P10275), Cyclin B1(P14635), MYCN(P04198), RhoC(P08134), TRP-2(P40126), ㅁ메멧메소텔린(Mesothelin, Q13421), PSCA(O43653), MAGE A1(P43355), CYP1B1(Q16678), PLAC1(Q9HBJ0), BORIS(Q8NI51), NY-BR-1(Q9BXX3), RGS5(O15539), SART3(Q15020), Carbonic anhydrase IX(Q16790), PAX5(Q02548), OY-TES1(Q8NEB7), 정자 단백질 17(Sperm protein 17, Q15506), LCK(P06239), HMWMAA(Q6UVK1), AKAP-4(Q5JQC9), SSX2(Q16385), XAGE 1(Q9HD64), Legumain(Q99538), Tie 2(Q02763), VEGFR2(P35968), PDGFR-β(P09619), 및 Fos-related antigen 1(P15407)이다.
특정 실시양태에서, 하나 이상의 알파 바이러스 표면 막 당 단백질은 하나 이상의 종양-관련 항원에 작동 가능하게 연결된다. 하나의 실시양태에서, 상기 종양 특이적 항원은 암-고환 항원 NY-ESO-1의 일차 항원 영역이다. 특정 실시양태에서, 상기 종양 특이적 항원은 암 면역 요법을 위한 표적 인간 TAA의 목록을 포함한다(9). 구체적인 실시양태에서, 상기 SINV VGP 재조합 단백질은 융합 단백질을 형성하기 위해 NY-ESO-1 단백질의 1 차 항원 영역에 접합된다.
특정 실시양태에서, 부가적인 N-연결된 글리코실화 부분은 바이러스 당 단백질로 제조될 수 있다. N-연결된 글리칸은 아스파라긴-X-세린/트레오닌 서열의 일부로서 존재하는 아스파라긴 측쇄에 부착되며, 여기서 X는 프롤린을 제외한 임의의 아미노산이다.
또한 본원은 하나 이상의 종양-관련 항원 및 서열번호 1로 표시되는 아미노산 서열 또는 이의 단편을 갖는 하나 이상의 알파 바이러스 표면 막 당 단백질을 포함하는 융합 단백질을 코딩하는 핵산 구조물에 관한 것이다. 특정 실시양태에서, 상기 단편은 40-80, 80-150, 150-200, 200-300, 300-400, 400-500, 500-600, 600-700, 700-800, 800-850, 850-900 아미노산 잔기를 갖는다. 특정 실시양태에서, 상기 단편은 서열번호 2와 적어도 85%, 90%, 95%, 99% 이상 동일하다. 특정 실시양태에서, 상기 종양-관련 항원은 전장 단백질이다. 특정 실시양태에서, 상기 종양-관련 항원은 전장 단백질의 단편이다. 특정 실시양태에서, 상기 단편은 5-10, 10-20, 20-30, 30-40, 40-80, 80-150, 150-200, 200-300, 300-400, 400-500, 500-600 아미노산 잔기를 갖는다. 특정 실시양태에서, 상기 단편은 야생형 종양 관련 항원과 적어도 85%, 90%, 95%, 99% 동일하다. 아미노산 서열 간의 동일성/상동성은 블로섬(BLOSUM) 30, BLOSUM 40, BLOSUM 45, BLOSUM 50, BLOSUM 55, BLOSUM 60, BLOSUM 62, BLOSUM 65, BLOSUM 70, BLOSUM 75, BLOSUM 80, BLOSUM 85, 및 BLOSUM 90 중 임의의 하나와 같은 잘 알려진 스코어링 매트릭스를 사용하여 계산 될 수 있다
특정 실시양태에서, 상기 종양-관련 항원은 서열번호 3 내지 11 중 임의의 서열의 적어도 10개 이상의 연속적인 아미노산인 폴리펩티드 단편이고, 상기 적어도 10개 이상의 연속적인 아미노산을 포함하는 폴리펩티드 단편은 면역원성이며, 상기 면역원성 폴리펩티드 단편은 서열번호 3 내지 11의 폴리펩티드의 1100개 미만의 아미노산을 포함하는 단편이다.
하나의 실시양태에서, 본원에서 알파 바이러스 표면 막 당 단백질 E1, E2 및 선택적으로 E3, 링커 및 적어도 하나 이상의 종양-관련 항원으로 필수적으로 이루어진 단리 또는 재조합 융합 단백질이 기재되어 있으며, 상기 융합 단백질은 개체에게 투여하였을 때 면역 반응을 자극한다. 하나의 실시양태에서, 상기 융합 단백질은 서열번호 1과 적어도 98% 이상의 동일성을 갖는 아미노산 서열을 포함한다. 하나의 실시양태에서, 상기 융합 단백질은 적어도 서열번호 1의 66-978 위치의 아미노산 잔기를 포함한다. 하나의 실시양태에서, 상기 융합 단백질은 서열번호 2와 적어도 95%의 동일성을 갖는 핵산 분자에 의해 코딩된다. 하나의 실시양태에서, 상기 융합 단백질은 서열번호 1의 (i) 1-65 위치; (ii) 979-984 위치; 또는 (iii) 1-65 및 979-984 위치에서 아미노산 잔기의 결실을 추가로 포함한다. 하나의 실시양태에서, 상기 E2는 적어도 300개 아미노산 길이이고 서열번호 1의 66-429 위치에서 적어도 95%의 서열 동일성을 갖는 아미노산 서열을 포함한다. 하나의 실시양태에서, 상기 E1은 적어도 300개 아미노산 길이이고 서열번호 1의 449-854 위치에서 적어도 95%의 서열 동일성을 갖는 아미노산 서열을 포함한다. 하나의 실시양태에서, 상기 종양-관련 항원은 서열번호 3 내지 11 중 임의의 서열의 적어도 10 개의 연속적인 아미노산인 폴리펩티드 단편이고, 상기 적어도 10개의 연속적인 아미노산을 포함하는 폴리펩티드 단편은 면역원성이며, 상기 면역원성 폴리펩티드 단편은 서열번호 3 내지 11의 폴리펩티드의 1100개 미만의 아미노산을 포함하는 단편이다.
또한 당업자는 상기가 바이러스 항원에 적용될 수 있다는 것을 알 수 있다.따라서, 특정 실시양태에서, 상기 종양 관련 항원은 바이러스 항원으로 대체된다. 특정 실시양태에서, 상기 융합 단백질은 하나 이상의 바이러스 항원 및 하나 이상의 알파 바이러스 표면 막 당 단백질을 포함한다. 특정 실시 양태에서, 상기 바이러스 항원은 HSV-1 당 단백질 B(P06437), 당 단백질 E(P04488), HIV gag-pol(P04585), 수두(수두 대상 포진(Varicella zoster)), 당 단백질 B (Q4JR05) 또는 당 단백질 E(Q9J3M8)이다.
2. VGP-TAA 제조 방법
본원에서는 폴리펩티드 발현을 유도하는 조건 하에서 상기 융합 단백질을 코딩하는 핵산으로 형질 전환된 숙주 세포를 배양하는 단계를 포함하는 융합 단백질을 생산하는 방법을 제공한다. 이어서, 폴리펩티드는 예를 들어, 배양 상등액으로 정제될 수 있다.
본 발명은 화학적 수단에 의해 폴리펩티드의 최소한 일부분 이상을 합성하는 단계를 포함하는 본 발명의 폴리펩티드를 제조하는 방법을 제공한다.
상기 기재된 단백질, 폴리펩티드, 하이브리드 폴리펩티드, 에피토프 및 면역원성 단편 중 임의의 모든 것은, 재조합, 단리 또는 실질적으로 정제된(그들의 천연 상태의 단백질, 폴리펩티드, 하이브리드 폴리펩티드, 에피토프 및 면역원성 단편과 함께 존재하는 물질들로부터) 다수의 형태 중 어느 하나일 수 있으며, 이에 제한되는 것은 아니다.
본 발명의 한 측면에서, 본원에 기재된 상기 융합 단백질은 하나 이상의 종양-관련 항원에 작동 가능하게 연결된 하나 이상의 바이러스 표면 막 당 단백질을 포함하는 핵산 작제물에 의해 코딩된다. 상기 융합 단백질은 하나 이상의 종양-관련 항원에 작동 가능하게 연결된 바이러스 표면 막 당 단백질의 뉴클레오티드 서열을 갖는 뉴클레오티드에 의해 코딩되는 재조합 단백질이다. 하나의 실시양태에서, 상기 핵산 작제물은 발현 벡터이다. 하나의 실시양태에서, 상기 발현 벡터는 비-바이러스 성, 바이러스 성 또는 플라스미드이다. 특정 실시양태에서, 상기 발현 벡터는 유전자 또는 유전자 단편, 프로모터, 인핸서, 종결 시그널, 폴리-A 테일, 링커, 폴리 링커, 작동 링커, 다중 클로닝 부위, 마커, STOP 코돈, 내부 리보솜 진입 부위, 숙주 상동성 서열(host homologous sequences for integration) 또는 기타 정의된 요소(elements) 을 포함한다. 핵산 구조물을 제조하는 방법은 당해 분야에 잘 알려져 있다(Molecular Cloning: A Laboratory Manual, Sambrook et al, eds., Cold Spring Harbor Laboratory, 2nd Edition, Cold Spring Harbor, N.Y., 1989 참조).
일부 실시양태에서, 본 발명의 핵산은 낮은 스트린전시 조건(low stringency conditions)하에서 표적에 하이브리드화 한다; 다른 실시양태에서, 중간의 스트린전시 조건(intermediate stringency conditions)하에서 하이브리드화 한다; 바람직한 실시양태에서, 본 발명의 핵산은 높은 스트린전시 조건(high stringency conditions)하에서 하이브리드화 한다. 낮은 스트린전시 하이브리드화 조건의 예시적인 세트는 50℃ 및 10×SSC이다. 중간의 스트린전시 하이브리드화 조건의 예시적인 세트는 55℃ 및 1×SSC이다. 높은 스트린전시 하이브리드화 조건의 예시적인 세트는 68℃ 및 0.1×SSC이다.
본 발명은 이들 서열에 상보적인 서열을 함유하는 핵산을 포함한다(예를 들어, 안티센스 또는 프로빙, 또는 프라이머로서 사용하기 위한 핵산).
본 발명의 핵산은 하이브리드화 반응(예를 들어, 노던 또는 서던 블롯, 또는 핵산 마이크로 어레이 또는 '유전자 칩'), 증폭 반응(예를 들어, PCR, SDA, SSSR, LCR, TMA, NASBA 등) 및 다른 핵산 기술에 사용될 수 있다.
본 발명에 따른 핵산은 다양한 형태 (예: 단일 가닥, 이중 가닥, 벡터, 프라이머, 프로브, 표지 등)를 취할 수 있다. 본 발명의 핵산은 원형 또는 가지형 일 수 있지만, 일반적으로 선형일 것이다. 달리 명시되거나 요구되지 않는 한, 핵산을 이용하는 본 발명의 임의의 실시양태는 이중 가닥 형태 및 이중 가닥 형태를 이루는 2개의 상보적인 단일 가닥 형태의 각각을 이용할 수 있다. 프라이머 및 프로브는 일반적으로 단일 가닥이며, 안티센스 핵산도 마찬가지이다.
본 발명의 핵산은 바람직하게는 정제되거나 실질적으로 정제된 형태, 즉 다른 핵산(예를 들어, 자연 발생한 핵산이 없는), 특히 숙주 세포 핵산을 실질적으로 함유하지 않은 것으로서, 일반적으로 적어도 약 50 중량% 이상 순수한 것 및 보통 적어도 약 90 % 이상 순수한 것이다.
본 발명의 핵산은 게놈 또는 cDNA 라이브러리 등으로부터 많은 방법, 예를 들면 전체 또는 부분적으로 화학적 합성(예: DNA의 포스포라미디트 합성), 뉴클레아제(예: 제한 효소)를 사용하여 더 긴 핵산을 분해, 더 짧은 핵산 또는 뉴클레오티드를 결합(예: 리가아제 또는 폴리머라아제를 사용)함으로써 제조될 수 있다.
본 발명의 핵산은 고체 지지체(예: 비드, 플레이트, 필터, 필름, 슬라이드, 마이크로 어레이 지지체, 수지 등)에 부착 될 수 있다. 본 발명의 핵산은 예를 들어, 방사성 또는 형광성 라벨 또는 바이오틴 라벨 로 표지될 수 있다. 이는 핵산이 검출 기술에 사용되는 경우에 특히 유용하며, 예를 들면, 여기서 핵산은 프라이머 또는 프로브이다.
상기 용어 "핵산"은 일반적으로 데옥시리보뉴클레오티드, 리보뉴클레오티드 및/또는 이들의 유사체를 함유하는 임의의 길이의 중합체 형태의 뉴클레오티드를 의미한다. 이는 DNA, RNA, DNA/RNA 하이브리드를 포함한다. 또한, 이는 변형된 주쇄(예: 펩타이드 핵산(PNA) 또는 포스포로티오에이트(phosphorothioates)) 또는 변형된 염기와 같은 DNA 또는 RNA 유사체를 포함한다. 따라서, 본 발명은 mRNA, tRNA, rRNA, 리보자임, DNA, cDNA, 재조합 핵산, 분지된 핵산, 플라스미드, 벡터, 프로브, 프라이머 등을 포함한다. 본 발명의 핵산이 RNA의 형태를 취하는 경우, 5′캡을 갖거나 갖지 않을 수 있다.
본 발명의 핵산은 벡터의 일부, 즉 하나 이상의 세포 유형의 형질 도입/형질 감염을 위해 제조된 핵산 작제물의 일부일 수 있다. 벡터는 예를 들어, 삽입된 뉴클레오티드의 분리, 증식 및 복제를 위해 제조된 "클로닝 벡터", 숙주 세포에서 뉴클레오티드 서열의 발현을 위해 제조된 "발현 벡터", 재조합 바이러스 또는 바이러스-유사 입자의 생산을 초래하도록 제조된 "바이러스 벡터" 또는 둘 이상의 유형의 벡터의 속성을 포함하는 "셔틀 벡터"일 수 있다. 바람직한 벡터는 전술한 바와 같은 플라스미드이다. "숙주 세포 (host cell)"는 외인성 핵산의 수령자일 수 있거나 수령되어 온 개별 세포 또는 세포 배양액을 포함한다. 숙주 세포는 단일 숙주 세포의 자손을 포함하며, 상기 자손은 자연적, 우발적 또는 고의적인 돌연변이 및/또는 변화로 인해 원래의 모세포와 완전히 동일(형태학적 또는 전체 DNA 보체에서)하지 않을 수 있다. 숙주 세포는 본 발명의 핵산으로 생체 내 또는 시험 관내에서 형질 감염되거나 감염된 세포를 포함한다.
핵산이 DNA인 경우, RNA 서열의 "U"는 DNA에서 "T"로 대체되어 인식될 것이다. 유사하게, 핵산이 RNA인 경우, DNA 서열에서의 "T"는 RNA에서 "U"로 대체되어 인식될 것이다.
핵산과 관련하여 사용될 때 상기 용어 "보체(complement)" 또는 "보완적(complementary)"은 왓슨-크릭(Watson-Crick) 염기쌍을 의미한다. 따라서, C의 보체는 G이고, G의 보체는 C이며, A의 보체는 T(또는 U)이며, T (또는 U)의 보체는 A이다. 또한, 이는 I(퓨린 이노신)와 같은 염기, 예를 들어. 피리미딘(C 또는 T)을 보체로 사용할 수 있다.
본 발명의 핵산은 예를 들어, 폴리펩티드를 생성; 생물학적 샘플에서 핵산 검출을 위한 하이브리드화된 프로브로서 사용하거나; 핵산의 추가적인 복사본을 생성하는데 사용하거나; 리보자임 또는 안티센스 올리고 뉴클레오타이드를 생성하는데 사용하거나; 단일 가닥 DNA 프라이머 또는 프로브로서; 또는 삼중 가닥 형성 올리고 뉴클레오티드로서 사용될 수 있다.
본 발명은 본 발명의 핵산의 제조 방법을 제공하며, 여기서 핵산은 화학적 수단을 사용하여 부분적으로 또는 전체적으로 합성된다.
본 발명은 본 발명의 뉴클레오티드 서열을 포함하는 벡터(예: 클로닝 또는 발현 벡터) 및 이러한 벡터로 형질 전환된 숙주 세포를 제공한다.
본 발명에 따른 핵산 증폭은 정량적 및/또는 실시간일 수 있다.
본 발명의 특정 실시양태에서, 핵산은 바람직하게는 길이가 적어도 7 개 뉴클레오티드(예를 들어, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 45, 50, 55, 60, 65, 70, 75, 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, 200, 225, 250, 275, 300 뉴클레오티드 또는 그 이상)이다.
본 발명의 특정 실시양태에서, 핵산은 바람직하게는 길이가 최대 500 뉴클레오티드(예를 들어, 450, 400, 350, 300, 250, 200, 150, 140, 130, 120, 110, 100, 90, 80, 75, 70, 65, 60, 55, 50, 45, 40, 39, 38, 37, 36, 35, 34, 33, 32, 31, 30, 29, 28, 27, 26, 25, 24, 23, 22, 21, 20, 19, 18, 17, 16, 15 개 뉴클레오티드 또는 그 이하)이다.
본 발명의 프라이머 및 프로브, 및 하이브리드화에 사용되는 다른 핵산은 바람직하게는 길이가 10 내지 30 뉴클레오티드(예를 들어, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29 또는 30 뉴클레오티드)이다.
특정 실시양태에서, 융합 단백질을 코딩하는 상기 개시된 핵산 작제물은 작동 링커를 통해 하나 이상의 종양-관련 항원에 접합된 하나 이상의 알파 바이러스 표면 막 당 단백질을 포함한다. 하나의 실시양태에서, 상기 링커는 직접 링크(direct link)이다. 하나의 실시양태에서, 상기 링커는 스페이서 영역(spacer region)이다. 용어 "작동 링커(operative linker)"는 핵산 또는 단백질의 생물학적 처리를 확보하는 방식으로 핵산 작제물 또는 융합 단백질의 두 부분을 함께 결합시키는 뉴클레오티드 또는 아미노산 잔기의 서열로 이해된다. 작동 링커가 직접 연결인 경우, 개방 판독 프레임 또는 개방 판독 프레임의 단편을 각각 코딩하는 두 개의 핵산이 서로 바로 인접하였고, 프레임 내에 위치한다. 작동 링커가 스페이서 영역에 의해 매개되는 경우, 일련의 뉴클레오티드가 하나 이상의 알파 바이러스 표면 막 당 단백질 및 하나 이상의 종양-관련 항원을 코딩하는 뉴클레오티드 사이에 삽입된다. 특정 실시양태에서, 상기 작동 링커는 적어도 하나의 폴리 링커 또는 다중 클로닝 사이트(multiple cloning site, MCS)를 포함한다.
핵산 작제물의 예는 서열번호 2로 표시되는 서열뿐만 아니라 도 6에도 제공된다. 서열번호 1의 부분적인 벡터 서열은 상기 기재된 바와 같이 다양한 요소를 서브클로닝(subcloning)함으로써 생성되었다. 이러한 부분 서열은 모두 pUC57에 삽입된 다음 pFastBac1로 옮겨진다(GenBank 수탁 번호 AY598466을 참조).
하나의 실시양태에서, 막 횡단 및 6K 영역은 제거되고, E2 및 E1은 유연한 링커에 의해 연결된다. E3 서열은 ER 표적화 서열로서 작용하고, E2/E1 이량체화를 보조한다. TAA는 다른 유연한 링커(flexible linker) 및 프로테아제 절단 부위와 함께 E1의 C-말단에 첨가된다. VGP는 골지체에서 분비된 후 삼량체화하여, TAA를 갖는 용해성 스파이크를 형성한다. 하나의 실시양태에서, 상기 단백질은 바큘로 바이러스 발현 시스템에 의해 곤충 세포에서 제조되었다.
하나의 실시 양태에서, 조작된 재조합 알파 바이러스 당 단백질(VGPs)은 바큘로 바이러스 발현 시스템을 사용하여 생산되고, 천연 바이러스와 비교할만한 표적 특이성을 갖는다.
특정 실시양태에서, 적절한 글리코실화는 바람직하지 않은 면역 반응을 유도하지 않는 융합 단백질에서 유지된다.
특정 실시양태에서, 상기 융합 단백질은 가용성이다. 특정 실시양태에서, 상기 융합 단백질은 불용성이다.
특정 실시 양태에서, 본 발명에 기재된 방법은 직접적으로 종양 세포를 사멸시키는 것이다. 특정 실시양태에서, 본 발명에 기재된 방법은 바이러스 진입시에 발생하며 바이러스 복제를 필요로 하지 않는 세포 사멸(apoptosis)의 유도이다. 특정 실시양태에서, 융합 단백질상의 당 단백질은 세포 사멸을 유도한다. 특정 실시양태에서, 다른 종양-관련 항원의 방출은 종양 사멸을 유발한다. 특정 실시 양태에서, 종양 세포 표면에 바이러스 단백질의 표시는 세포 독성 T 세포 및/또는 NK 반응을 유도한다.
특정 실시양태에서, 상기 재조합 발현 벡터는 특정 전달 비히클을 통해 전달된다. 상기 전달 비히클은 RNA 또는 DNA-기반 비히클, 지질-기반 비히클, 세포-기반 비히클, 생분해성 고분자 미세구, 리포솜, 콜로이드성 금 입자 또는 지질다당류(lipopolysaccharide)일 수 있다. 또한 노출된 DNA(naked DNA)는 유전자 총(gene gun)과 같은 입자 충격 장비를 사용하는 탄도 이동과 같은 기계적 또는 전기적 기술에 의해 전달 될 수 있다.
하나의 실시양태에서, VGP-TAA 융합 단백질은 재조합 발현 벡터에 의해 생성된다. 하나의 실시양태에서, 신드비스 융합 당 단백질은 Sf9 곤충 세포에서 바큘로 바이러스 발현에 의해 생성된다. 상기 바큘로 바이러스 시스템은 재조합 단백질 발현을 위한 곤충 세포를 사용하는 다용도의 강력한 진핵 벡터 시스템이며, 다른 발현 벡터 시스템에 비해 많은 이점을 제공한다(10). 바큘로 바이러스는 특정한 무척추동물에만 감염할 수 있기 때문에, 포유류에 비-병원성을 나타낸다. 박테리아 단백질 발현과 달리, 바큘로 바이러스 시스템에서 발현된 단백질은 포유류 발현 시스템에서 생산된 것과 유사하게 처리, 접힘 및 변형된다. 게다가, 바큘로 바이러스 - 발현된 단백질은 쉽게 재조합 단백질을 대량으로 생산하도록 스케일 업(scale up) 된다. 현탁 배양에서 잘 자라는 곤충 세포주를 이용할 수 있으며, 대규모 생물 반응기(large-scale bioreactors)에서 재조합 단백질을 생산할 수 있다. 바큘로 바이러스 시스템의 사용은 본 발명의 단백질에 특유한 다른 이점을 제공한다. 곤충 및 포유류 세포는 모두 N-연결 글리코실화를 할 수 있지만, 특정한 글리코실화 경로는 다르다. 곤충 세포에서 생산된 N-글리칸은 고-만노오스 또는 파우시만노시드(paucimannosidic) 구조를 가질 수 있으며, 이들 모두는 말단 만노오스 잔기를 갖는다(11). 포유류 세포에서 생산된 N-글리칸은 고-만노오스 구조 또는 갈락토오스 및 시알산에서 종결되는 복합체 구조를 가질 수 있다(11). VGP를 코딩하는 유전자는 유전자 합성을 통해 생산되고 곤충 세포 발현을 위해 코돈 최적화된다. pE2 및 E1 신드비스 당 단백질의 세포외 영역으로 구성된 재조합 융합 단백질은 유연한 링커에 의해 연결되고 제2링커에 의해 TAA에 연결되었다(도 3 참조). 하나의 실시양태에서, 상기 TAA는 NY-ESO-1이다. 다른 실시양태에서, 다른 TAA가 코딩 서열에 삽입된다. 특정 실시양태에서, 2개 이상의 TAA가 텐덤(tandem)으로 있는 작제물이 제조되는데, 이를 통해 보다 강력한 면역 반응을 유도할 수 있다.
특정 실시양태에서, 면역 반응의 임의의 유형, 예를 들어, T 세포 매개 및 항체 매개 반응은 면역 반응을 유도하기 위한 다양한 강도를 갖는 항원의 에피토프로 개시 될 수 있다. 특정 실시양태에서, 상기 융합 단백질은 통상적인 면역화 방법을 사용하는 경우에는 너무 약한 것으로 알려진 종양-관련 항원에 대한 면역 반응을 성공적으로 유도한다. 특정 실시양태에서, 본 발명에 기재된 바와 같이 상기 융합 단백질은 기존의 면역화 방법(Saroja, Laskshmi 및 Bhaskaran. Int J Pharm Investig. 2011년)보다 5-10 배, 10-20 배, 20-30 배, 30-50 배, 50-100 배, 100-500 배, 500-1000 배 더 성공적으로 면역 반응을 유도한다.
특정 실시양태에서, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 20, 30, 40, 50 또는 그 이상의 TAA가 VGP에 접합된다. pE2의 E3 성분은 단백질의 분비를 위한 신호 펩타이드로 작용하고, E1과 E2의 결합을 보조하고, 퓨린(furin)에 의해 성숙한 단백질로부터 절단된다(7). 상기 성숙한 분비된 단백질은 SINV 엔빌로프에서 관찰되는 삼량체 당 단백질 스파이크를 모방한 E2와 E1의 헤테로다이머 복합체의 삼량체를 형성한다. 제2의 유연한 링커는 E2/E1의 다중화를 방해하지 않으며 NY-ESO-1을 적절하게 접을 수 있다. 특정 실시양태에서, 상기 TAA는 NY-ESO-1의 아미노산 잔기 1 내지 180을 함유한다. 다른 실시양태에서, 상기 TAA는 NY-ESO-1의 아미노산 잔기 81-180을 함유한다. 특정 실시양태에서, His-태그는 정제를 목적으로 단백질의 C-말단에 추가된다. 상기 융합 단백질을 분석하여 비-변성 겔 및 크기-배제 크로마토그래피에 의해 다중 구조를 결정한다. 상기 융합 단백질은 특이적인 ELISA 및 웨스턴 블랏 분석에 의해 분석된다. 상기 융합 단백질은 상업적 항체로 검출될 수 있는 몇 가지 항원 표적(NY-ESO-1, His-tag 및 SINV E1 및 E2)을 갖는다. 특정 실시 양태에서, 상기 TAA는 RGL4이다. 특정 실시 양태에서, 상기 TAA는 인간 유두종 바이러스의 E6 단백질이다. 특정 실시 양태에서, 상기 TAA는 인간 유두종 바이러스의 E7 단백질이다.
또한 본원에는 상기한 융합 단백질을 코딩하는 핵산 작제물을 포함하는 세포가 기재되어 있다. 그러한 재조합 세포는 시험관내 연구를 위한 도구로서, 핵산 작제물을 위한 전달 비히클로서 또는 유전자 치료 요법의 일부로서 사용될 수 있다.
또한 본원에서는 상기한 융합 단백질과 면역 특이적으로 결합하는 항체 또는 결합 단편이 기재되어 있다. 특정 실시양태에서, 상기 항체는 항원에 면역 특이적으로 결합하는 면역 글로불린 분자 및 이의 활성 단편이다. 상기 항체 및 결합 단편은 개체의 면역화에 사용될 수 있다. 상기 항체 및 결합 단편은 항원을 검출하기 위한 분석에 사용될 수 있다.
3. 면역원성 조성물 및 의약품
본 발명의 폴리펩티드는 면역원성 조성물에서 활성성분(면역원)으로서 유용하며, 이러한 조성물은 백신으로서 유용할 수 있다. 본 발명에 따른 백신은 예방적 용도(즉, 감염 방지용) 또는 치료적 용도(즉, 감염 치료용) 일 수 있지만, 일반적으로 예방적 용도로 사용된 것이다.
면역원성 조성물은 약학적으로 허용될 수 있다. 상기 면역원성 조성물은 보통 항원 이외에 기타 성분을 포함 할 수 있는데, 예를 들면, 이들은 전형적으로 하나 이상의 약제학적 담체, 부형제 및/또는 보조제를 포함한다. 또한, 하나 이상의 종양-관련 항원에 작동 가능하게 연결된 하나 이상의 알파 바이러스 표면 막 당단백질을 포함하는 융합 단백질을 코딩하는 핵산 서열을 포함하는 백신이 본원에 개시되어 있다. 따라서 상기 백신은 핵산 작제물을 포함하거나 상기 정의된 바와 같은 융합 단백질을 포함할 수 있다. 뿐만 아니라 상기 백신은 약물로서 사용될 수 있다.
상기 백신 조성물은 활성제제와 함께 부형제 또는 안정화제로도 알려져 있는 하나 이상의 약학적으로 허용 가능한 담체(carriers)의 혼합물과 같은 공지된 방법에 따라 제제화될 수 있다. 이러한 부형제는 개체, 바람직하게는 척추동물, 보다 바람직하게는 인간에 투여하는 것이 허용될 수 있는데, 그것은 투여 용량 및 농도에 노출된 세포 또는 개체에게는 비-독성이기 때문이다. 특정 실시양태에서, 허용 가능한 담체는 수용성 pH 완충 용액이다. 이러한 부형제, 담체 및 제제의 예는, Remington 's Pharmaceutical Sciences (Maack Publishing Co, Easton, PA) 문헌 등에 기재되었습니다. 생리학적으로 허용 가능한 담체의 예는 다음을 포함 하나 이에 한정되지 않는다: 인산염, 시트르산 및 기타 유기산과 같은 완충제; 아스코르브산을 포함하는 항산화제; 저분자량(약 10 잔기 미만) 폴리펩티드; 혈청 알부민, 젤라틴 또는 면역 글로불린과 같은 단백질; 폴리비닐피롤리돈과 같은 친수성 중합체; 글리신, 글루타민, 아스파라긴, 아르기닌 또는 라이신과 같은 아미노산; 포도당, 만노오스 또는 덱스트린을 포함하는 단당류, 이당류 및 기타 탄수화물; EDTA와 같은 킬레이트 제제; 만니톨 또는 소르비톨과 같은 당 알코올; 나트륨과 같은 염-형성 카운터 이온; 및/또는 TWEEN ™, 폴리에틸렌글리콜 (PEG) 및 PLURONICS™와 같은 비-이온성 계면 활성제.
효과적인 투여에 적합한 약학적으로 허용 가능한 조성물을 제형화하기 위해, 상기 조성물은 본원에 기재된 바와 같은 전달 비히클 또는 상기 융합 단백질 내에 포함된 핵산 구조물인 유효량의 핵산 구조물을 함유할 것이다. 담체는 면역 반응의 유도를 향상시키기 위한 융합 단백질의 커플링에 의한 스캐폴드(scaffold)로서 사용될 수 있다. 상기 담체 단백질은 면역원성 결정 인자를 제시하기에 적합한 임의의 단백질을 포함하는 임의의 통상적인 담체일 수 있다. 적합한 담체는 전형적으로 단백질, 다당류, 폴리락트산, 폴리글리콜산, 중합체성 아미노산, 아미노산 공중합체, 지질 응집체(예를 들면, 오일 방울 또는 리포솜) 및 불활성 바이러스 입자와 같이 전형적으로 크고, 느리게 대사 작용을 하는 거대 분자이다. 이러한 담체는 당업자에게 잘 알려져 있다. 게다가, 이들 담체는 면역 자극제 ("보조제")로서 기능할 수 있다. 동물의 예방 접종은 보조제 및/또는 약제학적 담체로 수행될 수 있다. 통상적인 담체 단백질은 키홀-림펫 헤모시아닌, 트랜스페린, 소 혈청 알부민 또는 인간 혈청 알부민과 같은 혈청 단백질, 오발부민, 면역 글로불린 또는 인슐린과 같은 호르몬을 포함하나 이에 한정되지 않는다. 상기 담체는 보조제와 함께 존재할 수 있다. 백신 조성물은 개체에서 면역 반응을 자극하는 것을 포함하여, 예방 및 치료 용도에 유용하다. 본원에 개시된 상기 백신 조성물은 전신 또는 국소 독성 반응 또는 임의의 다른 부작용을 유발하지 않는다.
특정 면역 반응을 향상시키기 위해 보조제(adjuvants)를 백신 조성물에 포함시킬 수 있다. 따라서, 항원(들)/핵산 작제물 및/또는 전달 비히클(이들 모두는 면역원성 결정 인자로도 지칭 될 수 있음)과 조합 될 때, 강한 특이적 면역 반응을 유도할 수 있는 백신 조성물을 생성하는 보조제를 확인하는 것이 특히 중요하다. 또한 상기 면역원성 결정 인자는 면역화(immunization) 전에 2종 이상의 상이한 보조제와 혼합될 수 있다. 마우스, 랫트 및 토끼와 같은 실험 동물에서 항체 생성을 위해 다수의 보조제가 기술 및 사용되어 왔다. 그러한 환경에서는 주된 목적이 강한 항체 반응을 얻는 것이기 때문에, 부작용에 대한 허용의 정도가 다소 높다. 의약품 사용 및 승인을 위해서, 특히 인간에게 사용하기 위해서는, 보조제를 포함한 백신 조성물의 성분이 잘 특성화되는 것이 요구된다. 또한 상기 조성물은 부작용의 위험을 최소화할 것이 요구된다. 하나의 실시양태에서, 백신 조성물은 보조제를 포함한다. 바람직한 실시양태에서, 상기 백신 조성물은 포유동물, 가장 바람직하게는 인간 개체에게 투여하기에 적합하다. 보조제의 선택은 원하는 면역 반응 유형, B-세포 및/또는 T-세포 활성화를 자극하는 능력에 의해 선택될 수 있으며, 상기 백신 조성물은 관련 림프 조직에 대한 분포 및 제시를 최적화하도록 제조될 수 있다.
리포폴리사카라이드 및 리피드 A를 포함하는 그의 다양한 유도체는 리포좀 또는 기타의 지질 에멀젼과 조합하여 강력한 보조제가 되는 것으로 밝혀졌다. 프로인드 보조제(Freund's Complete Adjuvant)는 대부분의 실험 연구에서 표준이다. 신속한 이화 작용으로부터 항원을 보호하기 위해 면역원성 조성물에 미네랄 오일을 첨가할 수 있다. 면역원성 조성물에서 보조제로서 많은 다른 유형의 물질을 사용할 수 있는데, 사포닌과 같은 식물성 생성물, 키틴과 같은 동물성 생성물 및 수많은 합성 화학 물질이 포함된다.
면역원성 조성물은 완충액과 같은 희석제, 아스코르브산과 같은 항산화제, 저분자량(약 10 잔기 미만) 폴리펩티드, 단백질, 아미노산, 포도당, 수크로스 또는 덱스트린을 포함하는 탄수화물, EDTA와 같은 킬레이트 제, 글루타티온 및 기타 안정화제 및 부형제를 함유할 수 있다. 중성 완충 식염수 또는 비-특이적 혈청 알부민과 혼합된 식염수는 예시적인 적절한 용액이다.
조성물의 pH는 일반적으로 5.0 내지 8.1일 수 있고, 보다 일반적으로 6.0 내지 8.0일 수 있으며, 예를 들어, 6.5 내지 7.5, 또는 7.0 내지 7.8일 수 있다.
상기 조성물은 바람직하게는 무균이다. 상기 조성물은 바람직하게는 비-발열성(non-pyrogenic)이며, 예를 들어, 투여량(dose)당 <1 EU(내독소 단위, 표준 측정치)를 함유하고, 바람직하게는 투여량(dose)당 <0.1 EU를 함유한다. 상기 조성물은 바람직하게는 글루텐이 없다.
4. 투여량(Dosage)
본원에 개시된 백신 조성물은 전형적으로 개체에게 이익을 제공하기에 충분한 양으로 개체에 투여된다. 이 양은 "치료 유효량(therapeutically effective amount)"으로 정의된다. 상기 “치료 유효량”은 특정 조성물의 효과 또는 효능, 투여 기간 또는 빈도, 및 개체의 특정 치료 반응을 포함하는 개체의 크기 및 상태에 의해 결정될 것이다. 게다가, 치료 유효량을 결정할 때, 투여 경로를 고려해야 한다. 백신 조성물의 치료 유효량은 전체 핵산 약 0.1㎍/kg 내지 1mg/kg 범위일 것으로 예상된다. 적절한 용량은 전체 DNA 약 5㎍/kg 내지 500mg/kg, 전체 DNA 10㎍/kg 내지 250㎍/kg 또는 전체 DNA 10㎍/kg 내지 170㎍/kg을 포함한다. 하나의 실시양태에서, 인간 개체(18-50세, 45-75kg)에는 DNA 1.2 mg-7.2 mg이 투여된다. "전체 DNA" 및 “전체 핵산"은 별개의 면역원성 분자를 코딩하는 핵산 풀(pool)을 나타낸다. 예를 들어, 5 개의 상이한 면역원성 분자를 코딩하는 전체 DNA의 50 ㎎의 투여량은 각 분자의 1 ㎎을 가질 수 있다. 상기 백신은 약 2 내지 6회와 같이 여러번 투여될 수 있다. 예시적인 방법에서, DNA 조성물 100 ㎍을 인간 개체에 0, 4 및 12 주(투여 당 100 ㎍)에 투여하였다. 상기 백신 조성물의 치료 유효량은 융합 단백질의 약 0.1㎍/kg 내지 1mg/kg 범위일 것이다. 적합한 투여량은 약 5㎍/kg 내지 500mg/kg의 융합 단백질, 10㎍/kg 내지 250㎍/kg의 융합 단백질 또는 10㎍/kg 내지 170㎍/kg의 융합 단백질을 포함한다. 하나의 실시양태에서, 인간 개체(18-50 세, 45-75 kg)에는 융합 단백질 1.2 mg-7.2 m이 투여된다. 인간 백신은 전형적으로 약 0.5 ml의 투여량으로 투여되지만, 소아에게는 절반 투여량(즉, 약 0.25 ml)이 투여 될 수 있다.
본원에 기재된 치료(treatment)는 다양한 “단위 투여량(unit dose)”을 포함할 수 있다. “단위 투여량”은 본원의 치료 조성물의 지정된-정량(predetermined-quantity)을 함유하는 것으로 정의된다. 투여량 및 특정 경로 및 제형은 임상 분야의 기술 범위 내에 있다. 단위 투여량은 단일 주사(injection)로서 투여될 필요는 없고, 일정 시간 동안 연속적인 주입(infusion)을 포함할 수 있다. 단위 투여량은 적어도 0.01, 0.05, 0.1, 0.5, 1.0, 2.5, 5.0, 10.0, 15.0, 25.0 또는 50.0mg 이상의 상기 활성 성분을 함유할 수 있다. 선택적으로 임의의 단위 투여량은 0.01, 0.05, 0.1, 0.5, 1.0, 2.5, 5.0, 10.0, 15.0, 25.0 또는 50.0 mg 미만의 활성 성분을 함유한다. 적어도 하나의 실시양태에서, 단위 투여량은 약 0.001mg 내지 약 50mg의 활성 성분을 함유한다. 하나 이상의 실시양태에서, 단위 투여량은 약 1mg 내지 약 10mg의 활성 성분을 함유한다.
5. 투여(Administration)
백신 조성물은 치료 유효량으로 개체에게 투여될 수 있다. 유효량은 개체의 상태, 체중, 성별 및 연령과 같은 다양한 요소에 따라 달라질 수 있다. 다른 요인으로는 투여 방법이 포함된다. 약학적 조성물 또는 수의학적 조성물은 피하, 국소, 구강 및 근육 내와 같은 다양한 경로에 의해 개인에게 제공될 수 있다. 약학적 조성물의 투여는 경구 또는 비-경구로 수행된다. 비-경구 전달 방법은 국소, 동맥 내(조직에 직접 투여), 근육내, 피하, 골수내, 척수강내, 심실내, 정맥 주사, 복강내 또는 비강내 투여를 포함한다. 또한, 백신 조성물의 예방 및 치료 방법에 사용하기 위한 적합한 국소용, 경구용, 전신용 및 비-경구용 약제학적 제제가 제공된다.
예를 들어, 상기 백신 조성물은 정제, 캡슐(각각 시한 방출 및 서방성 제형을 포함), 환제, 분말제, 과립제, 엘릭서, 틴크제, 용액제, 현탁제, 시럽제 및 유제와 같은 경구 투여형 또는 주사로 투여될 수 있다. 마찬가지로, 이들은 또한 약학 분야에서 통상의 지식을 가진 자에게 잘 알려진 형태를 사용하여 정맥 내 (볼러스(bolus) 및 주입 모두), 복강 내, 피하, 폐색을 포함하거나 포함하지 않는 국소 또는 근육 내 형태로 투여될 수 있다. 본 발명에 기재된 화합물 중 임의의 것을 포함하는 백신의 유효하지만 비-독성인 양은 예방 또는 치료제로서 사용될 수 있다. 또한, 필요하다면 통상적인 약학적으로 허용 가능한 담체, 희석제, 방부제, 보조제, 완충제 등을 함유하는 동결 건조된 형태 및 용액, 현탁액 또는 에멀젼 형태와 같이 당업계에서 주사 가능한 면역원성 펩타이드 조성물을 제제화하기에 적합한 임의의 및 모든 통상적인 투약 형태가 포함된다.
백신 조성물의 바람직한 투여 방식은, 이에 제한되지는 않으나, 정맥내 또는 피하 투여, 경피 투여, 근육 내 투여, 비강내 투여, 경구 투여, 직장 투여, 질 투여, 폐 투여 및 일반적으로 임의의 점막 투여와 같은 전신적인 투여 방법에 의해 투여 될 수 있다
본원에 기재된 백신은 1 회, 2 회, 3 회, 4 회, 5 회 이상 투여될 수 있다. 백신을 한 번 이상 투여하면 면역 반응이 향상된다. 상기 백신은 이전 투여와 다른 형태로 백신을 투여함으로써 추가적으로 증진 될 수 있다. 상기 추가 접종(booster shot)은 동종 또는 이종 추가 접종이다. 동종 추가 접종은 첫 번째 및 후속 백신이 동일한 작제물, 융합 단백질, 보다 구체적으로 동일한 전달 비히클을 포함하는 것이다. 이종 추가 접종은 동일한 작제물 또는 융합 단백질이 다른 벡터 내에 포함되어 있는 것이다.
백신의 바람직한 수용체는 포유 동물이고, 보다 바람직한 양태에서 포유 동물은 소, 돼지, 말, 양, 염소, 라마, 마우스, 랫트, 원숭이, 개, 고양이 및 인간으로 이루어진 군에서 선택되는 개체이다.
하나의 실시양태에서, 상기 백신 조성물은 제2 활성 성분을 추가로 포함한다. 상기 제2 활성 성분은 항생제, 화학 요법제, 항-알레르기제, 사이토카인, 보체 인자 및 면역계의 동시-자극 분자(co-stimulatory molecules)이다.
6. 치료 및 예방 방법
또한, 본원에 기재된 백신을 개체에 투여하는 것을 포함하여, 개체에서 면역 반응을 유도하는 방법이 기술되어 있다. 면역 반응에는 다음과 같은 유형의 반응이 포함된다: MHC-1 의존성 반응, MHC-1 및/또는 MHC-II 의존성 반응, T 세포 의존성 반응, CD4 T 세포 의존성 반응, CD4+ T 세포 독립적 반응, CD8+ T 세포 의존성 반응 및 B 세포 의존성 면역 반응. 상기 방법은 동물의 유전적 면역화 또는 이를 필요로 하는 개체의 임상적 상태를 치료하기 위해 사용된다.
본 발명에서 기재된 바와 같이, “치료”는 치료학적 치료 및 예방학적 치료를 포함하며, 치료 목적은 표적화된 병리학적 상태 또는 질환을 예방 또는 완화시키는 것이다. 치료가 필요한 개체는 질환을 가지기 쉬운 개체 또는 질환이 예방된 개체들 뿐만 아니라 이미 질환을 가지고 있는 개체들을 포함한다. 상기 용어 '치료요법(theraphy)' '치료학적(therapeutic)', '치료(treatment)' 또는 '치료하는(treating)'은 질병의 증상이나 진행을 감소, 완화 또는 억제 또는 제거하는 능력이나 활성을 포함한다. 치료의 바람직한 효과는 질병의 발생 또는 재발을 예방, 증상 완화, 질병의 직접 또는 간접적인 병적 결과의 감소, 전이 예방, 질병 진행률 감소, 질병 상태의 개선 또는 완화, 및 차도 또는 개선된 예후를 포함한다. 일부 실시양태에서, 본원의 방법 및 조성물은 질환 또는 질병의 발생을 지연시키거나 질환 또는 질병의 진행을 늦추는데 사용된다.
본 발명에 따른 치료는 본 발명의 펩타이드, 핵산, 항체 조성물을 치료가 필요한 환자에게 투여하는 것을 포함하는 암 또는 다른 종양성 질환(neoplastic disorder)을 치료하는 방법을 포함할 수 있다. 적어도 하나의 실시양태에서, 상기 치료는 전구 약물(prodrug) 형태의 약물과 같은 화학 요법 약물을 환자에게 투여하는 것을 추가로 포함한다. 상기 두 성분은 함께, 예를 들어 결합된 알약의 형태, 또는 개별적으로 투여될 수 있다. 투여는 순차적 또는 동시적일 수 있다. “순차적인 투여(Sequential administration)” 투여는 상기 성분들이 다른 시간 또는 시점에 투여되는 것을 나타내는 것이며 서로 중복될 수도 있다. 동시 투여는 상기 성분들이 동시에 투여되는 것을 나타낸다.
유효량 또는 바람직하게는 본 발명의 치료의 치료학적인 유효량이 투여된다. "유효량"은 요구되는 치료 또는 예방 결과를 달성하는데 필요한 용량 및 투여 기간에서 유효한 양을 의미한다. 상기 유효량은 치료제가 병용 투여되는 약물 또는 전구 약물에 따라 다를 수 있다. 본 발명의 치료의 "치료학적 유효량"은 요구하는 치료 결과를 이끌어 내기 위해서는 환자의 질환 상태, 연령, 성별 및 체중 및 단백질의 능력과 같은 요인에 따라 달라질 수 있다. 치료학적 유효량은 치료학적으로 유익한 효과룰 나타내는 양이 단백질의 임의의 독성 또는 유해한 효과를 나타내는 양보다 많은 경우를 포함한다. 또한 치료학적 유효량은 효능, 예를 들어 임상적 효능을 부여하기에 충분한 양을 포함한다.
또한 본 발명은 본 발명의 조성물의 유효량을 투여하는 단계를 포함하며, 포유동물에서 면역 반응을 일으키는 방법을 제공한다. 상기 면역 반응은 바람직하게는 보호성(protective) 면역 반응이고, 바람직하게는 항체 및/또는 세포-매개된 면역을 포함한다. 상기 방법은 부스터 반응을 일으킬 수 있다.
또한 본 발명은 약물로서 사용하기 위한, 예를 들어, 포유동물에서 면역 반응을 일으키는 데 사용하기 위한 본 발명의 폴리펩티드를 제공한다.
또한 본 발명은 포유동물에서 면역 반응을 일으키는 약물의 제조에 있어서 본 발명의 폴리펩티드의 용도를 제공한다.
또한 본 발명은 본 발명의 면역원성 조성물로 미리 충전된 전달 장치를 제공한다.
상기한 용도 및 방법에 의해 포유 동물에서 면역 반응을 일으킴으로써, 포유동물은 HIV, 대상포진 및 헤르페스(herpes)를 포함하는 잠복성 바이러스 감염으로부터 보호될 수 있다.
또한 대장균 질병이 이들 종에서 문제가 있기 때문에, 포유 동물은 바람직하게는 인간이지만, 예를 들어, 소, 돼지, 닭, 고양이 또는 개일 수 있다. 상기 백신이 예방 용도로 사용되는 경우, 인간은 바람직하게는 어린이 (예 : 유아(toddler) 또는 영아(infant)) 또는 10대이다: 백신이 치료 용도로 사용되는 경우, 인간은 바람직하게는 10대 또는 성인일 수 있다. 예를 들어 안전성, 투여량, 면역원성 등을 평가하기 위해 어린이를 대상으로 한 백신을 성인에게 투여 할 수 있다. 본 발명의 백신은 어린이 및 성인 모두를 치료하는데 사용될 수 있다. 따라서 인간 환자는 1세 미만, 1-5세, 5-15세, 15-55세 또는 55세 이상일 수 있다. 바람직하게는 백신 접종을 받는 환자는 노인(예: 50세 이상, 60세 이상, 및 바람직하게 65세 이상), 청년(예: 5세 이하), 입원 환자, 의료 종사자, 군 복무자 및 군인, 임산부, 만성 질환자 또는 면역 결핍 환자이다. 그러나 상기 백신은 이 그룹에만 적합한 것은 아니고, 인구 집단에서보다 일반적으로 사용될 수 있다.
치료학적 치료의 효능을 확인하는 한 가지 방법은 본 발명의 조성물을 투여 한 후 대장균 감염을 모니터링 하는 것을 포함한다. 예방적 치료의 효능을 확인하는 한 가지 방법은 상기 조성물을 투여한 후, 본 발명의 조성물에서 항원에 대하여 전신(예: IgG1 및 IgG2a 생산 수준의 모니터링) 및/또는 점막(예: IgA 생산 수준의 모니터링) 면역 반응을 모니터링하는 것을 포함한다. 전형적으로, 항원-특이적인 혈청 항체 반응은 챌린지 전(pre-challenge)이 아닌 면역화 후(post-immunisation)에 결정되는 반면, 항원-특이적 점막 항체 반응은 면역화 후 및 챌린지 후(post-challenge)에 결정된다.
본 발명의 조성물의 면역원성을 평가하는 다른 방법은 면역블롯 및/또는 마이크로 어레이에 의해 환자의 혈청 또는 점막 분비물을 스크리닝하기 위해 단백질을 재조합적으로 발현하는 것이다. 상기 단백질과 환자 샘플 사이의 양성 반응은, 환자가 문제의 단백질에 면역 반응을 발생시킨다는 것을 나타낸다. 또한 이 방법은 면역우성 항원 및/또는 항원 내 항원 결정기를 동정하는데 사용될 수 있다.
또한, 본원에서는 알파 바이러스 표면 막 당 단백질로 처리함으로써 인간 T 세포의 성장을 자극하는 방법이 기재되어있다.
또한, 본원에서는 알파 바이러스 표면 막 당 단백질로 처리함으로써 인간 조혈 세포(T 세포, NK 세포, B 세포, 수지상 세포, 조절 T 세포, 대식세포, 적혈구 및 모든 다른 것들을 포함)를 활성화시키는 방법이 기재되어있다.
또한, 본원에서는 알파 바이러스 표면 막 당 단백질로 처리함으로써 아네르기(anergy)로부터 T 세포를 방출하는 방법이 기재되어있다.
또한, 본원에서는 알파 바이러스 표면 막 당 단백질로 처리함으로써 T 세포의 중단점 억제(Breakpoint Inhibition)를 극복하는 방법이 기재되어있다.
또한, 본원에서는 알파 바이러스 표면 막 당 단백질로 처리함으로써 암을 치료하는 방법이 기재되어있다.
6.1. 병용 요법
특정 실시양태에서, 상기한 융합 단백질은 적어도 하나의 다른 치료제와 병용 요법으로 사용될 수 있다. 상기 융합 단백질 및 치료제는 부가적(additively) 또는 보다 바람직하게는 상승적(synergistically)으로 작용할 수 있다. 바람직한 실시양태에서, 융합 단백질을 포함하는 조성물은 다른 치료제의 투여와 동시에 투여되는데, 여기서 다른 치료제는 융합 단백질과 동일한 조성물의 일부이거나 상이한 조성물의 일부일 수 있다. 다른 실시양태에서, 융합 단백질을 포함하는 조성물은 다른 치료제의 투여 전 또는 투여 후에 투여된다. 융합 단백질이 치료에 유용한 많은 질환이 만성 질환이기 때문에, 특정 실시양태에서 병용 요법은 융합 단백질을 포함하는 조성물과 다른 치료제, 예를 들어, 특정 약물과 관련된 독성을 최소화할 수 있는 치료제를 포함하는 조성물을 교대로 투여하는 것을 포함한다. 각 약물 또는 치료제의 투여 기간은 예를 들어, 1 개월, 3 개월, 6 개월 또는 1 년일 수 있다. 특정 실시양태에서, 융합 단백질이 잠재적으로 부작용(비-제한적인 예를 들어, 독성)을 일으키는 또 다른 치료제와 동시에 투여되는 경우, 상기 치료제는 불리한 측면이 유도되는 한계치 이하로 유리하게 투여 될 수 있다 .
특정 실시양태에서, 상기 융합 단백질은 체크 포인트(check point) 치료법 또는 화학 요법과 함께 투여된다. 특정 실시양태에서, 상기 융합 단백질은 CTLA4, PD1 또는 PDL1에 대한 항체와 함께 투여된다.
본 발명의 융합 단백질은 방사선 조사(irridiation) 또는 하나 이상의 화학 치료제와 함께 투여될 수 있다. 방사선 치료의 경우, 상기 방사선 조사는 감마선 또는 엑스레이가 될 수 있다. 방사선 요법의 일반적인 개요를 보려면, Hellman, Chapter 12: Principles of Radiation Therapy Cancer, in: Principles and Practice of Oncology, DeVita et al., eds., 2.nd. Ed., J.B. Lippencott Company, Philadelphia를 참조한다. 유용한 화학 요법 제에는 메토트렉세이트(methotrexate), 탁솔(taxol), 메르캅토퓨린(mercaptopurine), 티오구아닌(thioguanine), 히드록시우레아(hydroxyurea), 시타라빈(cytarabine), 사이클로포스파마이드(cyclophosphamide), 이포스파마이드(ifosfamide), 니트로소요소(nitrosoureas), 시스플라틴(cisplatin), 카보 플라틴(carboplatin), 미토마이신(mitomycin), 다카르바진(dacarbazine), 프로카비진(procarbizine), 에토포시드(etoposides), 캄파테신(campathecins), 블레오마이신(bleomycin), 독소루비신(doxorubicin), 이다루비신(idarubicin), 다우노루비신(daunorubicin), 닥티노마이신(dactinomycin), 플리카마이신(plicamycin), 미톡산트론(mitoxantrone), 아스파라기네이즈(asparaginase), 빈블라스틴(vinblastine), 빈크리스틴(vincristine), 비노렐빈(vinorelbine), 파클리탁셀(paclitaxel) 및 도세탁셀 (docetaxel)이 포함된다. 특정 실시양태에서, 상기한 융합 단백질을 포함하는 조성물은 하나 이상의 화학 요법제를 추가로 포함하고/하거나 방사선 요법과 동시에 투여된다. 또 다른 특정 실시양태에서, 화학 요법 또는 방사선 요법은 본 조성물의 투여 전 또는 투여 후에 투여되며, 바람직하게는 적어도 1 시간, 5 시간, 12 시간, 1 일, 1 주, 1 개월, 보다 바람직하게는 수개월(예를 들어, 3 개월내)에 투여 될 수 있다.
암과 같은 질환의 예방, 치료 및/또는 관리를 위해 유용하거나, 사용되어 왔거나 현재 사용되고 있는 임의의 치료제(예를 들어, 치료 또는 예방 제제)는, 본 발명의 조성물 및 방법에 사용될 수 있다. 임의의 치료제(예를 들어, 치료제 또는 예방제)는 이에 제한되지는 않으나, 펩티드, 폴리펩티드, 접합체, 핵산 분자, 소형 분자, 모방 제제, 합성 약물, 무기 분자 및 유기 분자를 포함한다. 암 치료법의 비-제한적인 예는 화학 요법, 방사선 요법, 호르몬 요법 및/또는 생물학적 요법/면역 요법 및 수술을 포함한다. 특정 실시 양태에서, 본 발명의 예방적 및/또는 치료학적 유효 처방은 치료제의 혼합물의 투여를 포함한다.
암 치료제의 예는 다음을 포함하나 이에 제한되지 않는다: 아시비신(acivicin); 아클라루비신(aclarubicin); 아코다졸 염산염(acodazole hydrochloride); 아크로닌(acronine); 아도제레신(adozelesin); 알데스류킨(aldesleukin); 알트레타민(altretamine); 엠보마이신(ambomycin); 아메탄트론 아세테이트(ametantrone acetate); 아미노글루테치미드(aminoglutethimide); 암사크린(amsacrine); 아나스트로졸(anastrozole); 안트라마이신(anthramycin); 아스파라기네이즈(asparaginase); 아스펠린(asperlin); 아카시티딘(azacitidine); 아제테파(azetepa); 아조토마이신(azotomycin); 바티마스타트(batimastat); 벤조데파(benzodepa); 비칼루타미드(bicalutamide); 비산트렌 염산염(bisantrene hydrochloride); 비스나파이드 다이메실레이트(bisnafide dimesylate); 비스포스포네이트(bisphosphonates; 예를 들어, 파미드로네이트(pamidronate; Aredria), 나트륨 클론드로네이트(sodium clondronate; Bonefos), 졸레드로닉 산(zoledronic acid; Zometa), 알렌드로네이트(alendronate; Fosamax), 에티드로네이트(etidronate), 이반도르네이트(ibandornate), 시마드로네이트(cimadronate), 리세드로메이트(risedromate), 및 틸루드로메이트(tiludromate)); 비젤레신(bizelesin); 블레오마이신 설페이트(bleomycin sulfate); 염화브레퀴날(brequinar sodium); 브로피리민(bropirimine); 부설판(busulfan); 카티노마이신(cactinomycin); 카루스테론(calusterone); 카라세미드(caracemide); 카르베티머(carbetimer); 카보플라틴(carboplatin); 카르무스틴(carmustine); 카루비신 염산염(carubicin hydrochloride); 카제레신(carzelesin); 세데핀골(cedefingol); 클로람부실(chlorambucil); 시로레마이신(cirolemycin); 시스플라틴(cisplatin); 클라드리빈(cladribine); 크리스나톨 메실레이트(crisnatol mesylate); 시클로포스파미드(cyclophosphamide); 시타라빈(cytarabine); 다카바진(dacarbazine); 닥티노마이신(dactinomycin); 다우노루비신 염산염(daunorubicin hydrochloride); 데시타빈(decitabine); 덱소마플라틴(dexormaplatin); 데자구아닌(dezaguanine); 데자구아닌 메실레이트(dezaguanine mesylate); 디아지퀴온(diaziquone); 도세탁셀(docetaxel); 독소루비신(doxorubicin); 독소루비신 염산염(doxorubicin hydrochloride); 드로록시펜(droloxifene); 드로록시펜 시트레이트(droloxifene citrate); 드로모스타놀론 프로피오네이트(dromostanolone propionate); 두아조마이신(duazomycin); 에다트렉세이트(edatrexate); 에프로니신 염산염(eflornithine hydrochloride); EphA2 저해제; 엘사미트루신(elsamitrucin); 엔로플라틴(enloplatin); 엔프로메이트(enpromate); 에피프로피딘(epipropidine); 에피루비신 염산염(epirubicin hydrochloride); 에부로졸(erbulozole); 에소루비신 염산염(esorubicin hydrochloride); 에스트라무스틴(estramustine); 에스트라무스틴 인산나트륨염(estramustine phosphate sodium); 에타니다졸(etanidazole); 에토포시드(etoposide); 에토포시드 포스페이트(etoposide phosphate); 에토프린(etoprine); 파드로졸 염산염(fadrozole hydrochloride); 파자라빈(fazarabine); 펜레티니드(fenretinide); 플록슈리딘(floxuridine); 플루다라빈 포스페이트(fludarabine phosphate); 플루오로우라실(fluorouracil); 플루오로시타빈(fluorocitabine); 포스퀴돈(fosquidone); 포스트리에신나트륨(fostriecin sodium); 젬시타빈(gemcitabine); 젬시타빈 염산염(gemcitabine hydrochloride); 히이드록시우레아(hydroxyurea); 아이다루비신 염산염(idarubicin hydrochloride); 아이포스파미드(ifosfamide); 일모포신(ilmofosine); 인터루킨(interleukin) II(재조함 인터루킨 II, 또는 rIL2를 포함), 인터페론 알파(interferon alpha)-2a; 인터페론 알파-2b; 인터페론 알파-n1; 인터페론 알파-n3; 인터페론 베타-I a; 인터페론 감마-I b; 이프로플라틴(iproplatin); 이리노테칸 염산염(irinotecan hydrochloride); 란레오타이드 아세테이트(lanreotide acetate); 레트로졸(letrozole); 류프로라이드 아세테이트(leuprolide acetate); 리아로졸 염산염(liarozole hydrochloride); 로메트렉솔나트륨(lometrexol sodium); 로무스틴(lomustine); 로소크산트론 염산염(losoxantrone hydrochloride); 마소프로콜(masoprocol); 마이탄신(maytansine); 메클로레타민 염산염(mechlorethamine hydrochloride); 항-CD2 항체; 메제스트롤 아세테이트(megestrol acetate); 메렌제스트롤 아세테이트(melengestrol acetate); 멜파란(melphalan); 메노가릴(menogaril); 머캅토퓨린(mercaptopurine); 메토트렉세이트(methotrexate); 메토트렉세이트 나트륨(methotrexate sodium); 메토프린(metoprine); 메투레데파(meturedepa); 마이틴도마이드(mitindomide); 마이토칼신(mitocarcin); 마이토크로민(mitocromin); 마이토질린(mitogillin); 마이토말신(mitomalcin); 마이토마이신(mitomycin); 마이토스퍼(mitosper); 마이토탄(mitotane); 마이톡산트론염산염(mitoxantrone hydrochloride); 미코페놀산(mycophenolic acid); 노코다졸(nocodazole); 노갈라마이신(nogalamycin); 오르마플라틴(ormaplatin); 옥시슈란(oxisuran); 파클리탁셀(paclitaxel); 페가스파가제(pegaspargase); 페리오마이신(peliomycin); 펜타무스틴(pentamustine); 페플로마이신 황산염(peplomycin sulfate); 페르포스파마이드(perfosfamide); 피포브로만(pipobroman); 피포술판(piposulfan); 피록산트론 염산염(piroxantrone hydrochloride); 플리카마이신(plicamycin); 플로메스탄(plomestane); 포르피머나트륨(porfimer sodium); 포르피로마이신(porfiromycin); 프레드니무스틴(prednimustine); 프로카바진 염산염(procarbazine hydrochloride); 퓨로마이신(puromycin); 퓨로마이신 염산염(puromycin hydrochloride); 피라조퓨린(pyrazofurin); 리보프린(riboprine); 로글레티마이드(rogletimide); 사핑골(safingol); 사핑골 염산염(safingol hydrochloride); 세무스틴(semustine); 심트라젠(simtrazene); 스파르포세이트 나트륨(sparfosate sodium); 스파르소마이신(sparsomycin); 스피로게르마늄 염산염(spirogermanium hydrochloride); 스피로무스틴(spiromustine); 스피로플라틴(spiroplatin); 스트렙토니그린(streptonigrin); 스트렙토조신(streptozocin); 수로페눌(sulofenur); 탈리소마이신(talisomycin); 테코갈란 나트륨(tecogalan sodium); 테가푸르(tegafur); 테록산트론 염산염(teloxantrone hydrochloride); 테모포르핀(temoporfin); 테니포사이드(teniposide); 테록시론(teroxirone); 테스토락톤(testolactone); 티아미프린(thiamiprine); 티오구아닌(thioguanine); 티오테파(thiotepa); 티아조푸린(tiazofurin); 티라파자민(tirapazamine); 토레미펜 시트레이트(toremifene citrate); 트레스토론 아세테이트(trestolone acetate); 트리시리빈 포스페이트(triciribine phosphate); 트라이메트렉세이트(trimetrexate); 트라이메트렉세이트 글루쿠로네이트(trimetrexate glucuronate); 트립토렐린(triptorelin); 투부로졸 염산염(tubulozole hydrochloride); 우라실 머스타드(uracil mustard); 우레데파(uredepa); 바프레오티드(vapreotide); 베르테포르핀(verteporfin); 빈블라스틴 설페이트(vinblastine sulfate); 빈크리스틴 설페치트(vincristine sulfate); 빈데신(vindesine); 빈데신 설페이트(vindesine sulfate); 비네피딘 설페이트(vinepidine sulfate); 빈글리시네이트 설페이트(vinglycinate sulfate); 빈류로신 설페이트(vinleurosine sulfate); 비노렐빈 타르트레이트(vinorelbine tartrate); 빈로시딘 설페이트(vinrosidine sulfate); 빈졸리딘 설페이트(vinzolidine sulfate); 보로졸(vorozole); 제니플라틴(zeniplatin); 지노스타틴(zinostatin); 조루비신 염산염(zorubicin hydrochloride).
암 치료제의 다른 예는 다음을 포함하나 이에 제한되지 않는다: 20-에피-1,25(20-epi-1,25) 디하이드록시비타민 D3(dihydroxyvitamin D3); 5-에티닐우라실(5-ethynyluracil); 아비레이트론(abiraterone); 아클라루비신(aclarubicin); 아실풀베네(acylfulvene); 아데시페놀(adecypenol); 아도제레신(adozelesin); 알데스류킨(aldesleukin); ALL-TK 길항제(antagonists); 알트레타민(altretamine); 엠바무스틴(ambamustine); 아미독스(amidox); 아미포스틴(amifostine); 아미노레불린산(aminolevulinic acid); 암루비신(amrubicin); 암사크린(amsacrine); 아나그렐리드(anagrelide); 아나스트로졸(anastrozole); 안드로그라폴라이드(andrographolide); 혈관신생 억제제(angiogenesis inhibitors); 길항제 D(antagonist D); 길항제 G; 안타렐릭스(antarelix); 항-배위 형성 단백질-1(anti-dorsalizing morphogenetic protein-1); 항안드로겐(antiandrogen), 전립선암(prostatic carcinoma); 항에스트로겐(antiestrogen); 항네오플라스톤(antineoplaston); 안티센스 올리고뉴클레오티드(antisense oligonucleotides); 아피디콜린 글리시네이트(aphidicolin glycinate); 세포 사멸 유전자 조절체(apoptosis gene modulators); 세포 사멸 조절제(apoptosis regulators); 아퓨린산(apurinic acid); 아라-CDP-DL-PTBA(ara-CDP-DL-PTBA); 아르기닌 디아미나제(arginine deaminase); 아술라크린(asulacrine); 아타메스탄(atamestane); 아트리무스틴(atrimustine); 악시나스타틴 1(axinastatin 1); 악시나스타틴 2(axinastatin 2); 악시나스타틴 3(axinastatin 3); 아자세트론(azasetron); 아자톡신(azatoxin); 아자티로신(azatyrosine); 바카틴 III 유도체(baccatin III derivatives); 발라놀(balanol); 바티마스타트(batimastat); Bcl-2 저해제; ABT-737을 포함하는 Bcl-2 패밀리(family) 저해제; BCR/ABL 길항제; 벤조콜린(benzochlorins); 벤조일스타우로스포린(benzoylstaurosporine); 베타 락탐 유도체(beta lactam derivatives); 베타-알레틴(beta-alethine); 베타클라마이신 B(betaclamycin B); 베툴린산(betulinic acid); bFGF 저해제; 바이칼루타마이드(bicalutamide); 비산트렌(bisantrene); 비사지리디닐스퍼민(bisaziridinylspermine); 비스나파이드(bisnafide); 비스트라텐 A(bistratene A); 비젤레신(bizelesin); 브리플레이트(breflate); 브로피리민(bropirimine); 부도티탄(budotitane); 부티오닌 설폭시민(buthionine sulfoximine); 칼시포트리올(calcipotriol); 칼포스틴 C(calphostin C); 캄프토테신 유도체(camptothecin derivatives); 카나리폭스(canarypox) IL-2; 카페시타바인(capecitabine); 카르복사마이드-아미노-트리아졸(carboxamide-amino-triazole); 카르복시아미도트리아졸(carboxyamidotriazole); 카레스트 M3(CaRest M3); CARN 700; 연골 분화 저해제(cartilage derived inhibitor); 카르제레신(carzelesin); 카제인 키나아제 저해제(casein kinase inhibitors, ICOS); 카스타노스퍼민(castanospermine); 세트로핀 B(cecropin B); 세트로레릭스(cetrorelix); 클로린(chlorlns); 클로로퀴녹살린 설폰아마이드(chloroquinoxaline sulfonamide); 시카르포스트(cicaprost); 시스-포르피린(cis-porphyrin); 클라드리빈(cladribine); 크클로미펜 아날로그(clomifene analogues); 클로트리마졸(clotrimazole); 콜리스마이신 A(collismycin A); 콜리스마이신 B; 콤브레스타틴 A4(combretastatin A4); 콤브레스타틴 아날로그(combretastatin analogue); 코나제닌(conagenin); 크램베스시딘 816(crambescidin 816); 크리스나톨(crisnatol); 크리토피신 8(cryptophycin 8); 크리토피신 A 유도체(cryptophycin A derivatives); 쿠라신 A(curacin A); 사이클로펜탄트라퀴논(cyclopentanthraquinones); 사이클로플라탐(cycloplatam); 사이페마이신(cypemycin); 사이타라바인 옥포스페이트(cytarabine ocfosfate); 사이톨릭 요인(cytolytic factor); 사이토스타틴(cytostatin); 다클릭시맙(dacliximab); 데시타빈(decitabine); 디하이드로디데민 B(dehydrodidemnin B); 데스로레린(deslorelin); 덱사메타손(dexamethasone); 덱시포스파마이드(dexifosfamide); 덱스라족산(dexrazoxane); 덱스베라파밀(dexverapamil); 디아지쿠온(diaziquone); 디데민 B(didemnin B); 디독스(didox); 디에틸노르스퍼민(diethylnorspermine); 디하이드로-5-아자시티딘(dihydro-5-azacytidine); 디하이드로탁솔(dihydrotaxol), 디옥사마이신(dioxamycin); 디페닐 스피로무스틴(diphenyl spiromustine); 도세탁셀(docetaxel); 도코사놀(docosanol); 도라세트론(dolasetron); 독시플루리딘(doxifluridine); 드로록시펜(droloxifene); 드로나비놀(dronabinol); 두오카르마이신 SA(duocarmycin SA); 엡셀렌(ebselen); 에코무스틴(ecomustine); 에델포신(edelfosine); 에드레콜로맙(edrecolomab); 에플로르니틴(eflornithine); 엘레민(elemene); 에미테푸르(emitefur); 에피루비신(epirubicin); 에프리스테라이드(epristeride); 에스트라무스틴 아날로그(estramustine analogue); 에스트로겐 작용제(estrogen agonists); 에스트로겐 길항제(estrogen antagonists); 에타니다졸(etanidazole); 에토포시드 포스페이트(etoposide phosphate); 엑세메스탄(exemestane); 파드로졸(fadrozole); 파자라빈(fazarabine); 펜레티나이드(fenretinide); 필그람스팀(filgrastim); 피나스테라이드(finasteride); 플라보피리돌(flavopiridol); 플레제라스틴(flezelastine); 플루아스테론(fluasterone); 플루다라빈(fludarabine); 플루오로다우노루니신 염산염(fluorodaunorunicin hydrochloride); 포르페니멕스(forfenimex); 포르메스탄(formestane); 포스트리에신(fostriecin); 포테무스틴(fotemustine); 가돌리늄 텍사피린(gadolinium texaphyrin); 갈리움 니트레이트(gallium nitrate); 갈로시타빈(galocitabine); 가니레릭스(ganirelix); 젤라티네이즈 저해제(gelatinase inhibitors); 젬시타빈(gemcitabine); 글루타티온 저해제(glutathione inhibitors); HMG CoA 리덕테이즈 억제제(reductase inhibitors; 예를 들어, 아트로바스타틴(atorvastatin), 세리바스타틴(cerivastatin), 플루바스타틴(fluvastatin), 레스콜(lescol), 루피터(lupitor), 로바스타틴(lovastatin), 로수바스타틴(rosuvastatin), 및 심바스타틴(simvastatin)); 헵술팜(hepsulfam); 헤레구린(heregulin); 헥사메틸렌 비스아세타마이드(hexamethylene bisacetamide); 하이퍼리신(hypericin); 이반드론산(ibandronic acid); 이다루비신(idarubicin); 이독시펜(idoxifene); 이드라만톤(idramantone); 일모포신(ilmofosine); 이로마스타트(ilomastat); 이미다조아크리돈(imidazoacridones); 이미퀴모드(imiquimod); 면역반응촉진 펩티드(immunostimulant peptides); 인슐린-유사 성장 인자-1 수용체 저해제(insulin-like growth factor-1 receptor inhibitor); 인터페론 작용제(interferon agonists); 인터페론(interferons); 인터루킨(interleukins); 이오벤구안(iobenguane); 이오도독소루비신(iododoxorubicin); 이포메아놀, 4-이로플락트(ipomeanol, 4-iroplact); 이르소글라딘(irsogladine); 이소벤가졸(isobengazole); 이소호모할리콘드린 B(isohomohalicondrin B); 이타세트론(itasetron); 자스플라키놀라이드(jasplakinolide); 카하라라이드 F(kahalalide F); 라멜라린-N 트리아세테이트(lamellarin-N triacetate); 란레오타이드(lanreotide); 레이나마이신(leinamycin); 레노그라스팀(lenograstim); 렌티난 설페이트(lentinan sulfate); 렙톨스타틴(leptolstatin); 레트로졸(letrozole); 백혈병 저해 인자(leukemia inhibiting factor); 백혈구 알파 인터페론(leukocyte alpha interferon); 레오프롤라이드+에스트로겐+프로게스테론(leuprolide+estrogen+progesterone); 류프로레린(leuprorelin); 레바미솔(levamisole); LFA-3TIP; 리아로졸(liarozole); 선형 폴리아민 아날로그(linear polyamine analogue); 리포필릭 디사카라이드 펩티드(lipophilic disaccharide peptide); 리포필릭 플라티넘 혼합물(lipophilic platinum compounds); 리소클리나마이드 7(lissoclinamide 7); 로바플라틴(lobaplatin); 롬브리신(lombricine); 로메트렉솔(lometrexol); 로니다민(lonidamine); 로속산트론(losoxantrone); 로바스타틴(lovastatin); 록소루비신(loxoribine); 루르토테칸(lurtotecan); 루테티움 텍사피린(lutetium texaphyrin); 리소필린(lysofylline); 용해 펩티드(lytic peptides); 마이탄신(maitansine); 만노스타틴 A(mannostatin A); 마리마스타트(marimastat); 마소프로콜(masoprocol); 마스핀(maspin); 마트릴리신 저해제(matrilysin inhibitors); 기질 메탈로프로테이나제 저해제(matrix metalloproteinase inhibitors); 메노가릴(menogaril); 멀바론(merbarone); 메테렐린(meterelin); 메티오니나제(methioninase); 메토클로프라미드(metoclopramide); MIF 저해제; 미페프리스톤(mifepristone); 밀테포신(miltefosine); 미리모스팀(mirimostim); 미스매치드 이중 가닥 RNA(mismatched double stranded RNA); 미토구아존(mitoguazone); 미토락톨(mitolactol); 미토마이신 아날로그(mitomycin analogues); 미토나파이드(mitonafide); 미토톡신 섬유아세포 성장 인자-사포린(mitotoxin fibroblast growth factor-saporin); 미톡산트론(mitoxantrone); 모파로텐(mofarotene); 몰그라모스팀(molgramostim); 모노클로날 항체(monoclonal antibody), 인간 융모성 성선 자극호르몬(human chorionic gonadotrophin); 모노포스포릴 리피드 A+미오박테리아 세포 벽 sk(monophosphoryl lipid A+myobacterium cell wall sk); 모피다몰(mopidamol); 다중 의약 내성 유전자 저해제(multiple drug resistance gene inhibitor); 다중 종양 억제 1-기반 치료제(multiple tumor suppressor 1-based therapy); 머스타드 항암제(mustard anticancer agent); 마이카페록사이드 B(mycaperoxide B); 마이코박테리아 세포벽 추출물(mycobacterial cell wall extract); 마이리아포론(myriaporone); N-아세틸디날린(N-acetyldinaline); N-서브스티튜티드 벤자마이드(N-substituted benzamides); 나파렐린(nafarelin); 나그레스팁(nagrestip); 날록손+펜타조신(naloxone+pentazocine); 나파빈(napavin); 나프테르핀(naphterpin); 나르토그라스팀(nartograstim); 네다플라틴(nedaplatin); 네모루비신(nemorubicin); 네리드로닉산(neridronic acid); 천연 엔도펩티다아제(neutral endopeptidase); 닐루타마이드(nilutamide); 니사마이신(nisamycin); 니트릭 옥사이드 조절제(nitric oxide modulators); 니트록사이드 안티옥시던트(nitroxide antioxidant); 니트룰린(nitrullyn); 06-벤질구아닌(O6-benzylguanine); 옥트레오타이드(octreotide); 우키세논(okicenone); 올리고뉴클레오티드(oligonucleotides); 온아프리스톤(onapristone); 온단세트론(ondansetron); 온단세트론; 오라신(oracin); 오랄 사이토카인 유도제(oral cytokine inducer); 오르마플라틴(ormaplatin); 오사테론(osaterone); 옥사리플라틴(oxaliplatin); 옥사우노마이신(oxaunomycin); 파클리탁셀(paclitaxel); 파클리탁셀 아날로그(paclitaxel analogues); 파클리탁셀 유도체(paclitaxel derivatives); 팔라우아민(palauamine); 팔미토일리족신(palmitoylrhizoxin); 파미드로닉산(pamidronic acid); 파낙시트리올(panaxytriol); 파노미펜(panomifene); 파라박틴(parabactin); 파젤립틴(pazelliptine); 페가스파르가제(pegaspargase); 펠데신(peldesine); 펜도산 폴리설페이트 나트륨(pentosan polysulfate sodium); 펜토스타틴(pentostatin); 펜트로졸(pentrozole); 페르플루브론(perflubron); 페르포스파마이드(perfosfamide); 페릴릴 알코올(perillyl alcohol); 페나지노마이신(phenazinomycin); 페닐아세테이트(phenylacetate); 포스파테이즈 저해제(phosphatase inhibitors); 피시바닐(picibanil); 필로카르핀 염산염(pilocarpine hydrochloride); 피라루비신(pirarubicin); 피리드렉심(piritrexim); 플라세틴 A(placetin A); 플라세틴 B; 플라스미노젠 활성화제 저해제(plasminogen activator inhibitor); 플라니텀 복합체(platinum complex); 플라티넘 혼합물(platinum compounds); 플라티넘-트리아민 복합체(platinum-triamine complex); 포르피머 나트륨(porfimer sodium); 포르피로마이신(porfiromycin); 프레드니손(prednisone); 프로필 비스-아크리돈(propyl bis-acridone); 프로스타글란딘(prostaglandin) J2; 프로테아좀 저해제(proteasome inhibitors); 단백질 A-비드 면역 조절제(protein A-based immune modulator); 단백질 키나아제 C 저해제(protein kinase C inhibitor); 단백질 키나아제 C 저해제(protein kinase C inhibitors), 마이크로알겔(microalgal); 단백질 티로신 포스페이트 저해제(protein tyrosine phosphatase inhibitors); 퓨린 뉴클레오사이드 포스포릴라아제 저해제(purine nucleoside phosphorylase inhibitors); 푸르퓨린(purpurins); 피라졸로아크리딘(pyrazoloacridine); 피리독실레이티드 헤모글로빈 폴리옥세틸렌 컨쥬게이트(pyridoxylated hemoglobin polyoxyethylene conjugate); 래프 길항제(raf antagonists); 랠시트렉시드(raltitrexed); 라모세트론(ramosetron); 라스 파르네실 단백질 트렌스퍼라아제 저해제(ras farnesyl protein transferase inhibitors); 라스 저해제(ras inhibitors); 라스-GAP 저해제(ras-GAP inhibitor); 레텔립틴 디메틸레이티드(retelliptine demethylated); 레늄 Re 186 에티드로네이트(rhenium Re 186 etidronate); 리족신(rhizoxin); 리보자임(ribozymes); RII 레티나마이드(RII retinamide); 로글레티마이드(rogletimide); 로히투킨(rohitukine); 로무르타이드(romurtide); 로퀴니멕스(roquinimex); 루비기논 B1(rubiginone B1); 루복실(ruboxyl); 사핑골(safingol); 사인토핀(saintopin); SarCNU; 사르코피톨 A(sarcophytol A); 사르그라모스팀(sargramostim); Sdi 1 미메틱(mimetics); 세무스틴(semustine); 세네신 유도 저해제 1(senescence derived inhibitor 1); 센스 올리고노클레오티드(sense oligonucleotides); 신호 트랜스덕션 저해제(signal transduction inhibitors); 신호 트랜스덕션 조절제(signal transduction modulators); 단일 사슬 항원 결합 단백질(single chain antigen binding protein); 시조푸란(sizofuran); 소부족산(sobuzoxane); 나트륨 보로캅테이트(sodium borocaptate); 나트륨 페닐아세테이트(sodium phenylacetate); 솔베롤(solverol); 소마토메딘 바인딩 단백질(somatomedin binding protein); 소네르민(sonermin); 스파르포식 산(sparfosic acid); 스피카마이신 D(spicamycin D); 스피로무스틴(spiromustine); 스플레노펜틴(splenopentin); 스폰지스타틴 1(spongistatin 1); 스쿠알라민(squalamine); 줄기세포 저해제(stem cell inhibitor); 줄기세포 분화 저해제(stem-cell division inhibitors); 스티피아마이드(stipiamide); 스트로멜리신 저해제(stromelysin inhibitors); 설피노신(sulfinosine); 수퍼액티브 바소액티브 인테스티날 펩티드 길항제(superactive vasoactive intestinal peptide antagonist); 수라디스타(suradista); 수라민(suramin); 스와인소닌(swainsonine); 합성 글리코사미노글리칸(synthetic glycosaminoglycans); 탈리무스틴(tallimustine); 5-플루오로우라실(5-fluorouracil); 류코보린(leucovorin); 타목시펜 메티오다이드(tamoxifen methiodide); 타우로무스틴 타자로텐(tauromustine; tazarotene); 테코갈란 나트륨(tecogalan sodium); 테가푸르(tegafur); 텔루가피리리움(tellurapyrylium); 텔로머라제 저해제(telomerase inhibitors); 테모포르핀(temoporfin); 테모졸로마이드(temozolomide); 테니포사이드(teniposide); 테트라클로로데카옥사이드(tetrachlorodecaoxide); 테트라조민(tetrazomine); 타리블라스틴(thaliblastine); 티오코랄린(thiocoraline); 트롬보포이에틴(thrombopoietin); 트롬보포이에틴 미메틱(thrombopoietin mimetic); 타이말파신(thymalfasin); 타이모포이에틴 수용체 작용제(thymopoietin receptor agonist); 타이모트리난(thymotrinan); 타이로이드 자극 호르몬(thyroid stimulating hormone); 틴 에틸 에티오푸르퓨린(tin ethyl etiopurpurin); 티라파자민(tirapazamine); 티타노신 비클로라이드(titanocene bichloride); 토프센틴(topsentin); 토레미펜(toremifene); 토티포텐트 줄기 세포 인자(totipotent stem cell factor); 트랜스레이션 저해제(translation inhibitors); 트레티노인(tretinoin); 트리아세틸우리딘(triacetyluridine); 트리시리빈(triciribine); 트리메트렉세이트(trimetrexate); 트리프토렐린(triptorelin); 트로피세트론(tropisetron); 투로스테라이드(turosteride); 티로신 키나아제 저해제(tyrosine kinase inhibitors); 티르포스틴(tyrphostins); UBC 저해제; 우베니멕스(ubenimex); 우로제니탈 시너스-유래된 성장 억제 인자(urogenital sinus-derived growth inhibitory factor); 우로기나아제 수용제 길항제(urokinase receptor antagonists); 바프레오티드(vapreotide); 바리올린 B(variolin B); 벡터 시스템(vector system), 에리트로사이트 유전자 치료법(erythrocyte gene therapy); 탈리도마이드(thalidomide); 베라레솔(velaresol); 베라민(veramine); 베르딘(verdins); 베르테포르핀(verteporfin); 비노렐빈(vinorelbine); 빈잘틴(vinxaltine); 보로졸(vorozole); 자노테론(zanoterone); 제니플라틴(zeniplatin); 질라스코브(zilascorb); 및 지노스타틴 스티말라머(zinostatin stimalamer).
일부 실시양태에서, 상기한 융합 단백질과 조합하여 사용되는 상기 치료제는 면역 조절제이다. 면역 조절제의 비-제한적인 예로는, 사이토카인(cytokines), 변형 펩티드(peptide mimetics), 및 항체(예를 들어, 인간, 인간화, 키메라, 모노클로날, 폴리클로날, Fvs, ScFvs, Fab 또는 F(ab)2 단편 또는 에피토프 결합 단편), 핵산 분자(예를 들어, 안티센스 핵산 분자 및 삼중나선(triple helices)), 소분자, 유기 화합물 및 무기 화합물과 같은 단백질성 제제(proteinaceous agents)를 포함한다. 특히, 면역 조절제는 이에 제한되지는 않으나, 메토트렉세이트, 레플루노마이드(leflunomide), 시클로포스파미드(cyclophosphamide), 사이톡산(cytoxan), 이뮤란(Immuran), 사이클로스포린 A(cyclosporine A), 미노사이클린(minocycline), 아자티오프린(azathioprine), 항생제(예를 들어, FK506(타크로리무스, tacrolimus)), 메틸프레드니솔론(methylprednisolone, MP), 코르티코스테로이드(corticosteroids), 스테로이드, 마이코페놀레이트 모페틸(mycophenolate mofetil), 라파마이신(시로리무스, sirolimus), 미조리빈(mizoribine), 데옥시스페르구알린(deoxyspergualin), 브레퀴날(brequinar), 말로노니트리로아마이드(malononitriloamindes)(예를 들어, 레프루나마이드(leflunamide))가 포함된다. 하나의 실시양태에서, 상기 면역 조절제는 화학 요법제이다. 또 다른 실시양태에서, 상기 면역 조절제는 화학 요법제 외의 면역 조절제이다. 일부 실시양태에서, 본 발명에 따라 사용되는 치료제는 면역 조절제가 아니다.
일부 실시양태에서, 융합 단백질과 조합하여 사용되는 치료제는 항-혈관 신생제(anti-angiogenic agent)이다. 항-혈관 신생제의 비-제한적 예로는 혈관 신생을 감소 또는 억제하는 단백질, 폴리펩티드, 펩티드, 접합체, TNF-α에 결합하는 항체와 같은 항체(예를 들어, 인간, 인간화, 키메라, 모노클로날, 폴리클로날, Fvs, ScFvs, Fab 단편, F(ab)2 단편 및 그의 항원 결합 단편), 핵산 분자(예를 들어, 안티센스 핵산 분자 및 삼중나선), 유기 분자, 무기 분자 및 소분자를 포함한다. 항-혈관 신생제의 다른 예는, 예를 들어, 전체적으로 참고 문헌으로 인용된 미국 공개 특허 공보 제2005/0002934A1호의 단락 277-282에서 찾을 수 있다. 다른 실시양태에서, 본 발명에 따라 사용되는 치료제는 항-혈관 신생제가 아니다.
일부 실시양태에서, 융합 단백질과 조합하여 사용되는 치료제는 염증성 약제이다. 항-염증제의 비-제한적인 예는 당업자에게 공지된 염증 질환 치료에 유용한 제제를 포함하는 임의의 항-염증제를 포함한다. 항-염증제의 비-제한적인 예는 비스테로이드 항염증제(non-steroidal anti-inflammatory drugs, NSAIDs), 스테로이드 항염증제(steroidal anti-inflammatory drugs), 항콜린제(anticholinergics)(예를 들어, 아트로핀 설페이트(atropine sulfate), 아트로핀 메틸니트레이트(atropine methylnitrate), 및 이프라트로피움 브로마이드(ipratropium bromide, ATROVENT.TM.)), β2-작용제(예를 들어, 아부테롤(abuterol; VENTOLIN.TM. 및 PROVENTIL.TM.), 비톨테롤(bitolterol; TORNALATE.TM.), 레브알부테롤(levalbuterol; XOPONEX.TM.), 메타프로테레놀(metaproterenol; ALUPENT.TM.), 피르부테롤(pirbuterol; MAXAIR.TM.), 터부탈린(terbutlaine; BRETHAIRE.TM. 및 BRETHINE.TM.), 알부테롤(albuterol; PROVENTIL.TM., REPETABS.TM., 및 VOLMAX.TM.), 포모테롤(formoterol; FORADIL AEROLIZER.TM.), 및 살메테롤(salmeterol; SEREVENT.TM. 및 SEREVENT DISKUS.TM.)), 및 메틸잔틴(methylxanthines)(예를 들어, 테오필린(theophylline; UNIPHYL.TM., THEO-DUR.TM., SLO-BID.TM., 및 TEHO-42.TM.))를 포함한다. NSAID의 예는 이에 제한되지는 않으나, 아스피린, 이부프로펜, 쎄레콕시브(celecoxib; CELEBREX.TM.), 디클로페낙(diclofenac; VOLTAREN.TM.), 에토돌락(etodolac; LODINE.TM.), 페노프로펜(fenoprofen; NALFON.TM.), 인도메타신(indomethacin; INDOCIN.TM.), 케토랄락(ketoralac; TORADOL.TM.), 옥사프로진(oxaprozin; DAYPRO.TM.), 나부멘톤(nabumentone; RELAFEN.TM.), 설린닥(sulindac; CLINORIL.TM.), 톨멘틴(tolmentin; TOLECTIN.TM.), 로페콕시브(rofecoxib; VIOXX.TM.), 나프록센(naproxen; ALEVE.TM., NAPROSYN.TM.), 케토프로펜(ketoprofen; ACTRON.TM.) 및 나부메톤(nabumetone; RELAFEN.TM.)을 포함한다. 이러한 NSAID는 시클로옥시게나제 효소(예를 들어, COX-1 및/또는 COX-2)를 억제함으로써 작용한다. 스테로이드성 항-염증제의 예는 이에 제한되지는 않으나, 글루코코르티코이드(glucocorticoids), 덱사메타손(dexamethason; DECADRON.TM.), 코르티코스테로이드류(예를 들어, 메틸프레드니솔론(MEDROL.TM.)), 코르티손(cortisone), 히드로코르티손(hydrocortisone), 프리드니손(prednisone; PREDNISONE.TM. 및 DELTASONE.TM.), 프리드니솔론(prednisolone; PRELONE.TM. 및 PEDIAPRED.TM.), 트리암시놀론(triamcinolone), 아줄피딘(azulfidine), 및 에이코사노이드(eicosanoids) 억제제(예를 들어, 프로스타글란딘(prostaglandins), 트롬복산(thromboxanes), 및 류코트리엔(leukotrienes)을 포함한다. 다른 실시양태에서, 본 발명에 따라 사용되는 치료제는 항-염증제가 아니다.
특정 실시양태에서, 사용되는 치료제는 알킬화제, 니트로소우레아, 대사 길항 물질 및 안트라시클린, 토포이소머라제 II 억제제 또는 유사 분열 저해제이다. 알킬화제는 이에 제한되지는 않으나, 부설판(busulfan), 시스플라틴 (cisplatin), 카보플라틴(carboplatin), 클로람부실(chlorambucil), 시클로포스파마이드(cyclophosphamide), 이포스파미드(ifosfamide), 데카르바진(decarbazine), 메클로레타민(mechlorethamine), 멜팔란(melphalan), 및 테모졸로마이드(themozolomide)를 포함한다. 니트로소우레아는 카르무스틴(carmustine, BCNU)과 로무스틴(lomustine, CCNU)을 포함하나 이에 제한되지 않는다. 대사 길항 물질(antimetabolite)은 5-플루오로우라실(5-fluorouracil), 카페시타빈(capecitabine), 메토트렉세이트(methotrexate), 젬시타빈(gemcitabine), 시타라빈(cytarabine) 및 플루다라빈(fludarabine)을 포함하나 이에 제한되지 않는다. 안트라시클린은 다우노루비신(daunorubicin), 독소루비신(doxorubicin), 에피루비신(epirubicin), 이다루비신(idarubicin) 및 미톡산트론(mitoxantrone)을 포함하나 이에 제한되지 않는다. 토포아이소머라제 II 억제제는 토포테칸(topotecan), 이리노테칸(irinotecan), 에토포시드(etoposide, VP-16), 및 테니포시드(teniposide)를 포함하나 이에 제한되지는 않는다. 유사 분열 저해제는 탁산(taxanes; 파클리탁셀(paclitaxel), 도세탁셀(docetaxel)) 및 빈카 알칼로이드(vinca alkaloids; 빈블라스틴(vinblastine, 빈 크리스틴(vincristine) 및 비노렐빈(vinorelbine))을 포함하나 이에 제한되지 않는다.
일부 실시양태에서, 상기 융합 단백질은 암 줄기 세포 및/또는 암세포를 파괴시키기 위해 x-ray, 감마선 및 다른 방사선원의 사용을 포함하는 방사선 요법과 조합하여 사용된다. 특정 실시양태에서, 상기 방사선 요법은 방사선이 원격 소스로부터 유도되는 외부 방사선 방출 또는 원격 요법으로 투여된다. 다른 실시 양태에서, 상기 방사선 요법은 방사성 선원이 암 줄기 세포, 암세포 및/또는 종양 덩어리에 가까운 신체 내부에 위치하는 내부 치료 또는 근접 치료제로서 투여된다.
7. 암의 유형
임의의 유형의 암은 본 발명에 따라 예방, 치료 및/또는 관리될 수 있다. 본 발명에 따라 예방. 치료 및/또는 관리될 수 있는 암의 비제한적인 예로는 다음을 포함한다; 이에 제한되지는 않으나, 급성 백혈병, 급성 림프구성 백혈병, 골수아구성(myeloblastic), 전골수구성(promyelocytic), 골수 단핵구성(myelomonocytic), 단핵구(monocytic)와 같은 급성 골수세포 백혈병, 및 적혈구백혈병 및 골수이형성 증후군과 같은 백혈병; 이에 제한되지는 않으나, 만성 골수성(과립구성) 백혈병, 만성 림프구성 백혈병, 털세포백혈병과 같은 만성 백혈병; 진성적혈구 증가증(polycythemia vera); 이에 제한되지는 않으나 호지킨 병( Hodgkin's disease) 및 비-호지킨 병과 같은 림프종; 무증후성 다발성 골수종, 비-분비성 골수종, 골경화 골수종, 형질세포성 백혈병, 단독형 형질세포종 및 골수외 형질세포종과 같은 다발성 골수종; 발덴스트롬 거대글로불린혈증(Waldenstrom's macroglobulinemia); 미확정 단일클론성 면역글로불린혈증(monoclonal gammopathy of undetermined significance); 양성 단일클론성 글로불린혈증(benign monoclonal gammopathy); 중쇄질환(heavy chain disease); plasmacytoid 수지상 세포 암, NK 세포성 림프종(피부 NK/T 세포 림프종 및 과형성 (CD4+/CD56+) 피부 신생물로 알려져 있음)을 포함하는 수지상 세포 암; 호염기성 백혈병; 이에 제한되지 않으나, 뼈 육종(bone sarcoma), 골육종(osteosarcoma), 연골육종, 유잉육종(Ewing's sarcoma), 악성거대세포종양, 골섬유육종, 척색종, 골막육종, 연조직 육종, 혈관육종(혈관내피육종), 섬유육종, 카포시 육종(Kaposi's sarcoma), 평활근육종, 지방육종, 림프관 육종, 시반종, 횡문근육종, 활막육종과 같은 뼈 및 결합 조직 육종; 이에 제한되지는 않으나, 신경교종, 성상세포종, 뇌간 신경교종, 상의세포종, 핍지교종, 비-신경교종, 청신경초종, 두 개인두종, 수모세포종, 뇌수막종, 솔방울세포종, 솔방울샘모세포종, 원발성 뇌 림프종과 같은 뇌종양; 이에 제한되지는 않으나, 유관암종, 선암, 소엽(소세포)암종, 비침윤성 관내 암종, 수질성 유방암, 점액성 유방암, 유관암, 유두암, 파제트병(Paget's disease) 및 염증성 유방암을 포함하는 유방암; 이에 제한되지는 않으나, 갈색세포종 및 부신피질암과 같은 부신암종; 이에 제한되지는 않으나, 유두 또는 소낭갑상선암, 갑상선 수질암 및 악성갑상선암과 같은 갑상선암; 이에 제한되지는 않으나, 인슐린종, 가스트린종, 글루카곤종, 비포마(vipoma), 소마토스타틴-분비 종양 및 유암 또는 도세포종(carcinoid or islet cell tumor)과 같은 췌장암; 이에 제한되지는 않으나, 쿠싱병, 프로락틴-분비 종양, 말단비대증 및 요붕증과 같은 뇌하수체암; 이에 제한되지는 않으나, 홍채 흑색종과 같은 안구 흑색종, 맥락막 흑색종, 섬모체 흑색종 및 망막아세포종과 같은 안암; 편평상피암, 선암 및 흑색종과 같은 질암; 편평상피암, 흑생종, 선암, 기저세포암, 육종 및 파제트병과 같은 외음부암; 이에 제한되지는 않으나, 편평상피암 및 선암과 같은 자궁경부암; 이에 제한되지는 않으나, 자궁내막암 및 자궁육종과 같은 자궁암; 이에 제한되지는 않으나, 난소 상피 암종, 경계성 종양, 생식세포 종양 및 간질종양과 같은 난소암; 이에 제한되지는 않으나, 편평세포암, 선암, 선모낭포암, 점막 표피종양, 선편평세포암종, 육종, 흑색종, 형질세포종, 사마귀모양암종 및 귀리세포(소세포) 암종과 같은 식도암; 이에 제한되지는 않으나, 선암, 진균양(폴립모양), 궤양, 표재 확산성(superficial spreading), 분산 확산성(diffusely spreading), 악성 림프종, 지방육종, 섬유육종 및 암육종과 같은 위암; 결장암; 직장암; 이에 제한되지는 않으나, 간세포암종 및 간아세포종과 같은 간암; 선암과 같은 담낭암; 이에 제한되지는 않으나, 유두, 결절성 및 확산과 같은 담관암; 이에 제한되지는 않으나, 비소세포성 폐암. 편평상피세포암(epidermoid carcinoma), 선암, 대세포 암종 및 소세포 폐암과 같은 폐암; 이에 제한되지는 않으나, 생식세포 종양, 정상피종, 악성, 고전적(전형적), 정모세포성, 비정상피종, 배아암종, 기형암종, 융모암종(난황종양)과 같은 고환암; 이에 제한되지는 않으나, 전립선 상피내 종양, 선암, 평활근육종 및 횡문근육종과 같은 전립선암; 음경 암(penal cancers); 이에 제한되지는 않으나, 편평세포암종과 같은 구강암; 기저암; 이에 제한되지는 않으나, 선암, 점막표피종양 및 섬모낭포암과 같은 침샘암; 이에 제한되지는 않으나, 편평세포암 및 사마귀모양종과 같은 인두암; 이에 제한되지는 않으나, 기저세포암종, 편평세포암종 및 흑색종, 표재 확산성 흑색종, 결절성 흑색종, 흑색점 악성 흑색종, 말단흑자흑색종과 같은 피부암; 이에 제한되지는 않으나, 신세포암(renal cell carcinoma), 선암, 신장세포암(hypernephroma), 섬유육종, 이행세포암(신장 골반 및/또는 자궁)과 같은 신장암; 빌름스 종양(Wilms' tumor); 이에 제한되지는 않으나, 이행상피암, 편평세포암종, 선암, 암육종증과 같은 방광암. 또한, 암은 점액육종, 골육종, 내피육종(endotheliosarcoma), 림프관 종양 육종(lymphangioendotheliosarcoma), 중피종, 활막종, 혈관막세포종, 상피세포암, 낭선암종, 기관지원성암종, 한선암종, 피지선암종, 유두암종, 유두샘암종을 포함한다(상기 질환에 대한 검토는 Fishman et al., 1985, Medicine, 2d Ed., J.B. Lippincott Co., Philadelphia and Murphy et al., 1997, Informed Decisions: The Complete Book of Cancer Diagnosis, Treatment, and Recovery, Viking Penguin, Penguin Books U.S.A., Inc., United States of America 참조).
다음을 포함하는 다양한 암 또는 다른 비정상적인 과증식성 질환(이에 제한되지 않음)의 치료, 예방 및/또는 관리에 예방적 및/또는 치료적으로 효과적인 요법은 유용하다: 방광, 유방, 대장, 신장, 간, 폐, 난소, 췌장, 위, 자궁 경부, 갑상선 및 피부의 암을 포함하는 암종; 편평 세포 암종; 백혈병, 급성 림프성 백혈병, 급성 림프구성 백혈병, B세포 림프종, T 세포 림프종, 버키트 림프종을 포함하는 림프계 계통의 조혈 종양; 급성 및 만성 골수성 백혈병 및 전골수성 백혈병을 포함하는 골수 계통의 조혈 종양; 섬유육종 및 횡문근육종을 포함하는 간엽 기원의 종양; 흑색종, 정상피종, 기형암(tetratocarcinoma), 신경아세포종 및 신경교종을 포함하는 다른 종양; 성상세포종. 신경아세포종, 신경교종 및 신경초종을 포함하는 중추 및 말초 신경계의 종양; 섬유육종, 횡문근육종 및 골육종을 포함하는 간엽 기원의 종양; 및 흑색종, 색소피부건조증, 각질세포종(keratoactanthoma), 정상피종, 갑상샘암 및 기형암을 포함하는 다른 종양. 일부 실시양태에서, 세포 사멸(apoptosis)의 이상과 관련된 암이 본 발명의 방법에 따라 예방, 치료 및/또는 관리된다. 그러한 암은 여포성 림프종, p53 돌연변이를 갖는 암종, 유방, 전립선 및 난소의 호르몬 의존성 종양 및 가족성 선종성 용종증과 골수이형성증후군과 같은 전암성 병변을 포함하나 이에 한정되지는 않는다. 특정 실시양태에서, 악성 또는 변화(예를 들어 화생 및 이형성증), 또는 피부, 폐, 간, 뼈, 뇌, 위, 대장, 유방, 전립선, 방광, 신장, 췌장, 난소 및/또는 자궁의 과증식성 질환은 본 발명의 방법에 따라 예방, 치료 및/또는 관리된다. 다른 특정 실시양태에서, 육종, 흑색종 또는 백혈병은 본 발명의 방법에 따라 예방, 치료 및/또는 관리된다. 특정 실시양태에서, 상기 개체는 급성 골수성 백혈병(acute myelogenous leukemia, AML)을 갖는다. 특정 다른 실시양태에서, 상기 개체는 골수이형성증후군(myelodysplastic syndrome, MDS)을 갖는다. 다른 실시양태에서, 상기 개체는 만성 골수성 백혈병(chronic myelomonocytic leukemia, CMML)을 갖는다. 다른 특정 실시양태에서, 골수이형성증후군은 본 발명의 방법에 따라 예방, 치료 및/또는 관리된다.
암 치료의 주요 목표는 전신 독성없이 적절한 치료제의 충분한 양으로 종양을 표적화 할 수 있어야 한다는 것이다.
특정 실시양태에서, 상기 암을 치료하는 방법은: (i) 암 세포의 감소, (ii) 암 세포의 증가의 부재; (iii) 암 세포의 생존 가능성의 감소; (iv) 개체에서 암세포의 성장 감소를 포함한다.
특정 실시양태에서, 본원의 방법으로 치료되는 상기 개체는 상기 질환을 가지는 것으로 진단되어 치료를 받은 개체이다. 특정 실시양태에서, 본원의 방법으로 치료되는 상기 개체는 암으로 진단되어 암 치료를 받은 개체이다.
특정 실시양태에서, 상기 개체는 암으로부터 완화되어 있다. 특정 실시양태에서, 상기 개체는 암이 재발한 개체이다. 특정 실시양태에서, 상기 개체는 암 치료에 실패하는 개체이다.
8. 키트
본 발명에 기재된 상태를 치료하는데 유용한 물질을 함유하는 제조 물품 및 키트가 본원에서 제공된다. 상기 제조 물품은 라벨과 함께 본원에 기재된 화합물의 용기(container)를 포함할 수 있다. 적합한 용기는 예를 들어, 병, 바이알 및 시험관을 포함한다. 상기 용기는 유리 또는 플라스틱과 같은 다양한 재료로 형성될 수 있다. 상기 용기는 암의 치료 또는 예방에 효과적인 백신을 함유하는 조성물을 보유한다. 용기상의 라벨은 상기 조성물이 특정 상태를 치료하는데 유용하다는 것을 나타낼 수 있고 또한 투여 지침을 나타낼 수 있다.
하나 이상의 실시양태에서, 본 발명은 백신의 치료 유효량을 포함하는 키트를 제공할 수 있다. 백신의 임의의 실시양태는 본원 내용의 하나 이상의 구현에 따라 하나 이상의 키트에 포함될 수 있음이 이해되어야 한다.
9. 면역 반응
개체에서 전장 단백질에 의해 발생하는 면역 반응과 폴리펩티드에 의해 발생하는 면역 반응의 비교는 당업계에서 이용 가능한 임의의 수단에 의해 수행될 수 있다. 하기의 실시예에서 사용된 하나의 간단한 방법은 마우스와 같은 모델 개체의 면역화 및 E. coli 치사량 접종을 포함한다. 적절한 비교를 위해, 당업자는 프로인드 보조제(Freund's complete adjuvant)와 같은 동일한 보조제를 자연적으로 선택할 것이다. 이러한 실험에서 본 발명의 면역원성 폴리펩티드 단편은, 만약에 예를 들어, 전장 단백질이 제공하는 보호의 적어도 70% 이상, 전장 단백질이 제공하는 보호의 적어도 80% 이상, 전장 단백질이 제공하는 보호의 적어도 85% 이상, 전장 단백질이 제공하는 보호의 적어도 90% 이상, 전장 단백질이 제공하는 보호의 적어도 95% 이상, 전장 단백질이 제공하는 보호의 적어도 97% 이상, 전장 단백질이 제공하는 보호의 적어도 98% 이상, 또는 전장 단백질이 제공하는 보호의 적어도 99% 이상의 보호를 제공한다면, 개체에서 실질적으로 유사한 면역 반응을 일으킬 것이다(즉, 치명적인 도전에 대해 실질적으로 동일한 보호를 제공할 것이다).
본 발명의 조성물은 체액성 면역 반응뿐만 아니라 세포-매개된 면역 반응을 모두 유도할 수 있다. 이러한 면역 반응은 항원에 대한 재노출시 신속하게 반응할 수 있는 오래 지속되는(예 : 중화) 항체 및 세포-매개 면역을 바람직하게 유도할 것이다.
두 종류의 T세포, CD4 및 CD8 세포는 일반적으로 세포-매개된 면역 및 체액 면역을 개시 및/또는 향상시키는데 필요하다고 알려져 있다. CD8 T세포는 CD8 보조 수용체(co-receptor)를 발현할 수 있고, 일반적으로 세포 독성 T 림프구(Cytotoxic T lymphocytes, CTL)라고 한다. CD8 T세포는 MHC 클래스 I 분자에 표시된 항원을 인식하거나 상호 작용할 수 있다.
CD4 T세포는 CD4 보조 수용체를 발현할 수 있고 일반적으로 T 헬퍼 세포라고 한다. CD4 T세포는 MHC 클래스 II 분자에 결합된 항원 펩타이드를 인식할 수 있다. MHC 클래스 II 분자와 상호 작용할 때, 상기 CD4 세포는 사이토카인과 같은 인자를 분비할 수 있다.
이 분비된 사이토카인은 B세포, 세포 독성 T세포, 대식세포 및 면역 반응에 관여하는 다른 세포들을 활성화시킬 수 있다.
도 1A-B는 알파 바이러스의 단백질의 구조를 나타낸 것이다. (A) 신드비스(Sindbis) 바이러스의 cryo-EM 밀도는 T=4 대칭성을 보임. 하나의 비대칭 단위에서 4개의 E2 분자. 이것들은 각 20면체 3중 축(icosahedral three-fold axis) 및 하나의 일반적으로 위치한 스파이크에서 삼량체 스파이크(trimeric spike)를 발생시킨다. (B) 캡시드, E3, E2, 6K 및 E1 단백질의 위치를 보여주는 소포체 막을 통한 신드비스 바이러스 구조 폴리프로테인의 스레딩(Threading) (Li, L. et al. Structural changes of envelope proteins during alphavirus fusion. Nature 468, 705-708 (2010)).
도 2A-B는 당단백질 스파이크의 도메인 구조를 나타낸 것이다. (A) p62-E1 헤테로다이머의 리본 도면. E1 도메인 I, II 및 III은 각각 빨간색, 노란색 및 파란색으로 표시되고, 융합 루프(fusion loop, FL)는 주황색으로 표시함. E3는 흰색/회색으로 색칠되어 있고, E2 도메인 A는 청록색, B는 짙은 녹색, C는 핑크색 및 β-리본은 진한 보라색. N-결합된 글리칸(N-linked glycans)은 볼과 막대기로 표시되며 원자 유형에 따라 색이 정해지고 분류됨. 이황화물은 녹색 막대기로 묘사됨. 검정색 화살표(p62와 E1의 C 말단을 각각 나타내는 핑크색 별과 파란색 별 옆에 있음)는 바이러스 막을 가리킴. 헤테로다이머 ‘플레이트(plate)'가 ’꼬여 있지 않은(untwisted)' 것으로 그려져 있는 삽입된 도면은 도메인이 서로 어떻게 관련되어 있는 지와 연결 상태를 보여줌. (B) p62 구성, E3를 보여주기 위한 a로부터 대략 90도 방향(Voss JE, et al. Glycoprotein organization of chikungunya virus particles revealed by x-ray crystallography. Nature 468, 709712 (2010)).
도 3은 조작된 재조합 신드비스 VGP의 구조를 나타낸 것이다. 왼쪽, SINV에 의해 코딩된 완전한 구조의 단백질 조성. 오른쪽, 종양-관련 항원(Tumor Associated Antigen, TAA)과 연결된 6K 부위 및 막관통 도메인(transmembrane domains)이 없는 조작된 VGP.
도 4A-C는 조작된 바이러스 당단백질 E2 E1 이량체 및 TAA가 형성한 스파이크 삼량체를 나타낸 것이다. 막관통(transmembrane) 및 6K 부위는 제거되었고 E2와 E1은 유연한 링커로 연결된다. 상기 E3 서열은 ER 표적 서열로서 작용하고, E2/E1 이량체화를 보조한다. TAA는 다른 유연한 링커 및 프로테아제 절단 부위와 함께 E1의 C-말단에 첨가된다. 골지체로부터 분비할 때 TAA를 운반하는 용해성 스파이크를 형성하는 삼량체화된 VGP.
도 5는 융합 단백질 E3-E2-링커-E1-TEV-링커-NY-ESO-1-6X His의 일례의 아미노산 서열을 나타낸 것이다. 1 내지 65 위치의 E3-아미노산 잔기; 66-429 위치의 E2-아미노산 잔기; 430-448 위치의 링커-아미노산 잔기; 449-854 위치의 E1-아미노산 잔기; 855-876 위치의 TEV-링커-아미노산 잔기; 및 877-978 위치의 NY-ESO-1 펩티드 단편 아미노산 잔기; 979-984 위치의 6X His-아미노산 잔기. 굵은 N은 글라이코실화 위치로서 261, 383, 587 및 693 위치의 아미노산 잔기이다.
도 6은 융합 단백질 E3-E2-링커-E1-TEV-링커-NY-ESO-1-6X His의 일례의 핵산 서열을 나타낸 것이다.
도 7은 정제된 융합 단백질의 웨스턴 블랏을 나타낸 것이다. 상등액을 100 ml 배양액으로부터 수득하였고, 단백질은 Ni 친화성 크로마토그래피로 정제하였다. 예상 분자량: 106.8 kDa.
레인 M2 : 용이한 웨스턴 마커(Easy western marker)
레인 1 : 세포 용해물의 중간층
레인 2 : 통과액(flow through)
레인 3 : 20 mM 이미다졸(imidazole) 용출액
레인 4 : 500mM 이미다졸 용출액
레인 5 : 용출 후 수지(resins)
항체 : 항-His 항체(Genscript, Cat.No. A00186)
도 8A-F는 본원에 기재된 융합 단백질을 제조하기에 유용한 항원의 아미노산 서열을 나타낸 것이다(서열번호 3-11).
도 9는 서열번호 12의 전체 신드비스 구조 단백질 서열(캡시드, E3, E2 세포외 도메인, E2 막통과 도메인, 6K, E1 세포외 도메인, E1 막통과 도메인)을 나타낸 것이다.
도 2A-B는 당단백질 스파이크의 도메인 구조를 나타낸 것이다. (A) p62-E1 헤테로다이머의 리본 도면. E1 도메인 I, II 및 III은 각각 빨간색, 노란색 및 파란색으로 표시되고, 융합 루프(fusion loop, FL)는 주황색으로 표시함. E3는 흰색/회색으로 색칠되어 있고, E2 도메인 A는 청록색, B는 짙은 녹색, C는 핑크색 및 β-리본은 진한 보라색. N-결합된 글리칸(N-linked glycans)은 볼과 막대기로 표시되며 원자 유형에 따라 색이 정해지고 분류됨. 이황화물은 녹색 막대기로 묘사됨. 검정색 화살표(p62와 E1의 C 말단을 각각 나타내는 핑크색 별과 파란색 별 옆에 있음)는 바이러스 막을 가리킴. 헤테로다이머 ‘플레이트(plate)'가 ’꼬여 있지 않은(untwisted)' 것으로 그려져 있는 삽입된 도면은 도메인이 서로 어떻게 관련되어 있는 지와 연결 상태를 보여줌. (B) p62 구성, E3를 보여주기 위한 a로부터 대략 90도 방향(Voss JE, et al. Glycoprotein organization of chikungunya virus particles revealed by x-ray crystallography. Nature 468, 709712 (2010)).
도 3은 조작된 재조합 신드비스 VGP의 구조를 나타낸 것이다. 왼쪽, SINV에 의해 코딩된 완전한 구조의 단백질 조성. 오른쪽, 종양-관련 항원(Tumor Associated Antigen, TAA)과 연결된 6K 부위 및 막관통 도메인(transmembrane domains)이 없는 조작된 VGP.
도 4A-C는 조작된 바이러스 당단백질 E2 E1 이량체 및 TAA가 형성한 스파이크 삼량체를 나타낸 것이다. 막관통(transmembrane) 및 6K 부위는 제거되었고 E2와 E1은 유연한 링커로 연결된다. 상기 E3 서열은 ER 표적 서열로서 작용하고, E2/E1 이량체화를 보조한다. TAA는 다른 유연한 링커 및 프로테아제 절단 부위와 함께 E1의 C-말단에 첨가된다. 골지체로부터 분비할 때 TAA를 운반하는 용해성 스파이크를 형성하는 삼량체화된 VGP.
도 5는 융합 단백질 E3-E2-링커-E1-TEV-링커-NY-ESO-1-6X His의 일례의 아미노산 서열을 나타낸 것이다. 1 내지 65 위치의 E3-아미노산 잔기; 66-429 위치의 E2-아미노산 잔기; 430-448 위치의 링커-아미노산 잔기; 449-854 위치의 E1-아미노산 잔기; 855-876 위치의 TEV-링커-아미노산 잔기; 및 877-978 위치의 NY-ESO-1 펩티드 단편 아미노산 잔기; 979-984 위치의 6X His-아미노산 잔기. 굵은 N은 글라이코실화 위치로서 261, 383, 587 및 693 위치의 아미노산 잔기이다.
도 6은 융합 단백질 E3-E2-링커-E1-TEV-링커-NY-ESO-1-6X His의 일례의 핵산 서열을 나타낸 것이다.
도 7은 정제된 융합 단백질의 웨스턴 블랏을 나타낸 것이다. 상등액을 100 ml 배양액으로부터 수득하였고, 단백질은 Ni 친화성 크로마토그래피로 정제하였다. 예상 분자량: 106.8 kDa.
레인 M2 : 용이한 웨스턴 마커(Easy western marker)
레인 1 : 세포 용해물의 중간층
레인 2 : 통과액(flow through)
레인 3 : 20 mM 이미다졸(imidazole) 용출액
레인 4 : 500mM 이미다졸 용출액
레인 5 : 용출 후 수지(resins)
항체 : 항-His 항체(Genscript, Cat.No. A00186)
도 8A-F는 본원에 기재된 융합 단백질을 제조하기에 유용한 항원의 아미노산 서열을 나타낸 것이다(서열번호 3-11).
도 9는 서열번호 12의 전체 신드비스 구조 단백질 서열(캡시드, E3, E2 세포외 도메인, E2 막통과 도메인, 6K, E1 세포외 도메인, E1 막통과 도메인)을 나타낸 것이다.
1. 융합 단백질의 제조
하나의 실시양태에서, 신드비스(Sindbis) 융합 단백질은 Sf9 곤충 세포에서의 바큘로 바이러스(baculovirus) 발현에 의해 생성된다. 바큘로 바이러스는 특정 무척추동물 종에만 감염할 수 있기 때문에, 포유동물에서 비-병원성이다. 박테리아 단백질 발현과 달리, 바큘로 바이러스 시스템에서 발현된 단백질은 포유류 발현 시스템에서 생산된 것과 유사하게 처리, 접힘 및 변형된다. 게다가, 바큘로 바이러스-발현된 단백질은 재조합 단백질을 대량으로 생산하도록 쉽게 스케일 업(scaled up)된다. 곤충 세포주는 현탁 배양에서 잘 자랄 수 있기 때문에, 대규모 생물 반응기(large-scale bioreactors)에서 재조합 단백질을 생산할 수 있다. 곤충 및 포유동물 세포는 모두 N-연결 글리코실화(N-linked glycosylation)를 만들 수 있는 반면, 특정 글리코실화 경로는 다르다. 곤충 세포에서 생산된 N-글리칸은 높은 함량의 만노오스 또는 포시만노오스(paucimannose) 구조를 가질 수 있으며, 이들 모두는 말단 만노오스 잔기를 가진다. 포유동물 세포에서 생산된 N-글리칸은 고 만노오스(high mannose) 구조 또는 갈락토오스 및 시알산(sialic acid)에서 종결되는 복합체 구조를 가질 수 있다. 수지상 세포(dendritic cell, “DC”) 수용체(수지상 세포 특이적 세포간 부착 분자-3-Grabbibg 비-인테그린) DC-SIGN에 대한 SINV의 결합은 엔빌로프(envelope) 당단백질의 고 만노오스 글리코실화를 필요로 한다. 포유동물 세포에서 생산된 바이러스는 추가적인 효소 변형없이 DC-SIGN에 결합하지 않는다. 따라서, 곤충 세포에서의 융합 단백질의 생산은 DC에 대한 TAA의 효과적인 표적화를 달성한다.
VGP를 코딩하는 유전자는 유전자 합성을 통해 생산되고 곤충세포 발현을 위해 코돈-최적화된다. 상기 재조합 융합 단백질은 제2 링커에 의해 TAA에 연결되고 유연한 링커(flexible linker)에 의해 결합된 pE2 및 E1 신드비스 당단백질의 세포외 도메인으로 구성된다(도 4 참조). 하나의 실시양태에서, TAA는 NY-ESO-1이다. 특정 실시양태에서, 기타 TAA이 코딩 서열에 삽입된다. 대안적으로, 두 개 이상 TAA를 동시에 갖는(in tandem) 작제물을 생성하여, 보다 강력한 면역 반응을 야기한다. pE2의 E3 성분은 단백질의 분비를 위한 신호 펩타이드로 작용하고, E1과 E2의 결합을 돕고, 푸린(furin)에 의한 자연적으로 성숙 단백질로부터 절단된다. 알파바이러스 당단백질은 E2 및 E1의 헤테로다이머 복합체의 삼량체를 형성하는 성숙한 분비된 단백질로 생성되며, 이는 SINV 엔빌로프에서 관찰된 삼량체 당 단백질 스파이크를 모방한다. 상기 제2 유연한 링커는 E2/E1의 다량체화를 방해하지 않으며 NY-ESO-1의 적절한 접힘을 허용한다. 게다가, NY-ESO-1의 처음 80개 아미노산은 글리신이 풍부하고 주로 T 세포 항원이 결핍되어 있기 때문에, 하나의 실시양태에서는 81-180 아미노산 잔기만이 작제물에 포함되어 있다. 특정 실시양태에서, 상기 TAA는 NY-ESO-1의 1-180, 81-100, 100-150, 150-180 아미노산 잔기를 포함한다. 정제 목적으로, 단백질의 C-말단에 His-tag가 첨가되었다. 신규한 단백질은 비-변성 겔 및 크기-배제 크로마토그래피에 의해 다량체 구조를 결정하기 위해 분석하였다. 더 나아가, 단백질에 특이적인 ELISA 및 웨스턴 블랏 분석이 개발되어 있다. 상기 단백질은 시판되는 항체로 검출되는 여러 항원 표적(NY-ESO-1, His-tag, 및 SINV E1 및 E2)을 갖는다.
본원에는 종양-관련 항원 NY-ESO-1으로 부터 유래된 절단된(truncated) 펩티드에 연결된 신드 비스 바이러스의 세포외 도메인 E3, E2 및 E1 단백질로 구성된 재조함 단백질인 바이러스 당단백질 복합체가 함께 제공된다. 신드비스 바이러스 구조 단백질 E3, E2, 6K, E1은 NCBI 웹 사이트 참조 서열 NP_062890.1의 아미노산 서열을 참조할 수 있다. 상기 E2 및 E1 단백질의 막관통 도메인(transmembrane domain)이 코딩 서열로부터 제거되었다. 상기 E2 및 E1 단백질은 6K 영역 대신에 유연한 글리신/세린 링커(GGGGSGGGGSGGGGSGGGG)에 의해 결합되었다. 상기 NY-ESO-1의 아미노산 서열은 NCBI 웹 사이트 참조 서열 NP_001318.1이다. NY-ESO-1의 N-말단은 매우 글리신이 풍부하고 주로 T 세포 항원이 결핍되어 있기 때문에, 하나의 실시양태에서는, 단백질의 처음 78개 아미노산은 결실되었다. 하나의 실시양태에서, 상기 신드비스 E3/E2/E1 서열은 TEV 절단 부위(ENLYFQ) 및 제2 글리신/세린 링커(GGGGGSGGGGSGGGGS)에 의해 절단된 102개 아미노산 NY-ESO-1 단백질에 연결되었다. 하나의 실시양태에서, 정제 목적으로, 단백질의 C-말단에 6x-His 태그가 첨가되었다. 재조합 단백질을 암호화하는 DNA 서열은 진스크립(Genscript, Piscataway, NJ)에 의해 합성되었고 코돈은 Sf9 세포에서 발현을 위해 최적화되었다. DH10Bac 균주는 재조합 바크미드(bacmid) 생성에 사용되었다. Sf9 곤충 세포를 Cellfectin II를 사용하여 bacmid로 형질 감염시키고, 27℃에서 5-7일 동안 Sf-900 II 배지에서 배양하였다. 원심분리 후 상등액을 수집하였고 P1 바이러스 스톡(P1 viral stock)으로 지정하였다. 세포를 P1으로 더 감염시켜 높은 적정농도의 P2 스톡을 만들었다. Sf9 세포를 P2 바이러스로 형질감염 시켰고, 72 시간 후에 배지를 수집하였다. 상등액을 프로테아제 억제제를 포함하는 5 0 mM Tris, 150 mM NaCl, pH8.0에 대해 투석하였고, 단백질을 Ni 컬럼(column)으로 정제하였고, 항-His 웨스턴 블랏으로 분석하였다.
2. 수용체 결합 분석
SINV는 종양 세포(laminin 수용체)와 수지상 세포 (DC-SIGN)의 수용체에 결합한다. 바이러스의 표면의 E2/E1 헤테로 다이머 삼량체의 입체 형태를 유지하는 융합 단백질은 이와 같은 수용체에 결합한다. DC-SIGN 결합의 경우, 단백질 A 마이크로 비드 및 DC-SIGN Fc 융합 단백질을 사용하는 분석법이 사용되었다. 융합 단백질은 DC-SIGN으로 최대한 코팅된 비드에 결합한 다음, VGP에 대해 형광 표지된 2차 항체(anti-His 또는 anti-NY-ESO-1)를 유동세포 분석기로 검출하는데 사용하였다. 결합(binding)은 다양한 단백질 농도에서 항 DC-SIGN 항체와 같은 다른 DC-SIGN 표적화 방법과 비교하여 분석하였다. 96-웰 플레이트 리더기가 장착된 유동 세포 분석기(flow cytometer)를 사용하여, 이들 분석은 고효율 방식으로 수행될 수 있다. 바이러스성 단백질은 DC-SIGN에 대한 항체와 유사한 친화성을 갖는 DC에 대한 항원을 표적으로 한다. 게다가, DC에 대한 융합 단백질의 결합은 인간(DC-SIGN 발현) 및 마우스(L-SIGN) 둘 다로부터 분석된다. 수용체-차단 항체(receptor-blocking antibodies)와 만난(mannan), 만노오스(mannose) 다당류(polysaccharide)는 상호 작용의 특이성을 입증하는데 사용된다. 라미닌(laminin) 수용체 결합의 경우, 상기 결합은 라미닌 수용체 발현의 변화 정도와 다양한 세포주를 사용하여 분석된다. 상기 결합은 라미닌 수용체에 대한 항체 사용 또는 수용체에 대한 천연 리간드인 과량의 라미닌으로 차단될 수 있다. 상기 융합 단백질은 방관자 세포(bystander cells )보다 우선적으로 이들 세포와 결합하여, DC에 종양-관련 항원을 효과적으로 전달하여 프로세싱 및 표시(presentation)되게 한다.
3. 시험관내(in vitro) 분석
SINV는 NK 세포 모집을 통해 종양 세포에 대한 면역계의 반응 및 바이러스에 의해 코딩된 종양-관련 항원에 대한 T 세포의 활성화를 증가시킨다. 이러한 효과의 후자는 DC-SIGN 수용체를 통해 바이러스에 의한 DC에 항원이 전달됨으로서 완성된다. 강력한 T세포 반응을 유도하기 위해, 상기 DC는 바이러스, 박테리아 또는 기생충에 공통인 병원체-관련 분자 패턴(pathogen-associated molecular patterns, PAMPs)의 검출을 통해 첫 번째로 활성화되어야 한다. 활성화된 DC는 보조 자극 분자 B7-1 및 B7-2뿐만 아니라 MHC 분자의 증가된 수준을 나타낸다. 따라서, 상기 재조합 융합 단백질이 DC 활성화를 유도하기에 충분한 면역원성을 갖는지 또는 보조제와 결합하는 것이 필요한지를 평가할 필요가 있다
인간 말초 혈액 단핵 세포(human peripheral blood mononuclear cells, PBMC)로부터, 특정 면역 세포 유형의 순수한 집단은 마그네틱 비드 선택에 의해 얻어지며, VGP/NY-ESO-1의 직접적인 효과를 평가한다. DC 및 NK 세포의 활성화는 세포 표면상의 활성화 마커의 유동 세포 계측 분석 및 ELISA에 의한 사이토카인의 검출에 의해 측정될 수 있다. 종양 특이적 반응을 조절하는 능력은 암 환자에게서 획득한 T 세포를 사용하여 평가된다. 이 환자들은 종양 항원에 노출되어 있으며, 건강한 공여자와 비교하여 종양 특이적 T 세포의 비율이 높다. 환자의 DC를 상기한 재조합 융합 단백질로 밤새 처리하고, 그동안 단백질을 흡수하고, 가공하였고, 관련 에피토프(epitope)는 세포 표면에 표시된다. DC는 며칠 동안 환자 T 세포와 함께 배양되었고, 이 시점에서 T 세포는 항원-특이적 반응에 대해 분석될 것이다. CFSE-표지된 T 세포를 사용하여, T 세포 증식을 유동 세포 계측법으로 측정한다. ELISPOT 분석은 활성화된 NY-ESO-1-특이적 T 세포를 검출하는데 사용된다. NY-ESO-1-특이적 T 세포는, ELISPOT 플레이트의 웰을 코팅하는 항체에 의한 검출을 위해 포획된 DC에 의해 표시된 특이적 에피토프를 인식할 때 IFNγ를 생성한다. 이러한 분석은 융합 단백질로부터의 펩티드가 수지상 세포에 의해 처리되고 표시되며, T 세포 반응이 인간에서 자극되는 것을 입증한다.
본 발명자가 VGP 치료의 가장 중요한 효과가 면역계의 활성화를 통해 있다고 판단하고 있으나, laminin 수용체를 통한 직접 종양 표적화의 역할은 무시되어서는 안된다. SINV는 바이러스 복제가 없을 때, 종양 세포에서 세포 사멸(apoptosis)을 유도한다. VGP가 종양 세포의 성장 및 생존에 미치는 영향을 시험관내(in vitro)에서 조사하였다. 직접적인 단백질-종양 상호작용이 치료 효과에 어떤 영향을 미치는지 평가하기 위해, 다양한 수준의 라미닌 수용체 발현을 가진 여러 종양 세포주를 사용하였다.
4. 생체 내(in vivo) 자극 분석
활발히 성장하는 종양을 치료하기 전에, VGP/NY-ESO-1을 사용하여 생체 내 종양-특이적 면역 반응을 유도하는 것이 중요하다. 정상 마우스는 NY-ESO-1을 만나지 않았으며 면역계에 의해 외래 항원으로 인식된다. 복강(ip) 주사에 의한 VGP/NY-ESO-1의 마우스의 면역화는 NK 세포 활성화 뿐만 아니라 융합 단백질-특이적 T 세포 뿐만 아니라 NY-ESO-1-특이적 T 세포의 활성화 및 증식을 야기한다. 이 치료법의 효과를 입증하기 위해, VGP/NY-ESO-1은 VGP 단독, NY-ESO-1 단독 및 항-DC-SIGN/NY-ESO-1(대조군)보다 더 큰 면역원성을 나타낸다. 체크 포인트 억제제 항 -CTLA-4 및 PD-1은 강력한 면역요법의 잠재력을 나타내며, 더 강한 면역 반응을 위해 상기 기재된 치료법과 상승 작용한다. 이러한 차단 항체의 공동 투여를 사용하거나 사용하지 않고 본원에 기재된 치료의 효과를 평가하였다.
공지된 MHC 결합 선호에 기초하여, NY-ESO-1 및 VGP로부터의 에피토프는 특정 마우스 종의 MHC 분자에 의해 표시된다. 대안적으로, NY-ESO-1 에피토프가 알려져 있는 인간 MHC 분자를 발현하는 유전자 이식(transgenic) 마우스를 사용할 수 있다. 면역 자극을 확인하기 위해, 혈액, 비장 및 배액 림프절의 샘플을 채취한다. MHC 테트라머 염색은 NY-ESO-1 및 VGP-특이적 T 세포의 확대된 집단의 존재를 확인하는데 사용된다. 이들 세포는 나이브 마우스(naive mice)에서 존재하지만, 검출 한계치보다 적은 양으로 존재한다. 성공적인 면역화에서, 이들 세포는 증식하고 유동 세포 계측법에 의해 쉽게 검출될 수 있다. 게다가, 유동 세포 계측법은 각각 순수한 세포 및 활성화된 세포에만 존재하는 CD62L 및 CD69와 같은 표면 마커를 조사하여 이들 테트라머+ 세포의 활성화 상태를 분석하는 데 사용된다. VGP-특이적 T 세포의 활성화는 부정확한 효과(off-target effect)로 간주되는 반면, 이러한 항원이 종양 자체에 표적이 될 수 있기 때문에 종양에 대한 면역 반응을 더 향상시킨다.
엘리스팟(ELISPOT) 분석법은 NY-ESO-1-특이적 T세포가 이펙터(effector) 기능을 가지고 있는지 결정하는데 사용된다. 면역화된 마우스의 비장 및 림프절로부터 수확된 CD8+ T세포를 NY-ESO-1로 미리 로딩된 항원-표시 세포와 함께 배양한다. 이에 반응하여, 이러한 에피토프에 특이적인 활성화된 T 세포는, 검출을 위해 웰의 바닥을 코팅하는 항체에 의해 포획되는 IFNγ와 같은 사이토카인을 생성한다. 이러한 활성화 된 T 세포의 상기 이펙터 기능은 세포 독성 분석법을 실시하여 분석하였다. ELISPOT 분석과 유사하게, 면역화된 마우스로부터의 CD8+ T 세포를 관련 펩타이드로 미리 로딩된 항원-표시 세포와 함께 배양한다. 대안적으로, NY-ESO-1을 발현시키기 위해 렌티바이러스(lentivirus)로 형질전환된 동족 마우스 세포주를 사용한다. 활성화된 CD8+ CTL은 이들 NY-ESO-1-표시 세포를 직접 사멸시키고, 세포 독성은 상층액 내의 젖산 탈수소효소(lactate dehydrogenase)와 같이 용출된 세포로부터 세포 내 단백질의 검출로 측정한다.
유동 세포 계측법에 의해 수행될 수 있는 다른 면역 세포 집단에서 치료의 효과를 분석한다. 구체적으로, 전체 세포 수 뿐만 아니라, 서로 관련되어 있는 여러 면역 세포 유형(CD4+ 및 CD8+ T 세포, DC, NK 세포, B세포, 대식세포)의 비율에 대한 치료 효과를 분석한다. 재조합 단백질에 대하여 마우스에 의해 생성된 항체는 혈청을 분석함으로써 평가된다. 혈장 세포는 NY-ESO-1 및 VGP에 특이적인 항체를 생성한다. 특정 실시양태에서, 다중 투여가 투여될 때, 이들 항체는 치료의 효과를 방해할 수 있다. 특정 실시양태에서, 이러한 항원은 항원성을 크게 만드는 종양 자체를 표적으로 하여 상기 항체는 종양 제거를 돕는다.
종양 모델로 진행하기 전에 강력한 항-종양 면역 반응을 생성하기 위해 적절한 투여 전략(단백질 양, 투여 횟수, 투여 빈도)을 조사한다. 게다가, ELISA는 마우스 혈청 및 조직에서 VGP를 검출하여 생체 내에서 단백질 교환 및 안정성뿐 아니라 투약을 평가하기 위해 개발된다.
T세포를 적절하게 활성화시키기 위해, DC는 병원체-관련 분자 패턴(PAMPs)의 검출을 통해 활성화된다. 특정 실시양태에서, VGP/NY-ESO-1은 면역원성을 증가시키기 위해 보조제와 결합한다.
[인용문헌]
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본 발명은 본원에 기재된 특정 실시양태에 의해 그 범위가 제한되지 않는다. 실제로, 상기 내용 이외에 본 발명에 추가하는 발명의 다양한 변형은 전술한 설명 및 수반하는 도면으로부터 당업자에게 명백할 것이다. 이러한 변형은 첨부된 청구 범위의 범주 내에 속한다.
특허, 특허 출원 및 출판물이 본 출원 전반에 걸쳐 인용되며, 특히 모든 개시된 화학 구조를 포함하는 그 개시 내용이 본 발명에 참고로 인용된다. 상기 공보 또는 문헌의 인용은 전술한 것들 중 위의 간행물 또는 문서의 인용은 앞서 언급한 내용 중 어느 하나가 관련 선행 기술임을 인정하는 것이 아니며, 또한 본 간행물 또는 문서의 내용이나 날짜에 대한 인정으로 여겨지지 않는다. 본 발명에 인용된 모든 참고 문헌은 각각의 개별 간행물, 특허 출원 또는 특허가 구체적으로 및 개별적으로 참조로 포함된 것과 동일한 범위로 참고 문헌으로 인용된다.
상기 전술한 명세서는 당업자에게 본 발명을 실시할 수 있게 하기에 충분하다고 여겨진다. 본원에서 보여지고 묘사된 것 이외의 본 발명의 다양한 변형은, 전술한 설명으로부터 당업자에게 명백할 것이며 첨부된 청구 범위의 범주 내에 속할 것이다.
<110> OMNICYTE
<120> FUSION PROTEINS COMPRISING MODIFIED ALPHA VIRUS SURFACE
GLYCOPROTEINS AND TUMOR ASSOCIATED ANTIGEN AND METHODS THEREOF
<130> IP17-0021
<150> PCT/US 2016/023203
<151> 2016-03-18
<150> US 62/134,933
<151> 2015-03-18
<160> 15
<170> KoPatentIn 3.0
<210> 1
<211> 984
<212> PRT
<213> Artificial Sequence
<220>
<223> Synthetic: E3-E2-link-E1-TEV-link-NY-ESO-1-6X His
<400> 1
Met Ser Ala Ala Pro Leu Val Thr Ala Met Cys Leu Leu Gly Asn Val
1 5 10 15
Ser Phe Pro Cys Asp Arg Pro Pro Thr Cys Tyr Thr Arg Glu Pro Ser
20 25 30
Arg Ala Leu Asp Ile Leu Glu Glu Asn Val Asn His Glu Ala Tyr Asp
35 40 45
Thr Leu Leu Asn Ala Ile Leu Arg Cys Gly Ser Ser Gly Arg Ser Lys
50 55 60
Arg Ser Val Ile Asp Asp Phe Thr Leu Thr Ser Pro Tyr Leu Gly Thr
65 70 75 80
Cys Ser Tyr Cys His His Thr Val Pro Cys Phe Ser Pro Val Lys Ile
85 90 95
Glu Gln Val Trp Asp Glu Ala Asp Asp Asn Thr Ile Arg Ile Gln Thr
100 105 110
Ser Ala Gln Phe Gly Tyr Asp Gln Ser Gly Ala Ala Ser Ala Asn Lys
115 120 125
Tyr Arg Tyr Met Ser Leu Lys Gln Asp His Thr Val Lys Glu Gly Thr
130 135 140
Met Asp Asp Ile Lys Ile Ser Thr Ser Gly Pro Cys Arg Arg Leu Ser
145 150 155 160
Tyr Lys Gly Tyr Phe Leu Leu Ala Lys Cys Pro Pro Gly Asp Ser Val
165 170 175
Thr Val Ser Ile Val Ser Ser Asn Ser Ala Thr Ser Cys Thr Leu Ala
180 185 190
Arg Lys Ile Lys Pro Lys Phe Val Gly Arg Glu Lys Tyr Asp Leu Pro
195 200 205
Pro Val His Gly Lys Lys Ile Pro Cys Thr Val Tyr Asp Arg Leu Lys
210 215 220
Glu Thr Thr Ala Gly Tyr Ile Thr Met His Arg Pro Arg Pro His Ala
225 230 235 240
Tyr Thr Ser Tyr Leu Glu Glu Ser Ser Gly Lys Val Tyr Ala Lys Pro
245 250 255
Pro Ser Gly Lys Asn Ile Thr Tyr Glu Cys Lys Cys Gly Asp Tyr Lys
260 265 270
Thr Gly Thr Val Ser Thr Arg Thr Glu Ile Thr Gly Cys Thr Ala Ile
275 280 285
Lys Gln Cys Val Ala Tyr Lys Ser Asp Gln Thr Lys Trp Val Phe Asn
290 295 300
Ser Pro Asp Leu Ile Arg His Asp Asp His Thr Ala Gln Gly Lys Leu
305 310 315 320
His Leu Pro Phe Lys Leu Ile Pro Ser Thr Cys Met Val Pro Val Ala
325 330 335
His Ala Pro Asn Val Ile His Gly Phe Lys His Ile Ser Leu Gln Leu
340 345 350
Asp Thr Asp His Leu Thr Leu Leu Thr Thr Arg Arg Leu Gly Ala Asn
355 360 365
Pro Glu Pro Thr Thr Glu Trp Ile Val Gly Lys Thr Val Arg Asn Phe
370 375 380
Thr Val Asp Arg Asp Gly Leu Glu Tyr Ile Trp Gly Asn His Glu Pro
385 390 395 400
Val Arg Val Tyr Ala Gln Glu Ser Ala Pro Gly Asp Pro His Gly Trp
405 410 415
Pro His Glu Ile Val Gln His Tyr Tyr His Arg His Pro Gly Gly Gly
420 425 430
Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly
435 440 445
Tyr Glu His Ala Thr Thr Val Pro Asn Val Pro Gln Ile Pro Tyr Lys
450 455 460
Ala Leu Val Glu Arg Ala Gly Tyr Ala Pro Leu Asn Leu Glu Ile Thr
465 470 475 480
Val Met Ser Ser Glu Val Leu Pro Ser Thr Asn Gln Glu Tyr Ile Thr
485 490 495
Cys Lys Phe Thr Thr Val Val Pro Ser Pro Lys Ile Lys Cys Cys Gly
500 505 510
Ser Leu Glu Cys Gln Pro Ala Ala His Ala Asp Tyr Thr Cys Lys Val
515 520 525
Phe Gly Gly Val Tyr Pro Phe Met Trp Gly Gly Ala Gln Cys Phe Cys
530 535 540
Asp Ser Glu Asn Ser Gln Met Ser Glu Ala Tyr Val Glu Leu Ser Ala
545 550 555 560
Asp Cys Ala Ser Asp His Ala Gln Ala Ile Lys Val His Thr Ala Ala
565 570 575
Met Lys Val Gly Leu Arg Ile Val Tyr Gly Asn Thr Thr Ser Phe Leu
580 585 590
Asp Val Tyr Val Asn Gly Val Thr Pro Gly Thr Ser Lys Asp Leu Lys
595 600 605
Val Ile Ala Gly Pro Ile Ser Ala Ser Phe Thr Pro Phe Asp His Lys
610 615 620
Val Val Ile His Arg Gly Leu Val Tyr Asn Tyr Asp Phe Pro Glu Tyr
625 630 635 640
Gly Ala Met Lys Pro Gly Ala Phe Gly Asp Ile Gln Ala Thr Ser Leu
645 650 655
Thr Ser Lys Asp Leu Ile Ala Ser Thr Asp Ile Arg Leu Leu Lys Pro
660 665 670
Ser Ala Lys Asn Val His Val Pro Tyr Thr Gln Ala Ser Ser Gly Phe
675 680 685
Glu Met Trp Lys Asn Asn Ser Gly Arg Pro Leu Gln Glu Thr Ala Pro
690 695 700
Phe Gly Cys Lys Ile Ala Val Asn Pro Leu Arg Ala Val Asp Cys Ser
705 710 715 720
Tyr Gly Asn Ile Pro Ile Ser Ile Asp Ile Pro Asn Ala Ala Phe Ile
725 730 735
Arg Thr Ser Asp Ala Pro Leu Val Ser Thr Val Lys Cys Glu Val Ser
740 745 750
Glu Cys Thr Tyr Ser Ala Asp Phe Gly Gly Met Ala Thr Leu Gln Tyr
755 760 765
Val Ser Asp Arg Glu Gly Gln Cys Pro Val His Ser His Ser Ser Thr
770 775 780
Ala Thr Leu Gln Glu Ser Thr Val His Val Leu Glu Lys Gly Ala Val
785 790 795 800
Thr Val His Phe Ser Thr Ala Ser Pro Gln Ala Asn Phe Ile Val Ser
805 810 815
Leu Cys Gly Lys Lys Thr Thr Cys Asn Ala Glu Cys Lys Pro Pro Ala
820 825 830
Asp His Ile Val Ser Thr Pro His Lys Asn Asp Gln Glu Phe Gln Ala
835 840 845
Ala Ile Ser Lys Thr Ser Glu Asn Leu Tyr Phe Gln Gly Gly Gly Gly
850 855 860
Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Ala Arg Gly
865 870 875 880
Pro Glu Ser Arg Leu Leu Glu Phe Tyr Leu Ala Met Pro Phe Ala Thr
885 890 895
Pro Met Glu Ala Glu Leu Ala Arg Arg Ser Leu Ala Gln Asp Ala Pro
900 905 910
Pro Leu Pro Val Pro Gly Val Leu Leu Lys Glu Phe Thr Val Ser Gly
915 920 925
Asn Ile Leu Thr Ile Arg Leu Thr Ala Ala Asp His Arg Gln Leu Gln
930 935 940
Leu Ser Ile Ser Ser Cys Leu Gln Gln Leu Ser Leu Leu Met Trp Ile
945 950 955 960
Thr Gln Cys Phe Leu Pro Val Phe Leu Ala Gln Pro Pro Ser Gly Gln
965 970 975
Arg Arg His His His His His His
980
<210> 2
<211> 2952
<212> DNA
<213> Artificial Sequence
<220>
<223> Synthetic construct
<400> 2
atgtcagccg ctccactcgt cactgctatg tgcctgctcg gtaacgtcag cttcccttgc 60
gacagacccc caacttgcta cactcgtgag ccatctaggg ctctcgatat cttggaggaa 120
aacgtgaacc acgaggctta cgacaccctg ctcaacgcca tcctgagatg cggatccagc 180
ggtcgctcca agcgtagcgt gattgacgat ttcacactca cgtcgcctta cttgggtacc 240
tgctcctact gtcaccatac tgtcccgtgt ttctcacctg tcaagatcga gcaggtttgg 300
gacgaagcag acgataacac aatccgcatt cagacgagcg ctcaattcgg ttacgatcag 360
agcggcgctg cctctgctaa caaataccgt tacatgtctc tcaaacaaga ccacaccgtc 420
aaggagggca ctatggacga tatcaagatt tctacttcag gaccttgccg ccgtctgtct 480
tacaaaggtt acttcttgct ggctaagtgt cctcccggag actcagtcac agttagtatc 540
gtctcttcaa actctgcaac atcatgcacg ctggcgcgca agattaaacc aaagttcgtt 600
ggccgtgaga aatacgacct cccaccggtg cacggaaaga aaatcccttg taccgtctac 660
gatcgtttga aggaaaccac tgccggctac attaccatgc acaggccaag accgcatgct 720
tacactagtt acctggaaga aagttcgggc aaagtgtacg ccaagcctcc ctcgggaaag 780
aacatcacat acgagtgcaa atgtggagac tacaagaccg gtactgtcag cacaaggacg 840
gaaatcaccg gttgcactgc tattaagcag tgtgtcgcct acaaatcgga ccaaactaag 900
tgggttttca actcccccga tctgatcaga cacgacgatc atactgccca gggaaaattg 960
cacctgccgt tcaagctcat tccttcaaca tgcatggtgc ccgtcgctca tgccccaaac 1020
gtgatccacg gtttcaagca tattagtctc caattggaca cagatcacct cacgctcttg 1080
acaacgagga gattgggagc taaccctgag cccaccactg aatggatcgt gggcaagaca 1140
gtccgcaact tcacggtgga ccgtgatggc ctggagtaca tctggggaaa ccacgaacca 1200
gttcgcgtgt acgctcagga gtccgcacca ggagacccac acggttggcc acatgaaatc 1260
gtccaacatt actaccaccg tcatcctggt ggaggaggtt cgggaggagg tggatccgga 1320
ggtggcggaa gcggtggcgg aggttacgag cacgctacaa cggtgcctaa cgtcccccag 1380
atcccataca aggccttggt ggaaagagct ggatacgcac cactgaacct cgagatcacc 1440
gtgatgtcca gcgaagtcct gccaagcaca aaccaggagt acatcacgtg caagttcacc 1500
actgtggtcc catcaccgaa aattaagtgc tgtggtagtc tggaatgcca acctgcagcg 1560
cacgctgact acacttgtaa ggttttcggc ggagtgtacc ccttcatgtg gggtggcgct 1620
cagtgcttct gtgacagtga gaactcgcaa atgtccgagg cttacgttga actgtctgca 1680
gactgcgcgt cagatcacgc acaggcgatc aaagtgcata ccgctgccat gaaggttggt 1740
ttgcgcattg tgtacggcaa cacaacgtct ttcctggatg tctacgttaa cggcgtgaca 1800
cctggaacgt caaaagacct gaaggtcatc gcaggcccga ttagtgcgtc gttcactcct 1860
ttcgatcaca aggttgtgat ccataggggt ctcgtgtaca actacgactt ccccgaatac 1920
ggcgctatga aaccaggcgc cttcggagat atccaagcaa ccagcctgac ttctaaggac 1980
ctcatcgcga gcacagatat tcgtctgctc aaaccgtctg ctaagaacgt gcacgtcccc 2040
tacacccagg cctcttcagg tttcgagatg tggaaaaaca actccggcag gccgctccaa 2100
gaaaccgctc ctttcggctg caagatcgca gtcaacccct tgagagcggt tgactgtagc 2160
tacggaaaca tccccatttc tatcgatatt ccaaacgcag cgttcatccg cacatcagac 2220
gccccactcg ttagtacggt gaagtgcgag gtcagtgaat gtacatactc ggctgatttc 2280
ggtggtatgg ccacgttgca gtacgtttcg gaccgtgagg gtcaatgccc tgtgcactcc 2340
catagttcga ccgccactct gcaggagagc accgttcacg tgctcgaaaa gggtgctgtc 2400
accgttcatt tctcaactgc aagtcctcaa gcgaacttca tcgtgtctct ctgcggcaag 2460
aaaaccactt gcaacgcaga gtgtaagcca ccggcggacc acatcgtctc aaccccccat 2520
aaaaacgatc aggagttcca agctgccatt tcgaagactt ccgaaaacct gtacttccag 2580
ggaggaggtg gaggatccgg tggaggaggt agcggaggag gtggatctgg tgctagggga 2640
ccagagtcca gattgctgga gttctacttg gctatgccct tcgccacccc aatggaggct 2700
gaattggcaa gacgttccct ggcacaagac gcacctccac tgcctgtccc cggagttctc 2760
ttgaaggagt tcactgtgag cggtaacatc ttgaccatta ggctgactgc agcggaccac 2820
agacagttgc aactgtcaat ctccagctgc ctgcagcaac tcagtctgct catgtggatt 2880
acccagtgtt tcttgccagt tttcctcgct caacccccct cgggacagag aagacaccat 2940
catcatcatc at 2952
<210> 3
<211> 449
<212> PRT
<213> Artificial Sequence
<220>
<223> WT1 - Wilms tumor protein
<400> 3
Met Gly Ser Asp Val Arg Asp Leu Asn Ala Leu Leu Pro Ala Val Pro
1 5 10 15
Ser Leu Gly Gly Gly Gly Gly Cys Ala Leu Pro Val Ser Gly Ala Ala
20 25 30
Gln Trp Ala Pro Val Leu Asp Phe Ala Pro Pro Gly Ala Ser Ala Tyr
35 40 45
Gly Ser Leu Gly Gly Pro Ala Pro Pro Pro Ala Pro Pro Pro Pro Pro
50 55 60
Pro Pro Pro Pro His Ser Phe Ile Lys Gln Glu Pro Ser Trp Gly Gly
65 70 75 80
Ala Glu Pro His Glu Glu Gln Cys Leu Ser Ala Phe Thr Val His Phe
85 90 95
Ser Gly Gln Phe Thr Gly Thr Ala Gly Ala Cys Arg Tyr Gly Pro Phe
100 105 110
Gly Pro Pro Pro Pro Ser Gln Ala Ser Ser Gly Gln Ala Arg Met Phe
115 120 125
Pro Asn Ala Pro Tyr Leu Pro Ser Cys Leu Glu Ser Gln Pro Ala Ile
130 135 140
Arg Asn Gln Gly Tyr Ser Thr Val Thr Phe Asp Gly Thr Pro Ser Tyr
145 150 155 160
Gly His Thr Pro Ser His His Ala Ala Gln Phe Pro Asn His Ser Phe
165 170 175
Lys His Glu Asp Pro Met Gly Gln Gln Gly Ser Leu Gly Glu Gln Gln
180 185 190
Tyr Ser Val Pro Pro Pro Val Tyr Gly Cys His Thr Pro Thr Asp Ser
195 200 205
Cys Thr Gly Ser Gln Ala Leu Leu Leu Arg Thr Pro Tyr Ser Ser Asp
210 215 220
Asn Leu Tyr Gln Met Thr Ser Gln Leu Glu Cys Met Thr Trp Asn Gln
225 230 235 240
Met Asn Leu Gly Ala Thr Leu Lys Gly Val Ala Ala Gly Ser Ser Ser
245 250 255
Ser Val Lys Trp Thr Glu Gly Gln Ser Asn His Ser Thr Gly Tyr Glu
260 265 270
Ser Asp Asn His Thr Thr Pro Ile Leu Cys Gly Ala Gln Tyr Arg Ile
275 280 285
His Thr His Gly Val Phe Arg Gly Ile Gln Asp Val Arg Arg Val Pro
290 295 300
Gly Val Ala Pro Thr Leu Val Arg Ser Ala Ser Glu Thr Ser Glu Lys
305 310 315 320
Arg Pro Phe Met Cys Ala Tyr Pro Gly Cys Asn Lys Arg Tyr Phe Lys
325 330 335
Leu Ser His Leu Gln Met His Ser Arg Lys His Thr Gly Glu Lys Pro
340 345 350
Tyr Gln Cys Asp Phe Lys Asp Cys Glu Arg Arg Phe Ser Arg Ser Asp
355 360 365
Gln Leu Lys Arg His Gln Arg Arg His Thr Gly Val Lys Pro Phe Gln
370 375 380
Cys Lys Thr Cys Gln Arg Lys Phe Ser Arg Ser Asp His Leu Lys Thr
385 390 395 400
His Thr Arg Thr His Thr Gly Lys Thr Ser Glu Lys Pro Phe Ser Cys
405 410 415
Arg Trp Pro Ser Cys Gln Lys Lys Phe Ala Arg Ser Asp Glu Leu Val
420 425 430
Arg His His Asn Met His Gln Arg Asn Met Thr Lys Leu Gln Leu Ala
435 440 445
Leu
<210> 4
<211> 1255
<212> PRT
<213> Artificial Sequence
<220>
<223> Mucin-1 (MUC1)
<400> 4
Met Thr Pro Gly Thr Gln Ser Pro Phe Phe Leu Leu Leu Leu Leu Thr
1 5 10 15
Val Leu Thr Val Val Thr Gly Ser Gly His Ala Ser Ser Thr Pro Gly
20 25 30
Gly Glu Lys Glu Thr Ser Ala Thr Gln Arg Ser Ser Val Pro Ser Ser
35 40 45
Thr Glu Lys Asn Ala Val Ser Met Thr Ser Ser Val Leu Ser Ser His
50 55 60
Ser Pro Gly Ser Gly Ser Ser Thr Thr Gln Gly Gln Asp Val Thr Leu
65 70 75 80
Ala Pro Ala Thr Glu Pro Ala Ser Gly Ser Ala Ala Thr Trp Gly Gln
85 90 95
Asp Val Thr Ser Val Pro Val Thr Arg Pro Ala Leu Gly Ser Thr Thr
100 105 110
Pro Pro Ala His Asp Val Thr Ser Ala Pro Asp Asn Lys Pro Ala Pro
115 120 125
Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr
130 135 140
Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser
145 150 155 160
Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His
165 170 175
Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala
180 185 190
Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro
195 200 205
Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr
210 215 220
Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser
225 230 235 240
Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His
245 250 255
Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala
260 265 270
Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro
275 280 285
Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr
290 295 300
Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser
305 310 315 320
Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His
325 330 335
Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala
340 345 350
Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro
355 360 365
Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr
370 375 380
Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser
385 390 395 400
Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His
405 410 415
Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala
420 425 430
Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro
435 440 445
Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr
450 455 460
Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser
465 470 475 480
Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His
485 490 495
Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala
500 505 510
Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro
515 520 525
Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr
530 535 540
Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser
545 550 555 560
Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His
565 570 575
Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala
580 585 590
Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro
595 600 605
Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr
610 615 620
Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser
625 630 635 640
Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His
645 650 655
Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala
660 665 670
Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro
675 680 685
Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr
690 695 700
Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser
705 710 715 720
Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His
725 730 735
Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala
740 745 750
Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro
755 760 765
Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr
770 775 780
Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser
785 790 795 800
Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His
805 810 815
Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala
820 825 830
Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro
835 840 845
Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr
850 855 860
Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser
865 870 875 880
Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala Pro Pro Ala His
885 890 895
Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro Gly Ser Thr Ala
900 905 910
Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Thr Arg Pro Ala Pro
915 920 925
Gly Ser Thr Ala Pro Pro Ala His Gly Val Thr Ser Ala Pro Asp Asn
930 935 940
Arg Pro Ala Leu Gly Ser Thr Ala Pro Pro Val His Asn Val Thr Ser
945 950 955 960
Ala Ser Gly Ser Ala Ser Gly Ser Ala Ser Thr Leu Val His Asn Gly
965 970 975
Thr Ser Ala Arg Ala Thr Thr Thr Pro Ala Ser Lys Ser Thr Pro Phe
980 985 990
Ser Ile Pro Ser His His Ser Asp Thr Pro Thr Thr Leu Ala Ser His
995 1000 1005
Ser Thr Lys Thr Asp Ala Ser Ser Thr His His Ser Ser Val Pro Pro
1010 1015 1020
Leu Thr Ser Ser Asn His Ser Thr Ser Pro Gln Leu Ser Thr Gly Val
1025 1030 1035 1040
Ser Phe Phe Phe Leu Ser Phe His Ile Ser Asn Leu Gln Phe Asn Ser
1045 1050 1055
Ser Leu Glu Asp Pro Ser Thr Asp Tyr Tyr Gln Glu Leu Gln Arg Asp
1060 1065 1070
Ile Ser Glu Met Phe Leu Gln Ile Tyr Lys Gln Gly Gly Phe Leu Gly
1075 1080 1085
Leu Ser Asn Ile Lys Phe Arg Pro Gly Ser Val Val Val Gln Leu Thr
1090 1095 1100
Leu Ala Phe Arg Glu Gly Thr Ile Asn Val His Asp Val Glu Thr Gln
1105 1110 1115 1120
Phe Asn Gln Tyr Lys Thr Glu Ala Ala Ser Arg Tyr Asn Leu Thr Ile
1125 1130 1135
Ser Asp Val Ser Val Ser Asp Val Pro Phe Pro Phe Ser Ala Gln Ser
1140 1145 1150
Gly Ala Gly Val Pro Gly Trp Gly Ile Ala Leu Leu Val Leu Val Cys
1155 1160 1165
Val Leu Val Ala Leu Ala Ile Val Tyr Leu Ile Ala Leu Ala Val Cys
1170 1175 1180
Gln Cys Arg Arg Lys Asn Tyr Gly Gln Leu Asp Ile Phe Pro Ala Arg
1185 1190 1195 1200
Asp Thr Tyr His Pro Met Ser Glu Tyr Pro Thr Tyr His Thr His Gly
1205 1210 1215
Arg Tyr Val Pro Pro Ser Ser Thr Asp Arg Ser Pro Tyr Glu Lys Val
1220 1225 1230
Ser Ala Gly Asn Gly Gly Ser Ser Leu Ser Tyr Thr Asn Pro Ala Val
1235 1240 1245
Ala Ala Thr Ser Ala Asn Leu
1250 1255
<210> 5
<211> 497
<212> PRT
<213> Artificial Sequence
<220>
<223> Latent membrane protein 2 (LMP2)
<400> 5
Met Gly Ser Leu Glu Met Val Pro Met Gly Ala Gly Pro Pro Ser Pro
1 5 10 15
Gly Gly Asp Pro Asp Gly Tyr Asp Gly Gly Asn Asn Ser Gln Tyr Pro
20 25 30
Ser Ala Ser Gly Ser Ser Gly Asn Thr Pro Thr Pro Pro Asn Asp Glu
35 40 45
Glu Arg Glu Ser Asn Glu Glu Pro Pro Pro Pro Tyr Glu Asp Pro Tyr
50 55 60
Trp Gly Asn Gly Asp Arg His Ser Asp Tyr Gln Pro Leu Gly Thr Gln
65 70 75 80
Asp Gln Ser Leu Tyr Leu Gly Leu Gln His Asp Gly Asn Asp Gly Leu
85 90 95
Pro Pro Pro Pro Tyr Ser Pro Arg Asp Asp Ser Ser Gln His Ile Tyr
100 105 110
Glu Glu Ala Gly Arg Gly Ser Met Asn Pro Val Cys Leu Pro Val Ile
115 120 125
Val Ala Pro Tyr Leu Phe Trp Leu Ala Ala Ile Ala Ala Ser Cys Phe
130 135 140
Thr Ala Ser Val Ser Thr Val Val Thr Ala Thr Gly Leu Ala Leu Ser
145 150 155 160
Leu Leu Leu Leu Ala Ala Val Ala Ser Ser Tyr Ala Ala Ala Gln Arg
165 170 175
Lys Leu Leu Thr Pro Val Thr Val Leu Thr Ala Val Val Thr Phe Phe
180 185 190
Ala Ile Cys Leu Thr Trp Arg Ile Glu Asp Pro Pro Phe Asn Ser Leu
195 200 205
Leu Phe Ala Leu Leu Ala Ala Ala Gly Gly Leu Gln Gly Ile Tyr Val
210 215 220
Leu Val Met Leu Val Leu Leu Ile Leu Ala Tyr Arg Arg Arg Trp Arg
225 230 235 240
Arg Leu Thr Val Cys Gly Gly Ile Met Phe Leu Ala Cys Val Leu Val
245 250 255
Leu Ile Val Asp Ala Val Leu Gln Leu Ser Pro Leu Leu Gly Ala Val
260 265 270
Thr Val Val Ser Met Thr Leu Leu Leu Leu Ala Phe Val Leu Trp Leu
275 280 285
Ser Ser Pro Gly Gly Leu Gly Thr Leu Gly Ala Ala Leu Leu Thr Leu
290 295 300
Ala Ala Ala Leu Ala Leu Leu Ala Ser Leu Ile Leu Gly Thr Leu Asn
305 310 315 320
Leu Thr Thr Met Phe Leu Leu Met Leu Leu Trp Thr Leu Val Val Leu
325 330 335
Leu Ile Cys Ser Ser Cys Ser Ser Cys Pro Leu Ser Lys Ile Leu Leu
340 345 350
Ala Arg Leu Phe Leu Tyr Ala Leu Ala Leu Leu Leu Leu Ala Ser Ala
355 360 365
Leu Ile Ala Gly Gly Ser Ile Leu Gln Thr Asn Phe Lys Ser Leu Ser
370 375 380
Ser Thr Glu Phe Ile Pro Asn Leu Phe Cys Met Leu Leu Leu Ile Val
385 390 395 400
Ala Gly Ile Leu Phe Ile Leu Ala Ile Leu Thr Glu Trp Gly Ser Gly
405 410 415
Asn Arg Thr Tyr Gly Pro Val Phe Met Cys Leu Gly Gly Leu Leu Thr
420 425 430
Met Val Ala Gly Ala Val Trp Leu Thr Val Met Ser Asn Thr Leu Leu
435 440 445
Ser Ala Trp Ile Leu Thr Ala Gly Phe Leu Ile Phe Leu Ile Gly Phe
450 455 460
Ala Leu Phe Gly Val Ile Arg Cys Cys Arg Tyr Cys Cys Tyr Tyr Cys
465 470 475 480
Leu Thr Leu Glu Ser Glu Glu Arg Pro Pro Thr Pro Tyr Arg Asn Thr
485 490 495
Val
<210> 6
<211> 158
<212> PRT
<213> Artificial Sequence
<220>
<223> Human papillomavirus type 16 Protein E6
<400> 6
Met His Gln Lys Arg Thr Ala Met Phe Gln Asp Pro Gln Glu Arg Pro
1 5 10 15
Arg Lys Leu Pro Gln Leu Cys Thr Glu Leu Gln Thr Thr Ile His Asp
20 25 30
Ile Ile Leu Glu Cys Val Tyr Cys Lys Gln Gln Leu Leu Arg Arg Glu
35 40 45
Val Tyr Asp Phe Ala Phe Arg Asp Leu Cys Ile Val Tyr Arg Asp Gly
50 55 60
Asn Pro Tyr Ala Val Cys Asp Lys Cys Leu Lys Phe Tyr Ser Lys Ile
65 70 75 80
Ser Glu Tyr Arg His Tyr Cys Tyr Ser Leu Tyr Gly Thr Thr Leu Glu
85 90 95
Gln Gln Tyr Asn Lys Pro Leu Cys Asp Leu Leu Ile Arg Cys Ile Asn
100 105 110
Cys Gln Lys Pro Leu Cys Pro Glu Glu Lys Gln Arg His Leu Asp Lys
115 120 125
Lys Gln Arg Phe His Asn Ile Arg Gly Arg Trp Thr Gly Arg Cys Met
130 135 140
Ser Cys Cys Arg Ser Ser Arg Thr Arg Arg Glu Thr Gln Leu
145 150 155
<210> 7
<211> 96
<212> PRT
<213> Artificial Sequence
<220>
<223> Human papillomavirus type 16 Protein E7
<400> 7
Met His Gly Asp Thr Pro Thr Leu His Glu Tyr Met Leu Asp Leu Gln
1 5 10 15
Pro Glu Thr Thr Asp Leu Tyr Cys Tyr Glu Gln Leu Asn Asp Ser Ser
20 25 30
Glu Glu Glu Asp Glu Ile Asp Gly Pro Ala Gly Gln Ala Glu Pro Asp
35 40 45
Arg Ala His Tyr Asn Ile Val Thr Phe Cys Cys Lys Cys Asp Ser Thr
50 55 60
Leu Arg Leu Cys Val Gln Ser Thr His Val Asp Ile Arg Thr Leu Glu
65 70 75 80
Asp Leu Leu Met Gly Thr Leu Gly Ile Val Cys Pro Ile Cys Ser Gln
85 90 95
<210> 8
<211> 150
<212> PRT
<213> Artificial Sequence
<220>
<223> Human papillomavirus type 18 Protein E6
<400> 8
Met Ala Arg Phe Glu Asp Pro Thr Arg Arg Pro Tyr Lys Leu Pro Asp
1 5 10 15
Leu Cys Thr Glu Leu Asn Thr Ser Leu Gln Asp Ile Glu Ile Thr Cys
20 25 30
Val Tyr Cys Lys Thr Val Leu Glu Leu Thr Glu Val Phe Glu Phe Ala
35 40 45
Phe Lys Asp Leu Phe Val Val Tyr Arg Asp Ser Ile Pro His Ala Ala
50 55 60
Cys His Lys Cys Ile Asp Phe Tyr Ser Arg Ile Arg Glu Leu Arg His
65 70 75 80
Tyr Ser Asp Ser Val Tyr Gly Asp Thr Leu Glu Lys Leu Thr Asn Thr
85 90 95
Gly Leu Tyr Asn Leu Leu Ile Arg Cys Leu Arg Cys Gln Lys Pro Leu
100 105 110
Asn Pro Ala Glu Lys Leu Arg His Leu Asn Glu Lys Arg Arg Phe His
115 120 125
Asn Ile Ala Gly His Tyr Arg Gly Gln Cys His Ser Cys Cys Asn Arg
130 135 140
Ala Arg Gln Glu Arg Leu
145 150
<210> 9
<211> 105
<212> PRT
<213> Artificial Sequence
<220>
<223> Human papillomavirus type 18 Protein E7
<400> 9
Met His Gly Pro Lys Ala Thr Leu Gln Asp Ile Val Leu His Leu Glu
1 5 10 15
Pro Gln Asn Glu Ile Pro Val Asp Leu Leu Cys His Glu Gln Leu Ser
20 25 30
Asp Ser Glu Glu Glu Asn Asp Glu Ile Asp Gly Val Asn His Gln His
35 40 45
Leu Pro Ala Arg Arg Ala Glu Pro Gln Arg His Thr Met Leu Cys Met
50 55 60
Cys Cys Lys Cys Glu Ala Arg Ile Lys Leu Val Val Glu Ser Ser Ala
65 70 75 80
Asp Asp Leu Arg Ala Phe Gln Gln Leu Phe Leu Asn Thr Leu Ser Phe
85 90 95
Val Cys Pro Trp Cys Ala Ser Gln Gln
100 105
<210> 10
<211> 473
<212> PRT
<213> Artificial Sequence
<220>
<223> Ral-GDS-related protein (RGL4)
<400> 10
Met Arg Lys Leu Leu Thr Asn Leu Pro Ala Ala Ala Val Leu Ser Ala
1 5 10 15
Gln Val Tyr Ser Ala Val Leu Gln Gly Leu Trp Glu Glu Asn Val Cys
20 25 30
Gly Thr Pro Gly Arg Thr Arg Val Cys Thr Ala Leu Leu Tyr Gly Gln
35 40 45
Val Cys Pro Phe Gln Asp Ser Thr Asp Gly Leu Arg Thr Ile Thr Ser
50 55 60
Ile Leu Phe Asn Trp Pro Pro Glu Asn Thr Ser Val Tyr Tyr Gln Pro
65 70 75 80
Pro Gln Arg Ser Ser Phe Arg Ile Lys Leu Ala Phe Arg Asn Leu Ser
85 90 95
Trp Pro Gly Leu Gly Leu Glu Asp His Gln Glu Ile Val Leu Gly Gln
100 105 110
Leu Val Leu Pro Glu Pro Asn Glu Ala Lys Pro Asp Asp Pro Ala Pro
115 120 125
Arg Pro Gly Gln His Ala Leu Thr Met Pro Ala Leu Glu Pro Ala Pro
130 135 140
Pro Leu Leu Ala Asp Leu Gly Pro Ala Leu Glu Pro Glu Ser Pro Ala
145 150 155 160
Ala Leu Gly Pro Pro Gly Tyr Leu His Ser Ala Pro Gly Pro Ala Pro
165 170 175
Ala Pro Gly Glu Gly Pro Pro Pro Gly Thr Val Leu Glu Pro Gln Ser
180 185 190
Ala Pro Glu Ser Ser Cys Pro Cys Arg Gly Ser Val Lys Asn Gln Pro
195 200 205
Ser Glu Glu Leu Pro Asp Met Thr Thr Phe Pro Pro Arg Leu Leu Ala
210 215 220
Glu Gln Leu Thr Leu Met Asp Ala Glu Leu Phe Lys Lys Val Val Leu
225 230 235 240
His Glu Cys Leu Gly Cys Ile Trp Gly Gln Gly His Leu Lys Gly Asn
245 250 255
Glu His Met Ala Pro Thr Val Arg Ala Thr Ile Ala His Phe Asn Arg
260 265 270
Leu Thr Asn Cys Ile Thr Thr Ser Cys Leu Gly Asp His Ser Met Arg
275 280 285
Ala Arg Asp Arg Ala Arg Val Val Glu His Trp Ile Lys Val Ala Arg
290 295 300
Glu Cys Leu Ser Leu Asn Asn Phe Ser Ser Val His Val Ile Val Ser
305 310 315 320
Ala Leu Cys Ser Asn Pro Ile Gly Gln Leu His Lys Thr Trp Ala Gly
325 330 335
Val Ser Ser Lys Ser Met Lys Glu Leu Lys Glu Leu Cys Lys Lys Asp
340 345 350
Thr Ala Val Lys Arg Asp Leu Leu Ile Lys Ala Gly Ser Phe Lys Val
355 360 365
Ala Thr Gln Glu Arg Asn Pro Gln Arg Val Gln Met Arg Leu Arg Arg
370 375 380
Gln Lys Lys Gly Val Val Pro Phe Leu Gly Asp Phe Leu Thr Glu Leu
385 390 395 400
Gln Arg Leu Asp Ser Ala Ile Pro Asp Asp Leu Asp Gly Asn Thr Asn
405 410 415
Lys Arg Ser Lys Glu Val Arg Val Leu Gln Glu Met Gln Leu Leu Gln
420 425 430
Val Ala Ala Met Asn Tyr Arg Leu Arg Pro Leu Glu Lys Phe Val Thr
435 440 445
Tyr Phe Thr Arg Met Glu Gln Leu Ser Asp Lys Glu Ser Tyr Lys Leu
450 455 460
Ser Cys Gln Leu Glu Pro Glu Asn Pro
465 470
<210> 11
<211> 180
<212> PRT
<213> Artificial Sequence
<220>
<223> Cancer/testis antigen 1 (NY-ESO-1)
<400> 11
Met Gln Ala Glu Gly Arg Gly Thr Gly Gly Ser Thr Gly Asp Ala Asp
1 5 10 15
Gly Pro Gly Gly Pro Gly Ile Pro Asp Gly Pro Gly Gly Asn Ala Gly
20 25 30
Gly Pro Gly Glu Ala Gly Ala Thr Gly Gly Arg Gly Pro Arg Gly Ala
35 40 45
Gly Ala Ala Arg Ala Ser Gly Pro Gly Gly Gly Ala Pro Arg Gly Pro
50 55 60
His Gly Gly Ala Ala Ser Gly Leu Asn Gly Cys Cys Arg Cys Gly Ala
65 70 75 80
Arg Gly Pro Glu Ser Arg Leu Leu Glu Phe Tyr Leu Ala Met Pro Phe
85 90 95
Ala Thr Pro Met Glu Ala Glu Leu Ala Arg Arg Ser Leu Ala Gln Asp
100 105 110
Ala Pro Pro Leu Pro Val Pro Gly Val Leu Leu Lys Glu Phe Thr Val
115 120 125
Ser Gly Asn Ile Leu Thr Ile Arg Leu Thr Ala Ala Asp His Arg Gln
130 135 140
Leu Gln Leu Ser Ile Ser Ser Cys Leu Gln Gln Leu Ser Leu Leu Met
145 150 155 160
Trp Ile Thr Gln Cys Phe Leu Pro Val Phe Leu Ala Gln Pro Pro Ser
165 170 175
Gly Gln Arg Arg
180
<210> 12
<211> 1245
<212> PRT
<213> Artificial Sequence
<220>
<223> Full Sindbis structural protein sequence (Capsid, E3, E2
Ectodomain, E2 Transmembrane Domain, 6K, E1 Ectodomain, E1
Transmembrane Domain)
<400> 12
Met Asn Arg Gly Phe Phe Asn Met Leu Gly Arg Arg Pro Phe Pro Ala
1 5 10 15
Pro Thr Ala Met Trp Arg Pro Arg Arg Arg Arg Gln Ala Ala Pro Met
20 25 30
Pro Ala Arg Asn Gly Leu Ala Ser Gln Ile Gln Gln Leu Thr Thr Ala
35 40 45
Val Ser Ala Leu Val Ile Gly Gln Ala Thr Arg Pro Gln Pro Pro Arg
50 55 60
Pro Arg Pro Pro Pro Arg Gln Lys Lys Gln Ala Pro Lys Gln Pro Pro
65 70 75 80
Lys Pro Lys Lys Pro Lys Thr Gln Glu Lys Lys Lys Lys Gln Pro Ala
85 90 95
Lys Pro Lys Pro Gly Lys Arg Gln Arg Met Ala Leu Lys Leu Glu Ala
100 105 110
Asp Arg Leu Phe Asp Val Lys Asn Glu Asp Gly Asp Val Ile Gly His
115 120 125
Ala Leu Ala Met Glu Gly Lys Val Met Lys Pro Leu His Val Lys Gly
130 135 140
Thr Ile Asp His Pro Val Leu Ser Lys Leu Lys Phe Thr Lys Ser Ser
145 150 155 160
Ala Tyr Asp Met Glu Phe Ala Gln Leu Pro Val Asn Met Arg Ser Glu
165 170 175
Ala Phe Thr Tyr Thr Ser Glu His Pro Glu Gly Phe Tyr Asn Trp His
180 185 190
His Gly Ala Val Gln Tyr Ser Gly Gly Arg Phe Thr Ile Pro Arg Gly
195 200 205
Val Gly Gly Arg Gly Asp Ser Gly Arg Pro Ile Met Asp Asn Ser Gly
210 215 220
Arg Val Val Ala Ile Val Leu Gly Gly Ala Asp Glu Gly Thr Arg Thr
225 230 235 240
Ala Leu Ser Val Val Thr Trp Asn Ser Lys Gly Lys Thr Ile Lys Thr
245 250 255
Thr Pro Glu Gly Thr Glu Glu Trp Ser Ala Ala Pro Leu Val Thr Ala
260 265 270
Met Cys Leu Leu Gly Asn Val Ser Phe Pro Cys Asp Arg Pro Pro Thr
275 280 285
Cys Tyr Thr Arg Glu Pro Ser Arg Ala Leu Asp Ile Leu Glu Glu Asn
290 295 300
Val Asn His Glu Ala Tyr Asp Thr Leu Leu Asn Ala Ile Leu Arg Cys
305 310 315 320
Gly Ser Ser Gly Arg Ser Lys Arg Ser Val Ile Asp Asp Phe Thr Leu
325 330 335
Thr Ser Pro Tyr Leu Gly Thr Cys Ser Tyr Cys His His Thr Val Pro
340 345 350
Cys Phe Ser Pro Val Lys Ile Glu Gln Val Trp Asp Glu Ala Asp Asp
355 360 365
Asn Thr Ile Arg Ile Gln Thr Ser Ala Gln Phe Gly Tyr Asp Gln Ser
370 375 380
Gly Ala Ala Ser Ala Asn Lys Tyr Arg Tyr Met Ser Leu Lys Gln Asp
385 390 395 400
His Thr Val Lys Glu Gly Thr Met Asp Asp Ile Lys Ile Ser Thr Ser
405 410 415
Gly Pro Cys Arg Arg Leu Ser Tyr Lys Gly Tyr Phe Leu Leu Ala Lys
420 425 430
Cys Pro Pro Gly Asp Ser Val Thr Val Ser Ile Val Ser Ser Asn Ser
435 440 445
Ala Thr Ser Cys Thr Leu Ala Arg Lys Ile Lys Pro Lys Phe Val Gly
450 455 460
Arg Glu Lys Tyr Asp Leu Pro Pro Val His Gly Lys Lys Ile Pro Cys
465 470 475 480
Thr Val Tyr Asp Arg Leu Lys Glu Thr Thr Ala Gly Tyr Ile Thr Met
485 490 495
His Arg Pro Arg Pro His Ala Tyr Thr Ser Tyr Leu Glu Glu Ser Ser
500 505 510
Gly Lys Val Tyr Ala Lys Pro Pro Ser Gly Lys Asn Ile Thr Tyr Glu
515 520 525
Cys Lys Cys Gly Asp Tyr Lys Thr Gly Thr Val Ser Thr Arg Thr Glu
530 535 540
Ile Thr Gly Cys Thr Ala Ile Lys Gln Cys Val Ala Tyr Lys Ser Asp
545 550 555 560
Gln Thr Lys Trp Val Phe Asn Ser Pro Asp Leu Ile Arg His Asp Asp
565 570 575
His Thr Ala Gln Gly Lys Leu His Leu Pro Phe Lys Leu Ile Pro Ser
580 585 590
Thr Cys Met Val Pro Val Ala His Ala Pro Asn Val Ile His Gly Phe
595 600 605
Lys His Ile Ser Leu Gln Leu Asp Thr Asp His Leu Thr Leu Leu Thr
610 615 620
Thr Arg Arg Leu Gly Ala Asn Pro Glu Pro Thr Thr Glu Trp Ile Val
625 630 635 640
Gly Lys Thr Val Arg Asn Phe Thr Val Asp Arg Asp Gly Leu Glu Tyr
645 650 655
Ile Trp Gly Asn His Glu Pro Val Arg Val Tyr Ala Gln Glu Ser Ala
660 665 670
Pro Gly Asp Pro His Gly Trp Pro His Glu Ile Val Gln His Tyr Tyr
675 680 685
His Arg His Pro Val Tyr Thr Ile Leu Ala Val Ala Ser Ala Thr Val
690 695 700
Ala Met Met Ile Gly Val Thr Val Ala Val Leu Cys Ala Cys Lys Ala
705 710 715 720
Arg Arg Glu Cys Leu Thr Pro Tyr Ala Leu Ala Pro Asn Ala Val Ile
725 730 735
Pro Thr Ser Leu Ala Leu Leu Cys Cys Val Arg Ser Ala Asn Ala Glu
740 745 750
Thr Phe Thr Glu Thr Met Ser Tyr Leu Trp Ser Asn Ser Gln Pro Phe
755 760 765
Phe Trp Val Gln Leu Cys Ile Pro Leu Ala Ala Phe Ile Val Leu Met
770 775 780
Arg Cys Cys Ser Cys Cys Leu Pro Phe Leu Val Val Ala Gly Ala Tyr
785 790 795 800
Leu Ala Lys Val Asp Ala Tyr Glu His Ala Thr Thr Val Pro Asn Val
805 810 815
Pro Gln Ile Pro Tyr Lys Ala Leu Val Glu Arg Ala Gly Tyr Ala Pro
820 825 830
Leu Asn Leu Glu Ile Thr Val Met Ser Ser Glu Val Leu Pro Ser Thr
835 840 845
Asn Gln Glu Tyr Ile Thr Cys Lys Phe Thr Thr Val Val Pro Ser Pro
850 855 860
Lys Ile Lys Cys Cys Gly Ser Leu Glu Cys Gln Pro Ala Ala His Ala
865 870 875 880
Asp Tyr Thr Cys Lys Val Phe Gly Gly Val Tyr Pro Phe Met Trp Gly
885 890 895
Gly Ala Gln Cys Phe Cys Asp Ser Glu Asn Ser Gln Met Ser Glu Ala
900 905 910
Tyr Val Glu Leu Ser Ala Asp Cys Ala Ser Asp His Ala Gln Ala Ile
915 920 925
Lys Val His Thr Ala Ala Met Lys Val Gly Leu Arg Ile Val Tyr Gly
930 935 940
Asn Thr Thr Ser Phe Leu Asp Val Tyr Val Asn Gly Val Thr Pro Gly
945 950 955 960
Thr Ser Lys Asp Leu Lys Val Ile Ala Gly Pro Ile Ser Ala Ser Phe
965 970 975
Thr Pro Phe Asp His Lys Val Val Ile His Arg Gly Leu Val Tyr Asn
980 985 990
Tyr Asp Phe Pro Glu Tyr Gly Ala Met Lys Pro Gly Ala Phe Gly Asp
995 1000 1005
Ile Gln Ala Thr Ser Leu Thr Ser Lys Asp Leu Ile Ala Ser Thr Asp
1010 1015 1020
Ile Arg Leu Leu Lys Pro Ser Ala Lys Asn Val His Val Pro Tyr Thr
1025 1030 1035 1040
Gln Ala Ser Ser Gly Phe Glu Met Trp Lys Asn Asn Ser Gly Arg Pro
1045 1050 1055
Leu Gln Glu Thr Ala Pro Phe Gly Cys Lys Ile Ala Val Asn Pro Leu
1060 1065 1070
Arg Ala Val Asp Cys Ser Tyr Gly Asn Ile Pro Ile Ser Ile Asp Ile
1075 1080 1085
Pro Asn Ala Ala Phe Ile Arg Thr Ser Asp Ala Pro Leu Val Ser Thr
1090 1095 1100
Val Lys Cys Glu Val Ser Glu Cys Thr Tyr Ser Ala Asp Phe Gly Gly
1105 1110 1115 1120
Met Ala Thr Leu Gln Tyr Val Ser Asp Arg Glu Gly Gln Cys Pro Val
1125 1130 1135
His Ser His Ser Ser Thr Ala Thr Leu Gln Glu Ser Thr Val His Val
1140 1145 1150
Leu Glu Lys Gly Ala Val Thr Val His Phe Ser Thr Ala Ser Pro Gln
1155 1160 1165
Ala Asn Phe Ile Val Ser Leu Cys Gly Lys Lys Thr Thr Cys Asn Ala
1170 1175 1180
Glu Cys Lys Pro Pro Ala Asp His Ile Val Ser Thr Pro His Lys Asn
1185 1190 1195 1200
Asp Gln Glu Phe Gln Ala Ala Ile Ser Lys Thr Ser Trp Ser Trp Leu
1205 1210 1215
Phe Ala Leu Phe Gly Gly Ala Ser Ser Leu Leu Ile Ile Gly Leu Met
1220 1225 1230
Ile Phe Ala Cys Ser Met Met Leu Thr Ser Thr Arg Arg
1235 1240 1245
<210> 13
<211> 19
<212> PRT
<213> Artificial Sequence
<220>
<223> Synthetic: glycine/serine linker
<400> 13
Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly
1 5 10 15
Gly Gly Gly
<210> 14
<211> 6
<212> PRT
<213> Artificial Sequence
<220>
<223> Synthetic: TEV cleavage site
<400> 14
Glu Asn Leu Tyr Phe Gln
1 5
<210> 15
<211> 16
<212> PRT
<213> Artificial Sequence
<220>
<223> Synthetic: glycine/serine Linker
<400> 15
Gly Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser Gly Gly Gly Gly Ser
1 5 10 15
Claims (31)
- 개체 투여시 면역 반응을 자극하며, 알파 바이러스 표면 막 당 단백질(alpha virus surface membrane glycoprotein) E1, E2 및 선택적으로 E3, 링커 및 적어도 하나 이상의 종양-관련 항원으로 필수적으로 구성되는 단리 또는 재조합 융합 단백질.
- 제1항에 있어서, 상기 융합 단백질은 서열번호 1로 표시되는 아미노산 서열과 적어도 98% 이상의 상동성을 갖는 것을 특징으로 하는 융합 단백질.
- 제1항에 있어서, 상기 융합 단백질은 적어도 서열번호 1의 66-978 위치의 아미노산 잔기를 포함하는 것을 특징으로 하는 융합 단백질.
- 제2항에 있어서, 상기 융합 단백질은 서열번호 1의 (i) 1-65 위치; (ii) 979-984 위치; 또는 (iii) 1-65 및 979-984 위치의 아미노산 잔기의 결실을 추가로 포함하는 것을 특징으로 하는 융합 단백질.
- 제1항에 있어서, 상기 융합 단백질은 서열번호 2로 표시되는 핵산 서열과 95% 이상의 상동성을 갖는 핵산 분자에 의해 코딩되는 것을 특징으로 하는 융합 단백질.
- 제1항에 있어서, 상기 E2는 길이가 적어도 300개 아미노산 이상이고 서열번호 1의 66-429 위치와 적어도 95% 이상의 상동성을 갖는 것을 특징으로 하는 융합 단백질.
- 제1항에 있어서, 상기 E1은 길이가 적어도 300개 아미노산 이상이고 서열번호 1의 449-854 위치와 적어도 95% 이상의 상동성을 갖는 것을 특징으로 하는 융합 단백질.
- 제1항에 있어서, 상기 종양-관련 항원은 서열번호 3 내지 11 중 임의의 10개 이상의 연속적인 아미노산을 포함하는 폴리펩티드 단편이고, 상기 10개 이상의 연속적인 아미노산을 포함하는 폴리펩티드 단편은 면역원성이고, 면역원성 폴리펩티드 단편은 서열번호 3 내지 11의 폴리펩티드의 1100개 미만의 아미노산을 포함하는 것을 특징으로 하는 융합 단백질.
- 개체에서 NK 세포, T-세포 또는 메모리 T-세포를 통해 면역 반응을 유도할 수 있는, 제1항 내지 제8항 중 어느 한 항의 융합 단백질을 포함하는 백신.
- 제1항 내지 제8항 중 어느 한 항의 융합 단백질 및 약학적으로 허용 가능한 담체를 포함하는 조성물.
- 제10항에 있어서, 보조제를 추가로 포함하는 조성물.
- 제1항 내지 제8항 중 어느 한 항의 융합 단백질을 코딩하는 핵산 분자를 포함하는 발현 벡터.
- 융합 단백질을 발현시키는, 제12항의 발현 벡터를 포함하는 세포.
- 제1항에 있어서, 상기 종양-관련 항원은 NCI Pilot Project to Prioritize Cancer Antigens과 관련하여 Clin Cancer Res 2009; 15:5323-5337의 표 3에 기재된 단백질의 폴리펩티드 단편인 것을 특징으로 하는 융합 단백질.
- 제1항 내지 제8항 중 어느 한 항에 있어서, 하나의 인접한 유전자 산물(one contiguous gene product)로서 발현되는 것을 특징으로 하는 융합 단백질.
- 제1항 내지 제8항 중 어느 한 항에 있어서, 이량체 또는 삼량체를 형성할 수 있는 것을 특징으로 하는 융합 단백질.
- 제1항 내지 제8항 중 어느 한 항에 있어서, 상기한 하나 이상의 종양-관련 항원이 알파 바이러스 표면 막 당 단백질 E1 또는 E2에 내부적으로 삽입되는 것을 특징으로 하는 융합 단백질.
- 제1항 내지 제8항 중 어느 한 항에 있어서, 상기한 하나 이상의 종양-관련 항원이 알파 바이러스 표면 막 당 단백질 E1 또는 E2 말단에 연결되는 것을 특징으로 하는 융합 단백질.
- 제1항 내지 제8항 중 어느 한 항에 있어서, 추가적으로 캡시드(Capsid) 단백질에 접합된 것을 특징으로 하는 융합 단백질.
- 제1항 내지 제8항 중 어느 한 항에 있어서, 상기 알파 바이러스 표면 막 당 단백질은 신드비스 알파 바이러스(Sindbis alpha virus) 단백질인 것을 특징으로 하는 융합 단백질.
- 적어도 하나 이상의 링커를 통해 하나 이상의 종양-관련 항원과 접합된 알파 바이러스 표면 막 당 단백질 E1 및/또는 E2로 필수적으로 구성되는 융합 단백질을 개체에 투여하는 것을 포함하는, 개체에서 면역 반응을 유도 또는 조절하기 위한 방법.
- 적어도 하나 이상의 링커를 통해 하나 이상의 바이러스 항원과 접합된 알파 바이러스 표면 막 당 단백질 E1 및/또는 E2를 필수적으로 구성되는 융합 단백질을 개체에 투여하는 것을 포함하는, 개체에서 HIV, 대상포진(Shingles) 및 헤르페스(Herpes)를 포함하는 잠복 바이러스 감염을 치료하는 방법.
- 제21항 또는 제22항에 있어서, 상기 E2는 길이가 적어도 300개 아미노산 이상이고 서열번호 1의 66-429 위치와 적어도 95% 이상의 상동성을 갖는 것을 특징으로 하는 방법.
- 제21항 또는 제22항에 있어서, 상기 E1은 길이가 적어도 300개 아미노산 이상이고 서열번호 1의 449-854 위치와 적어도 95% 이상의 상동성을 갖는 것을 특징으로 하는 방법.
- (a) 알파 바이러스 표면 막 당 단백질 E1 및/또는 E2; (b) 적어도 하나 이상의 종양-관련 항원 또는 바이러스 항원을 코딩하는 뉴클레오티드 구조물을 포함하는 발현 벡터에서 융합 단백질을 발현시키는 것을 포함하는 융합 단백질을 생산하는 방법으로서,
상기 종양-관련 항원 또는 바이러스 항원은 알파 바이러스 표면 막 당 단백질 E1 및/또는 E2에 연결되며,
상기 융합 단백질은 개체에 투여할 때 면역 반응을 자극하는 것을 특징으로 하는 융합 단백질을 생산하는 방법.
- 개체 투여시 면역 반응을 자극하는, 알파 바이러스 표면 막 당 단백질 E1, E2 및 적어도 하나의 링커로 필수적으로 구성되는 융합 단백질을 필요로 하는 개체에게 투여하는 것을 포함하는, 개체에서 암을 치료하는 방법.
- 제25항에 있어서, 상기 종양-관련 항원은 서열번호 3 내지 11 중 임의의 10개 이상의 연속적인 아미노산을 포함하는 폴리펩티드 단편이고, 상기 10개 이상의 연속적인 아미노산을 포함하는 폴리펩티드 단편은 면역원성이고, 면역원성 폴리펩티드 단편은 서열번호 3 내지 11의 폴리펩티드의 1100개 미만의 아미노산을 포함하는 것을 특징으로 하는 방법.
- 제25항에 있어서, 상기 융합 단백질은 포유동물 세포 시스템에서 생산되는 것을 특징으로 하는 방법.
- 제25항에 있어서, 상기 융합 단백질은 곤충 세포에서 생산되는 것을 특징으로 하는 방법.
- 제25항에 있어서, 상기 융합 단백질은 바큘로바이러스 벡터(baculovirus vector)에서 발현되고, 곤충 세포에서 발현되는 것을 특징으로 하는 방법.
- 제21항 내지 제24항 및 제26항 내지 제30항 중 어느 한 항에 있어서, 부가적인 요법(therapy)을 투여하는 것을 추가로 포함하는 것을 특징으로 하는 방법.
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| PCT/US2016/023203 WO2016149643A2 (en) | 2015-03-18 | 2016-03-18 | Fusion proteins comprising modified alpha virus surface glycoproteins and tumor associated antigen and methods thereof |
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| EP3589312A1 (en) * | 2017-03-03 | 2020-01-08 | New York University | Induction and enhancement of antitumor immunity involving virus vectors expressing multiple epitopes of tumor associated antigens and immune checkpoint inhibitors or proteins |
| CN110856724B (zh) * | 2018-08-24 | 2022-05-27 | 杭州康万达医药科技有限公司 | 包含核酸及car修饰的免疫细胞的治疗剂及其应用 |
| DE112020002641T9 (de) * | 2019-05-31 | 2022-10-06 | Guangzhou Virotech Pharmaceutical Co., Ltd. | M1-Virusmutante und deren Verwendung |
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2021
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2022
- 2022-10-13 US US18/046,267 patent/US20230181706A1/en active Pending
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| AU2021269306A1 (en) | 2021-12-09 |
| JP2018509937A (ja) | 2018-04-12 |
| US11471518B2 (en) | 2022-10-18 |
| CN107530410A (zh) | 2018-01-02 |
| CA2979697A1 (en) | 2016-09-22 |
| WO2016149643A3 (en) | 2016-12-01 |
| BR112017019776A2 (pt) | 2018-05-22 |
| EP3270958A4 (en) | 2018-11-14 |
| EP3270958A2 (en) | 2018-01-24 |
| WO2016149643A2 (en) | 2016-09-22 |
| RU2017132190A3 (ko) | 2019-08-30 |
| AU2016232771A1 (en) | 2017-10-05 |
| RU2017132190A (ru) | 2019-04-18 |
| JP6921053B2 (ja) | 2021-08-18 |
| US20230181706A1 (en) | 2023-06-15 |
| CN107530410B (zh) | 2021-11-09 |
| BR112017019776B1 (pt) | 2020-07-28 |
| AU2016232771B2 (en) | 2021-08-19 |
| CN114262380A (zh) | 2022-04-01 |
| HK1248610A1 (zh) | 2018-10-19 |
| US20210077600A1 (en) | 2021-03-18 |
| US10660948B2 (en) | 2020-05-26 |
| US20180243389A1 (en) | 2018-08-30 |
| MX2017011732A (es) | 2018-08-15 |
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