KR101063177B1 - 개 및 사람의 에를리키아증의 면역진단에 유용한 p153 및 p156 항원 및 이의 용도 - Google Patents
개 및 사람의 에를리키아증의 면역진단에 유용한 p153 및 p156 항원 및 이의 용도 Download PDFInfo
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- KR101063177B1 KR101063177B1 KR1020057007983A KR20057007983A KR101063177B1 KR 101063177 B1 KR101063177 B1 KR 101063177B1 KR 1020057007983 A KR1020057007983 A KR 1020057007983A KR 20057007983 A KR20057007983 A KR 20057007983A KR 101063177 B1 KR101063177 B1 KR 101063177B1
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Abstract
Description
관련 출원에 대한 참조설명
본 출원은 2002년 11월 4일에 출원되고 현재는 포기된 미국 가특허출원 60/423,573을 우선권으로 주장한다.
연방기금에 관한 설명
본 발명은 부분적으로 알레르기 및 감염 질환에 대한 국립 연구소의 연방정부 기금(승인번호 AI31431)을 사용하여 완성되었다. 따라서, 연방정부는 본 발명의 일부 권리를 갖는다.
본 발명은 일반적으로 분자 및 면역진단학 분야에 관한 것이다. 보다 상세하게는, 본 발명은 개의 에를리키아증(ehrlichiosis) 및 사람의 단핵구지향성(monocytotrophic) 에를리키아증의 종특이적 진단에 유용한 에를리키아 캐니스(Ehrlichia canis) 및 에를리키아 차펜시스(Ehrlichia chaffeensis) 유래의 종특이적 면역반응성 단백질 상동체(ortholog)(약 200kDa)에 관한 것이다.
개의 단핵구 에를리키아증은 주로 리케차 부류의 에를리키아 캐니스에 의해 유발되는 전세계적으로 분포된, 잠재적 치명성이 있는 진드기 매개 질환이다(Huxsoll et al., 1970). 이. 캐니스는 단핵구 및 대식세포에 대해 지향성을 나타내는 절대 세포내 세균(Nyindo et al., 1971)으로서, 척추동물 숙주에서 잠복기가 긴 감염을 확립한다(Harrus et al., 1998). 이 질환은 3단계를 특징으로 하는데, 즉 2 내지 4주간 지속되는 급성 단계; 개에 잠복 감염된 상태로 수년간 유지될 수 있는 준임상적 단계; 및 대부분의 개에서 골수 형성저하증 및 부적당한 예후로 인해 이 질환이 점차 악화되기 시작하는 만성 단계가 그것이다(Troy et al., 1990).
에를리키아 캐니스는 개과에 속하는 동물에서 감염되어 에를리키아증을 유발한다. 개의 에를리키아증에는 급성과 만성 단계가 있다. 급성 단계는 열, 장액성 콧물 및 눈물, 식욕감퇴, 우울증 및 체중 감량을 특징으로 한다. 만성 단계는 심한 범혈구감소증, 코피, 혈뇨, 혈변 뿐만 아니라 급성 질환 보다 심각한 임상 징후를 특징으로 한다. 이러한 질환이 초기에 치료된다면 개는 독시사이클린에 양호한 반응을 나타낸다. 하지만, 만성 감염된 개는 이 항생제에 그다지 반응하지 않는다. 따라서, 개의 에를리키아증 치료에는 조기 진단이 매우 중요하다.
급성 단계의 질환 치료에는 최선의 예후가 중요하다. 종종 백혈구감소증 및 저혈소판증과 같은 혈액 이상은 개의 에를리키아증의 유용한 증거를 제공하는 조기 진단에 중요한 인자이다(Troy et al., 1990). 하지만, 개의 에를리키아증의 임상 발현은 비특이적이기 때문에 진단하기가 매우 어렵다.
개의 에를리키아증 진단 시 간접 형광 항체(IFA) 검사법과 같은 혈청학적 방법은 이 방법의 간단성, 신뢰성 및 비용 효과 면으로 인해 표준 방법이 되었다(Troy et al., 1990). 하지만, 간접 형광 항체 검사법은 개를 감염시키는 근연성인 다른 에를리키아 종(이. 차펜시스, 이. 에윈지(E. ewingii), 아나플라즈마 파고사이토필럼(Anaplasma phagocytophilum) 및 에이. 플라티스(A. platys))과의 항원 교차 반응성으로 인해 종 특이적 진단을 할 수 없다는 단점이 있다. 또한, 주관적 해석은 교차 반응성 항원에 의해 유발되는 거짓 음성 결과 또는 거짓 양성 결과를 초래할 수도 있다. 이에 따라, 이. 캐니스의 특이적 검출을 위한 폴리머라제 연쇄 반응(PCR)과 같은 다른 진단 방법이 개발되었고, 세포 배양물 분리 보다는 민감한 방법으로 보고되었지만, 이 방법은 전문화된 훈련과 고가의 장비를 필요로 한다(McBride et al., 1996). 유기체의 분리방법은 시간 소모적인 방법으로서, 몇몇 실험실에서만 이 방법에 의해 일정한 성공을 거두었다. 또한, 이 방법을 이용하여 구체적인 병인론을 규명하기 위해서는 분리물의 특성 분석을 위한 추가 시험이 필요하다.
이. 캐니스와 이. 차펜시스 사이에 공유되는 혈청학적 교차반응성 항원은 보고되어 있다. 주요 혈청학적 교차반응성 단백질 중 일부는 28 내지 30kDa의 분자량을 나타내고(Chen et al., 1997; Rikihisa et al., 1994), 현재 이러한 단백질들은 상동성인 다중유전자 패밀리에 의해 암호화되어 있는 것으로 알려져 있다(Ohashi et al., 1998a, b). 이. 차펜시스 및 이. 캐니스에서 동정되고 서열분석된 p28 유전자에는 동일하지 않은 상동체가 각각 22개와 25개가 있다. 이. 캐니스와 이. 차 펜시스의 P28 단백질 사이에서는 유사한 종내 및 종간 균주 상동성이 관찰되는데, 이는 이 단백질의 혈청학적 교차반응성을 설명한다(McBride et al., 1999).
최근 보고에 따르면, 이. 차펜시스 유래의 rP28 단백질이 사람 단핵구지향성 에를리키아증(HME)의 증례를 진단하는데 있어서 비민감성인 수단이라는 실험결과가 입증되었다(Yu et al., 1999a). 이의 근본 원인은 이. 차펜시스의 여러 균주들에서 나타나는 P28 단백질의 다양성 때문인 것으로 보인다(Yu et al., 1999b). 이에 반해, 이. 캐니스에서 동정된 P28 유전자는 지리적으로 분산된 균주들 중에서 보존적이어서, 이. 캐니스 rP28은 개의 에를리키아증 진단에 유용한 것으로 증명되어 있다(McBride et al., 1999; Ohashi 1998a). 이. 캐니스의 당단백질(gp140) 및 이. 차펜시스의 당단백질(gp120)을 비롯하여 기타 다른 상동성인 면역반응성 단백질도 클로닝되어 있다(Yu et al., 1997, 2000). 이. 차펜시스의 rgp120의 반응성은 사람의 단핵구지향성 에를리키아증의 혈청진단용인 간접 형광 항체와 상당한 연관성이 있으며, 이. 캐니스의 rgp140을 이용한 예비 연구에서는 이 단백질이 민감하고 신뢰성있는 면역진단성 항원일 가능성이 있음을 암시하고 있다(Yu et al., 1999a, 2000).
이러한 종래 기술에는 이. 캐니스 및 이. 차펜시스에 대한 혈청학적 진단 및 분자 진단에 유용한 특정 항원 뿐만 아니라 이의 사용방법도 미흡하다. 이에, 본 발명은 당해 기술분야의 이러한 요구와 열망을 충족시키고자 한다.
발명의 개요
에를리키아 캐니스의 강한 면역반응성 43kD 단백질(p43)은 동정되어 있다(미국 특허 6,355,777). 면역진단성 항원으로서 p43은 간접 형광 항체 검사법과 비교했을 때 96%의 정확도가 있으며, 이. 캐니스 감염의 종 특이적 진단을 허용했다. 또 다른 연구에서 밝혀진 바에 따르면, 이. 캐니스 p43은 에를리키아 종에서 개시된 가장 큰 면역반응성 단백질인, 예상 분자량이 153kD인 단백질의 N-말단 부분을 나타낸다. 이러한 p153의 재조합 발현 단편을 단백질 겔 전기영동으로 분석해보면, 예상 분자량 보다 더 크게 나타나는데(약 10 내지 30%), 이는 N-말단 및 C-말단 단편 상에 존재하는 탄수화물 글리칸 때문으로, 이는 p153이 당단백질임을 시사한다.
입수용이한 이. 차펜시스 게놈 서열(95%)에 대하여 BLASTn 조사를 수행했고, 그 결과 p153 단백질 상동체를 암호화하는 유전자가 이. 차펜시스에서 확인되었다. 이. 캐니스 p153(4263bp)과 이. 차펜시스 p156(4389bp) 유전자는 염색체내 위치가 상동성(약 87%) 데옥시구아노신-트리포스페이트 트리포스포하이드롤라제 유전자와 개방 판독 프레임 앞에 있는 상동성(약 90%) 유전자간(intergenic) 서열의 하류로서 유사했다. 이 당단백질 유전자들 사이에는 핵산 서열 상동성(50%)이 관찰되어, p43 유전자 단편의 유전자 분기(divergence)에 관한 종래의 발견을 지지하고 있으며, p153 단백질 및 p156 단백질은 아미노산 유사성이 32%였다. 분자량이 200kD인 천연 이. 캐니스 단백질은 p153의 N-말단 영역(p43)에 대해 생성된 항혈청과 반응했으며, 이는 천연 단백질이 해독후 변형됨을 암시한다. 이와 마찬가지로, 이. 차펜시스 p156의 N-말단 영역을 함유하는 재조합 단백질도 예상(약 200kD) 보다 더 많이 이동했고, 재조합 단백질 상에서 탄수화물이 검출되었다. 이러한 N-말단 단편에서 주요 면역반응성 에피토프가 확인되었다. 이러한 염색체 위치, 아미노산 상동성 및 생물물리학적 성질은 p153 당단백질과 p156 당단백질(gp200으로 표시함)이 종 특이적 면역반응성 단백질 상동체라는 결론을 지지한다.
주요 면역반응성 에피토프는 이. 캐니스 p153의 N-말단(P43) 및 C-말단 영역과, 이. 차펜시스 p156 단백질 상동체의 N-말단 영역에서는 주요 면역반응성 에피토프가 확인되었고, 따라서 혈청학적 진단 및 백신에 유용하게 사용될 것이다. 또한, 이러한 단백질을 암호화하는 유전자는 종특이적이어서 분자 기초 진단학 개발에 유용하게 사용될 수 있을 것이다.
본 발명의 다른 관점, 추가 관점, 특징 및 장점은 이하에 제시되는 본 발명의 바람직한 구체예에 대한 설명으로부터 확인할 수 있을 것이다. 이러한 구체예들은 본 발명을 개시하기 위한 것이다.
본 발명의 전술한 특징, 장점 및 목적 뿐만 아니라 자명한 기타 다른 특징, 장점 및 목적이 달성되고 상세하게 이해될 수 있도록 하기 위해, 상기에 간략히 요약한 본 발명을, 첨부되는 도면에 예시된 특정 구체예와 관련하여 보다 상세하게 설명하고자 한다. 따라서, 도면은 본 명세서의 일부를 구성한다. 하지만, 첨부 도면은 본 발명의 바람직한 구체예를 설명하는 것으로서, 본 발명의 범위를 제한하는 것으로 간주되지 않아야 함은 자명한 것이다.
도 1A 및 도 1B는 이. 차펜시스 p156(상단 서열) 및 이. 캐니스 p153(하단 서열) 단백질 상동체의 립만-피어슨(Lipman-Pearson) 아미노산 배열을 도시한 것이다. 중간에는 동일한 아미노산, 보존적(:) 및 반보존적 치환을 나타낸 것이다.
도 2A 및 도 2B는 이. 캐니스 p153(A) 및 이. 차펜시스(B) 유래의 재조합 단백질 단편의 발현과 항-V5 항체에 의한 검출결과를 도시한 것이다. 이. 캐니스 p153: 레인 1, N-말단 단편(1107bp, nt-1-1107), 레인 2, 내부 단편(910bp, nt-1080-1990), 레인 3, 내부 단편(1000bp, nt-1950-2950), 레인 4, C-말단 단편(1280bp, nt-2940-4220). 이. 차펜시스 p156: 레인 1, N-말단 단편(1545bp, nt-125-1675), 레인 2, 내부 단편(1365bp, nt-1685-3050), 레인 3, C-말단(1365bp, nt-2950-4315).
도 3A는 이. 캐니스 p153 재조합 단편의 웨스턴 면역블롯을 도시한 것이다. 레인 1, N-말단 단편(1107bp, nt-1-1107), 레인 2, 내부 단편(910bp, nt-1080-1990), 레인 3, 내부 단편(1000bp, nt-1950-2950), 및 레인 4, C-말단 단편(1280bp, nt-2940-4220).
도 3B는 pRSET 발현 벡터를 이용하여 이. 콜리에서 발현시킨 상응하는 이. 캐니스 p153의 정제된 재조합 단편에서의 탄수화물 검출 결과를 도시한 것이다. 재조합 단백질에 부착된 글리칸은 산화되었고, 비오틴으로 표지되어 스트렙트아비딘-알칼리 포스파타제에 의해 검출되었다.
도 4A는 사람(좌측 패널) 및 개(우측 패널)의 혈청을 이용한 이. 차펜시스 p156 재조합 단편(레인 1 내지 3)의 웨스턴 블롯 결과를 도시한 것이다. 레인 1, 이. 차펜시스 p156 N-말단 단편(1545bp, nt-125-1675), 레인 2, 내부 단편(1365bp, nt-1685-3050), 및 레인 3, C-말단(1365bp, nt-2950-4315). 발현된 재조합 단백질 은 이. 차펜시스 p156의 약 95%를 나타낸다.
도 4B는 3개의 상응하는 재조합 이. 차펜시스 p156 단백질(레인 1 내지 3)의 탄수화물 검출결과를 도시한 것이다.
도 5는 이. 캐니스 감염된 개(레인 1) 및 재조합체 p43(gp200)(레인 2) 및 재조합체 gp140(레인 3) 폴리클로날 래빗 항혈청을 이용하여 이. 캐니스 전세포 용해물 중의 단백질을 입증하는 웨스턴 블롯 결과를 도시한 것이다.
이. 캐니스 p43 유전자 서열은 종래 1173bp로 보고되었으나(미국 특허 6,355,777), 추가 분석을 통해, 인위적 종결 코돈과 절단된 유전자 서열을 초래하는 DNA 서열분석 오류가 있었음을 확인했다. 프라이머-어댑터 유전자 워킹법을 통해, 본래 p43 클론의 2.4kbp 하류에서 추가적인 4.5kbp 서열이 분석되었다. 4263bp의 개방 판독 프레임을 확인하면서 불완전한 p43 유전자 서열이 완성되었고, 이 유전자는 예상 분자량이 153kD인 단백질(p153이라고 표기함)을 암호화한다. p153 유전자의 상류에는 데옥시구아노신-트리포스페이트 트리포스포하이드롤라제를 암호화하는 개방 판독 프레임과 p153 유전자 앞에 위치한 유전자간 비암호화 영역이 존재했고, 이들은 이. 캐니스 및 이. 차펜시스 사이에 높은 핵산 상동성을 나타냈다(각각, 87% 및 90%).
2.4kbp p43 클론을 이용한 이. 차펜시스 게놈 서열의 BLASTn 조사에서는 고도로 상동성인 핵산 서열을 확인했다. 크기가 이. 캐니스 p153과 거의 동일한 대형 개방 판독 프레임(4389bp)이 상동성 암호화 핵산 서열 및 유전자간 핵산 서열의 상류에 동일한 염색체내 위치에서 발견되었고, 예상 분자량이 156kD인 단백질을 암호화하였다(p156). 이. 캐니스 p153과 이. 차펜시스 p156 유전자 사이에서는 핵산 서열 상동성(약 50%)이 관찰되었으나, 단백질은 총 아미노산 서열 유사성이 32%로 확인되었다(도 1).
이. 차펜시스 p156 단백질을 나타내는 이. 콜리에서 발현된 유전자 작제물(nt-125-1670; nt-1685-3050; nt-2950-4315) 및 이. 캐니스 p153의 4개의 재조합 단편(nt-1-1107(p43); nt-1080-1990; nt-1950-2950; nt-2940-4220)은 이. 콜리에서 발현되었다(도 2). 이. 캐니스의 N-말단(nt-1-1107) 및 C-말단(nt-2940-4220) 재조합체가 발현하는 단백질 모두 강한 면역반응성을 나타냈다(도 3A). 하지만, 이. 차펜시스 p156은 N-말단 단편(nt-125-1670) 만이 면역반응성이었다(도 4A).
이. 캐니스(nt-1-1107 및 nt-2940-4420) 및 이. 차펜시스 p156 재조합 단백질 단편(nt-125-1607)은 SDS-PAGE에서 예상한 것 보다 더 많이 이동했고, 이는 이 단편에 해독후 변형이 일어났음을 시사한다. 이어서, 이. 캐니스 p153 및 이. 차펜시스 p156 펩타이드 단편에서 탄수화물이 검출되었다(도 3B 및 도 4B).
항-p43 항체는 이. 캐니스 전세포 용해물에서 약 200kD의 천연 단백질과 반응했다. 더욱이, 이러한 200kD 단백질은 이. 캐니스에 감염된 개의 혈청에 의해서도 인식되었다(도 5). 앞에서 p43으로 확인된 부분 유전자 서열(p153의 N-말단 부분)은 진뱅크 승인번호 AF252298로 할당되어 있다. p153을 암호화하는 보정된 서열은 진뱅크 승인번호 AY156950으로 할당되어 있다.
이러한 염색체 위치, 아미노산 상동성 및 생물물리학적 성질은 p153 당단백질과 p156 당단백질(gp200으로 표시함)이 종 특이적 면역반응성 상동체라는 결론을 지지한다. 이러한 단백질은 백신 개발에 사용할 수 있는 가능성이 있으며, 에를리키아 감염 진단에 민감하고 신뢰성있는 혈청진단학적 항원으로서 사용될 수 있다. 이러한 용도는 혈청진단학적 항원으로서 이. 캐니스 p43의 면역반응성과 잠재적 용도를 입증한 종래의 발견(미국 특허 6,355,777)에 의해서도 지지된다. p43에 대한 항체와의 반응은 간접 형광 항체(IFA) 역가가 >40인 시료와는 100% 상관성을 보였고, 간접 형광 항체 역가가 <40인 몇몇 시료와도 반응했다. p43 항체에 의한 몇몇 간접 형광 항체 음성 시료와의 약한 반응성은 p43 단백질이 보다 민감한 혈청진단학적 항원일 가능성이 있음을 암시한다. 본 발명에서 제시되는 이러한 결과는 p43이 이. 캐니스의 보다 큰 p153 단백질의 일부임을 시사한다.
본 발명은 에를리키아 캐니스 면역반응성 표면 단백질 p153 및 에를리키아 차펜시스 p156 단백질을 암호화하는 분리된 폴리뉴클레오타이드에 관한 것이다. 바람직하게, 이러한 분리된 폴리뉴클레오타이드는 서열번호 1 및 2에 제시된 아미노산 서열을 갖는 단백질을 암호화한다. 또한, 이러한 DNA는 유전자 코드의 축퇴성으로 인해 뉴클레오타이드 서열에 차이가 있을 수도 있다.
또한, 본 발명에는 이러한 분리된 폴리뉴클레오타이드와 세포내에서의 DNA 발현에 필요한 조절 인자를 함유하는 벡터; 분리 및 정제된 p153 및 p156 단백질; 및 이러한 단백질들에 대해 유도된 항체도 포함된다.
본 발명은 추가로 개 및 사람의 에를리키아증에 대한 백신 제조에 사용되는 p153 및 p156 단백질의 용도에 관한 것이다. 또한, 본 발명은 개의 혈청이 p153 또는 p156 단백질과 반응하는지의 여부를 측정하여 개 또는 사람이 에를리키아 종으로 감염되었는지의 여부를 결정하는 방법도 제공한다. 사용된 단백질은 재조합 유래인 것이며, 단백질에 대한 혈청의 반응을 검출하기 위해서는 웨스턴 블롯 분석을 사용할 수 있다. 종래 분리된 이. 캐니스 p28 단백질과의 반응도 이. 캐니스 감염의 신뢰할 수 있는 마커이므로, 진단법은 에를리키아 캐니스의 p153 단백질, gp140 및 p28 항원에 대한 면역반응성을 검출하는 것으로 이루어질 수 있다.
또한, 본 발명은 개 또는 사람이 에를리키아 종으로 감염되었는지의 여부를 측정하는 혈청진단학적 키트에 관한 것이다. 이러한 키트에는 본 명세서에 개시된 고정화 단백질(p153 또는 p156), 개 혈청에 적당한 희석 완충액, 리포터 분자가 결합된 개의 항혈청 제2 항체 및 리포터 분자 검출에 적당한 시약이 함유된다. 항원을 고정화시킬 수 있는 방법에는 막이나 미세역가 플레이트에 결합시키는 방법이 포함된다. 리포터 분자는 루시퍼라제, 서양고추냉이 퍼옥시다제, β-갈락토시다제 또는 형광성 표지일 수 있다.
본 발명은 또한 개가 에를리키아 종으로 감염되었는지의 여부를 측정하는 PCR 증폭 방법에 관한 것이다. 이 방법은 감염 가능성이 있는 개 또는 사람의 혈액으로부터 DNA를 추출한 뒤 이. 캐니스 p153 유전자 또는 이. 차펜시스 p156 유전자에 특이적인 올리고뉴클레오타이드 프라이머를 이용하여 PCR 증폭시키는 것이다. 수득되는 PCR 증폭 산물은 겔 전기영동과 같은 방법으로 크기별로 분리하고 적당한 크기의 산물이 검출되면 에를리키아 감염을 시사하게 된다.
또한, 본 발명은 p153 또는 p156 유전자의 PCR 검출용 키트에 관한 것이다. 이 키트는 혈액으로부터 DNA를 추출하는 시약, p153 또는 p156 특이적 올리고뉴클레오타이드 및 PCR 증폭용 시약을 함유한다.
본 발명에는, 당해 기술분야의 범위내의 통상적인 분자 생물학, 미생물학 및 재조합 DNA 기술이 사용될 수 있다. 이러한 기술들은 문헌에 충분히 설명되어 있다. 그 예로서, 문헌[Maniatis, Fritsch & Sambrook, "Molecular Cloning: A Laboratory Manual (1982);"DNA Cloning: A Practical Approach, "Volumes I and II(D. N. Glover ed. 1985);"Oligonucleotide Synthesis"(M. J. Gait ed. 1984);"Nucleic Acid Hybridization" [B. D. Hames & S. J. Higgins eds. (1985)]; "Transcription and Translation" [B. D. Hames & S. J. Higgins eds. (1984)]; "Animal Cell Culture" [R. I. Freshney, ed. (1986)]; "Immobilized Cells And Enzymes" [IRL Press, (1986)]; B. Perbal, "A Practical Guide To Molecular Cloning" (1984)]이 참고될 수 있다.
본 명세서에 사용된, "숙주"라는 용어는 원핵생물 뿐만 아니라 효모, 식물 및 동물 세포와 같은 진핵생물도 포함하는 것을 의미한다. 본 발명의 단백질을 암호화하는 재조합 DNA 분자 또는 유전자는 일반적으로 당업자에게 공지된 모든 기술을 이용하여 숙주의 형질전환에 이용될 수 있다. 원핵생물 숙주에는 이. 콜리, 에스. 팀피뮤리엄(S. tymphimurium), 세라티아 마르세슨스(Serratia marcescens) 및 바실러스 서브틸리스(Bacillus subtilis)가 포함된다. 진핵생물 숙주에는 피키아 파스토리스(Pichia pastoris)와 같은 효모, 포유동물 세포 및 곤충 세포가 포함된다.
일반적으로, 삽입된 DNA 단편의 효율적 전사를 촉진하는 프로모터 서열을 함유한 발현 벡터가 이러한 숙주와 관련하여 사용된다. 이러한 발현 벡터에는 일반적으로 복제 오리진, 프로모터, 종결인자, 뿐만 아니라 형질전환된 세포에 표현형적 선별 특성을 제공할 수 있는 특정 유전자가 함유된다. 형질전환된 숙주는 당해기술분야에 공지된 방법에 따른 발효 및 배양을 통해 세포 증식을 최적화할 수 있다. 적당한 전사 및 해독 조절 시그널을 함유하는 발현 벡터의 작제에도 당업자에게 공지된 방법을 사용할 수 있다. 이러한 기술들은 예컨대, 문헌[Sambrook et al. , 1989, Molecular Cloning : A Laboratory Manual (2nd Ed.), Cold Spring Harbor Press, N. Y.]에 설명되어 있다.
본 명세서에 사용된 "프라이머"라는 용어는 천연 정제된 제한 분해물이든지 또는 합성 생성물이든지의 여부를 불문하고 올리고뉴클레오타이드를 의미하는 것으로서, 핵산 가닥에 상보적인 프라이머 신장 산물의 합성이 유도되는 조건하에 존재할 때 합성 개시점으로 작용할 수 있는 것이다. 이러한 조건에는 뉴클레오타이드 및 DNA 폴리머라제와 같은 유도제의 존재 및 적당한 온도와 pH가 포함된다. 프라이머는 일본쇄이거나 이본쇄일 수 있으며, 유도제의 존재하에 바람직한 신장 산물의 합성을 개시하기에 충분한 길이이어야 한다. 프라이머의 정확한 길이는 다수 요인, 예컨대 온도, 프라이머 기원 및 사용 방법에 따라 달라진다. 예를 들어, 진단 용도인 경우에, 올리고뉴클레오타이드 프라이머는 일반적으로 15 내지 25개 또는 표적 서열의 복잡성에 따라 그 이상의 뉴클레오타이드를 함유한다. 이보다 적은 수의 뉴클레오타이드를 함유하는 프라이머도 사용될 수 있다.
본 명세서에 사용된 프라이머는 특정 표적 DNA 서열의 다른 가닥에 "실질적으로" 상보적인 것으로 선택한다. 이것은, 프라이머가 상대 가닥과 하이브리드화하기에 충분히 상보적이어야 함을 의미한다. 따라서, 프라이머 서열은 주형의 정확한 서열을 반영할 필요는 없다. 예를 들어, 프라이머의 5'-말단에는 비상보성 뉴클레오타이드 단편이 부착될 수 있는데, 단 프라이머 서열의 나머지는 그 가닥에 상보성이어야 한다. 또는, 비상보성 염기 또는 보다 긴 서열이 프라이머 내에 산재될 수 있는데, 단 이러한 프라이머 서열은 그 서열과 충분히 상보적이거나 그 서열과 하이브리드화하여 신장 산물의 합성을 위한 주형을 형성하는 것이어야 한다.
다음 실시예는 본 발명의 다양한 구체예를 예시하기 위한 것이지, 본 발명을 어떠한 방식으로든지 제한하기 위한 것이 아니다.
실시예 1
이. 캐니스 p153 및 이. 차펜시스 p156 단백질의 특성분석
이. 캐니스 p43 단백질 유전자는 종래 기술된 바와 같은 람다 Zap II 발현 라이브러리로부터 분리했다(McBride et al., 2001; 미국 특허 6,355,777). 본래 2.4kb 클론은 데옥시구아노신-트리포스페이트 트리포스포하이드롤라제 유전자를 암호화하는 개방 판독 프레임(ORF)과 절단된 p43 유전자 단편 앞에 있는 하류 229bp 유전자간 스페이스로 구성된다. p43 개방 판독 프레임의 완전 서열 분석에는 주형으로서 이. 캐니스 게놈 DNA(Jake, North Carolina 균주)를 이용하는 프라이머-어댑터 PCR법을 사용했다. 앰플리콘은 증폭용 프라이머를 사용하여 직접 서열분석하거나 또는 서열 분석을 위해 TOPO/TA에 클로닝했다. 전체 이. 캐니스 p43 클론(2.4kb)을 이용한 이. 차펜시스 게놈 서열의 BLASTn 조사를 통해 이. 차펜시스 상동체(p156 유전자)를 확인했다.
이. 캐니스 p153 및 이. 차펜시스 p156 유전자는 큰 단편(1 내지 1.5kbp)으로 나뉘었고, pUni/V5-His-TOPO Echo 공급체 벡터에 클로닝한 뒤, pBAD Thio-E 또는 pRSET Echo 수용체 발현 벡터와 재조합했다. 아라비노스 또는 IPTG 유도 후 재조합 단백질을 4시간 동안 발현시켰다. 발현된 재조합 단백질에 존재하는 글리칸 검출은 막 라벨링 프로토콜에 따라 당단백질 검출용 면역블롯 키트(Bio-Rad)를 사용하여 수행했다. 종래 기술된 이. 차펜시스 재조합 Dsb 단백질(McBride et al., 2002)도 이. 콜리에서 발현시켜 당단백질 검출 실험의 에를리키아 음성 대조군 단백질로서 사용했다. 이. 캐니스 전세포 용해물을 구배 겔(4 내지 12% Bis-Tris, Novagen)을 이용하는 겔 전기영동으로 분리하고 반건조 이동 장치(Bio-Rad)를 사용하여 순수 니트로셀룰로스 상으로 이동시켰다. 면역블롯팅은 종래 기술된 바와 같이 수행했다(McBride et al., 2001).
결론
이. 캐니스 p153의 N-말단(p43) 부분을 함유하는 클론의 강한 면역반응성은 이 단백질의 최초 동정 및 특성분석에서 확인되었다(McBride et al., 2001). 개에 존재하는 이. 캐니스에 대한 항체를 검출하기 위한 간접 형광 항체 검사법의 결과와 비교했을 때 p43은 우수한 감도 및 특이성을 나타냈다. 또한, p43은 항재조합체 p43 폴리클로날 항체가 이. 차펜시스 감염된 DH82 세포와 반응하지 않음으로써, 종특이적 검출을 허용하는 것으로 확인되었다. 유전자적으로 분기(divergent)되어 있고 아미노산 상동성도 낮은 이. 차펜시스에 존재하는 p153 상동체(p156)의 동정은 p43 단백질이 종특이적 항원이라는 발견을 지지하며, 이에 따라 우수한 종특이적 면역진단성 항원으로 사용될 수 있을 것이다. p153 단백질의 N-말단(p43) 및 C-말단 영역에는 주요 선형 B 세포 에피토프가 존재한다.
p43 재조합 단백질은 처음에는 인식하지 못했던 예상 분자량 보다 더 큰 분자인 것을 나타났다(약 30% 또는 약 10kD). 종래 보고된 에를리키아 당단백질 gp120 및 gp140은 예상한 것 보다 60 내지 100% 더 컸다. p43 단백질은 분자량 이동 정도는 훨씬 적었지만, 부착된 글리칸의 탄수화물 검출로 확인되는 당단백질이다. p43 발견에서와 같이, 발현된 이. 차펜시스 p156 재조합 유전자 단편도 예상 분자량 보다 훨씬 컸고, 이러한 단편에서 탄수화물이 검출되었다. 또한, 이. 캐니스 p153의 C-말단 단편도 예상 분자량보다 더 컸다(약 10% 또는 6kD).
p43 유전자가 확인되었을 때, 이에 상응하는 전세포 용해물 유래의 천연 이. 캐니스 단백질은 항p43 항혈청과 반응하지 않았다. 여기서 제시된 발견에 기초할 때, 이러한 모순의 원인은 p43 유전자가 불완전한 개방 판독 프레임을 나타내어 p43 유전자는 43kD 단백질을 암호화하지 않는다는 사실 때문이다. 또한, 이 단백질의 큰 분자량(>150kD)은 면역블롯을 통해 이 단백질을 일관되게 확인하기 위해서는 겔 전기영동 조건에 특별한 주의가 필요하다. 이. 캐니스 전세포 용해물의 200kD 단백질은 항-p43 폴리클로날 항체와 강한 면역반응성이었다. 이 단백질의 분자량은 분자량 증가에 기여하는 일부 글리칸과 커플링된 p153의 예상 분자량과 일치했다. 이와 같은 발견은 또한 거의 전체 개방 판독 프레임을 나타내는 이. 차펜시스 p156 재조합 단편의 분자량과 일치했다.
에를리키아 종의 당단백질은 병원성 세균의 특징적인 주요 단백질 중의 일부이다. 지금까지 발견된 에를리키아 당단백질은 감염된 환자 및 동물에서 항체에 의해 일관되고 강력하게 인식된다. 이와 같이 표면에 노출된 고유의 면역반응성 단백질은 백신 개발의 가능성을 갖고 있으며, 서브유니트 백신의 중요 성분이 될 수 있다.
다음의 참고문헌은 본원에 인용된 문헌들이다:
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Yu, et al. , 1997. Cloning and sequencing of the gene for a 120- kDa immunodominant protein of Ehrlichia chaffeensis. Gene 184: 149-154.
Yu, et al. , 1999a. Comparison of Ehrlichia chaffeensis recombinant proteins for serologic diagnosis of human monocytotropic ehrlichiosis. J. Clin. Microbiol. 37: 2568- 2575.
Yu, et al. , 1999b. Genetic diversity of the 28-kilodalton outer membrane protein gene in human isolates of Ehrlichia chaffeensis. J. Clin. Microbiol. 37: 1137-1143.
Yu, et al. , 2000. Molecular cloning and characterization of the 120-kilodalton protein gene of Ehrlichia canis and application of the recombinant 120-kilodalton protein for serodiagnosis of canine ehrlichiosis. J. Clin. Microbiol. 38: 369-374.
본 명세서에 언급된 모든 특허 또는 공개문헌은 본 발명이 속하는 당해 기술분야의 숙련된 자의 수준을 나타낸다. 이러한 특허 및 공개문헌은 각각 특이적으로 본원에 참고원용되는 것으로 표시되었지만 동일한 정도로 참고인용되었다.
당업자라면, 본 발명이 목적 수행과 언급된 결과 및 장점 뿐만 아니라 본 발명 고유의 결과와 장점 수득을 위해 상당히 최적화된 것임을 잘 알 것이다. 본 명세서에서 기술된 방법, 절차, 처리, 분자 및 특정 화합물과 함께 제시된 실시예는 현재의 바람직한 구체예를 나타내는 것이며, 예시적인 것으로서, 본 발명의 범위를 제한하는 것으로 간주되어서는 안된다. 따라서, 당업자가 수행할 수 있는 변화 및 다른 사용은 첨부되는 청구의 범위에 의해 한정되는 본 발명의 사상에 포함되는 것이다.
<110> RESEARCH DEVELOPMENT FOUNDATION
<120> P153 AND P156 ANTIGENS FOR THE IMMUNODIAGNOSIS
OF CANINE AND HUMAN EHRLICHIOSES AND USES THEREOF
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<150> US 60/423,573
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Claims (27)
- (a) 서열번호 2의 아미노산 서열을 갖는 p153 단백질을 암호화하는 분리된 DNA; 및(b) 유전자 코드의 축퇴성으로 인해 코돈 서열이 (a)의 분리된 DNA와 상이한, 상기 단백질을 암호화하는 분리된 DNA로 이루어진 그룹 중에서 선택되는, 에를리키아 캐니스(Ehrlichia canis) 면역반응성 표면 단백질 p153을 암호화하는 DNA.
- 제1항에 따른 DNA와 이 DNA를 세포에서 발현시키는데 필요한 조절 요소를 포함하는 벡터.
- 제2항에 있어서, DNA가 서열번호 2에 제시된 아미노산 서열을 갖는 p153 단백질을 암호화하는 벡터.
- 서열번호 2에 제시된 아미노산 서열을 갖는 p153 단백질을 암호화하는 제2항에 따른 벡터로 형질감염된 숙주 세포.
- 제4항에 있어서, 세포가 세균 세포, 포유동물 세포, 식물 세포 및 곤충 세포로 이루어진 그룹 중에서 선택되는 숙주 세포.
- (a) 서열번호 2의 아미노산 서열을 갖는 p153 단백질을 암호화하는 분리된 DNA; 및(b) 유전자 코드의 축퇴성으로 인해 코돈 서열이 (a)의 분리된 DNA와 상이한 분리된 DNA로 이루어진 그룹 중에서 선택되는 DNA에 의해 암호화되는, 분리 및 정제된 에를리키아 캐니스(Ehrlichia canis) 면역반응성 표면 단백질 p153.
- (a) 서열번호 1의 아미노산 서열을 갖는 p156 단백질을 암호화하는 분리된 DNA; 및(b) 유전자 코드의 축퇴성으로 인해 코돈 서열이 (a)의 분리된 DNA와 상이한, 상기 단백질을 암호화하는 분리된 DNA로 이루어진 그룹 중에서 선택되는, 에를리키아 차펜시스(Ehrlichia chaffeensis) 면역반응성 표면 단백질 p156을 암호화하는 DNA.
- 제7항에 따른 DNA와 이 DNA를 세포에서 발현시키는데 필요한 조절 요소를 포함하는 벡터.
- 제8항에 있어서, DNA가 서열번호 1에 제시된 아미노산 서열을 갖는 p156 단백질을 암호화하는 벡터.
- 서열번호 1에 제시된 아미노산 서열을 갖는 p156 단백질을 암호화하는 제8항에 따른 벡터로 형질감염된 숙주 세포.
- 제10항에 있어서, 세포가 세균 세포, 포유동물 세포, 식물 세포 및 곤충 세포로 이루어진 그룹 중에서 선택되는 숙주 세포.
- (a) 서열번호 1의 아미노산 서열을 갖는 p156 단백질을 암호화하는 분리된 DNA; 및(b) 유전자 코드의 축퇴성으로 인해 코돈 서열이 (a)의 분리된 DNA와 상이한 분리된 DNA로 이루어진 그룹 중에서 선택되는 DNA에 의해 암호화되는, 분리 및 정제된 에를리키아 차펜시스(Ehrlichia chaffeensis) 면역반응성 표면 단백질 p156.
- 제6항에 따른 p153 단백질에 대해 유도된 항체.
- 제12항에 따른 p156 단백질에 대해 유도된 항체.
- 제6항에 따른 p153 단백질을 포함하는, 개의 에를리키아증(ehrlichiosis)에 대한 백신.
- 제12항에 따른 p156 단백질을 포함하는, 개의 에를리키아증에 대한 백신.
- 개의 혈청이 서열번호 2의 아미노산 서열을 갖는 이. 캐니스(E.canis) p153 단백질 또는 서열번호 1의 아미노산 서열을 갖는 이. 차펜시스(E. chaffeensis) p156 단백질과 반응하는지의 여부를 측정하는 단계를 포함하고, 여기서 p153 단백질 또는 p156 단백질과의 반응이 상기 개가 각각 에를리키아 캐니스(Ehrlichia canis) 및 에를리키아 차펜시스(Ehrlichia chaffeensis)에 감염되었음을 나타내는 것인, 개의 에를리키아 종에 의한 감염 여부를 측정하는 방법.
- 제17항에 있어서, 단백질이 재조합 단백질인 방법.
- 제17항에 있어서, 개의 혈청이 상기 단백질과 반응하는지의 여부를 측정하는데 웨스턴 블롯 분석이 사용되는 방법.
- 제17항에 있어서, 개의 혈청이 이. 캐니스 p28 단백질과 반응하는지의 여부를 측정하는 단계를 추가로 포함하고, 여기서 서열번호 2의 아미노산 서열을 갖는 p153 단백질 및 p28 단백질 모두와의 면역반응성이 상기 개의 에를리키아 캐니스에 의한 감염을 나타내는 것인 방법.
- a) 서열번호 2의 아미노산 서열을 갖는 이. 캐니스(E.canis) p153 항원 및 서열번호 1의 아미노산 서열을 갖는 이. 차펜시스(E. chaffeensis) p156 항원으로부터 선택된 하나 이상의 에를리키아 항원;b) 개 혈청에 적당한 희석 완충액;c) 리포터 분자가 결합된 개의 항혈청 제2 항체; 및d) 상기 리포터 분자 검출에 적당한 시약을 포함하는, 개의 에를리키아 종에 의한 감염 여부를 측정하는 혈청진단 키트.
- 제21항에 있어서, 에를리키아 p28 항원 및 에를리키아 p43 항원으로부터 선택된 하나 이상의 항원을 추가로 포함하는 키트.
- 제21항 또는 제22항에 있어서, 에를리키아 항원이 막이나 미세역가 플레이트에 고정화된 키트.
- 제21항 또는 제22항에 있어서, 리포터 분자가 루시퍼라제, 서양고추냉이 퍼옥시다제, β-갈락토시다제 및 형광성 표지로 이루어진 그룹 중에서 선택되는 키트.
- 개의 혈액으로부터 DNA를 추출하는 단계;서열번호 2의 아미노산 서열을 갖는 p153 단백질을 암호화하는 이. 캐니스(E.canis) p153 유전자 또는 서열번호 1의 아미노산 서열을 갖는 p156 단백질을 암호화하는 이. 차펜시스(E. chaffeensis) p156 유전자에 특이적인 올리고뉴클레오타이드 프라이머를 이용하여 상기 DNA상에서 PCR 증폭을 수행하는 단계;수득되는 PCR 산물을 크기별로 분리하는 단계를 포함하고,여기서, 적당한 크기의 증폭 산물의 양성 검출이 이. 캐니스 또는 이. 차펜시스 감염을 나타내는 것인, 개가 에를리키아 종으로 감염되었는지의 여부를 측정하는 방법.
- 제25항에 있어서, PCR 산물이 겔 전기영동에 의해 검출되는 방법.
- a) 혈액으로부터 DNA를 추출하는 시약,b) 서열번호 2의 아미노산 서열을 갖는 p153 단백질을 암호화하는 이. 캐니스(E.canis) p153 유전자-특이적 또는 서열번호 1의 아미노산 서열을 갖는 p156 단백질을 암호화하는 이. 차펜시스(E. chaffeensis) p156 유전자-특이적 올리고뉴클레오타이드; 및c) PCR 증폭용 시약을 포함하는, 개의 에를리키아 종에 의한 감염 여부를 측정하기 위한 키트.
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US7842474B2 (en) | 2005-04-04 | 2010-11-30 | Idexx Laboratories, Inc. | Ehrlichia canis DIVA (differentiate infected from vaccinated animals) |
WO2006107924A2 (en) * | 2005-04-04 | 2006-10-12 | Idexx Laboratories, Inc. | Ehrlichia canis diva (differentiate infected from vaccinated animals) |
CA2612302C (en) | 2005-06-16 | 2015-07-28 | Research Development Foundation | Immunoreactive protein orthologs of ehrlichia canis and e. chaffeensis |
PT2187958T (pt) | 2007-09-11 | 2017-03-17 | Yissum Res Dev Company Of The Hebrew Univ Of Jerusalem | Vacina atenuada de erliquiose |
WO2009039414A2 (en) | 2007-09-21 | 2009-03-26 | Idexx Laboratories, Inc. | Methods and compositions for detection of ehrlichia chaffeensis (vlpt) |
EP2045816A1 (en) * | 2007-10-01 | 2009-04-08 | Paul Scherrer Institut | Fast readout method and swiched capacitor array circuitry for waveform digitizing |
EP2664344B1 (en) | 2007-10-31 | 2019-02-27 | Idexx Laboratories, Inc. | Ehrlichia canis diva (differentiate infection from vaccinated animals) |
JP5677703B2 (ja) * | 2008-01-10 | 2015-02-25 | リサーチ ディベロップメント ファウンデーション | Ehrlichiachaffeensisにのためのワクチンおよび診断 |
AU2010321790B2 (en) | 2009-11-20 | 2016-08-04 | Zoetis Services Llc | Peptides, devices, and methods for the detection of Ehrlichia antibodies |
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US9651546B2 (en) | 2012-10-11 | 2017-05-16 | Abaxis, Inc. | Peptides, devices, and methods for the detection of ehrlichia antibodies |
US9194870B2 (en) | 2014-01-21 | 2015-11-24 | Abaxis, Inc. | Peptides, devices, and methods for the detection of Anaplasma antibodies |
US9442112B2 (en) | 2014-04-04 | 2016-09-13 | Abaxis, Inc. | Compositions and methods for identifying Ehrlichia species |
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US6207169B1 (en) * | 1997-03-21 | 2001-03-27 | Corixa Corporation | Compounds and methods for the diagnosis and treatment of Ehrlichia infection |
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JP4494974B2 (ja) | 2010-06-30 |
US20040121433A1 (en) | 2004-06-24 |
CN100386430C (zh) | 2008-05-07 |
CN101294162A (zh) | 2008-10-29 |
EP1581638B1 (en) | 2007-09-05 |
US7204992B2 (en) | 2007-04-17 |
US7754224B2 (en) | 2010-07-13 |
CA2504762A1 (en) | 2004-05-21 |
AU2003290575A1 (en) | 2004-06-07 |
BR0315980A (pt) | 2005-09-20 |
EP1581638A1 (en) | 2005-10-05 |
JP2006505270A (ja) | 2006-02-16 |
ATE372378T1 (de) | 2007-09-15 |
US20070218082A1 (en) | 2007-09-20 |
BRPI0315980B1 (pt) | 2016-03-29 |
CN101294162B (zh) | 2011-03-30 |
DE60316189T2 (de) | 2007-12-20 |
DE60316189D1 (de) | 2007-10-18 |
AU2003290575B2 (en) | 2009-10-29 |
KR20050084679A (ko) | 2005-08-26 |
EP1581638A4 (en) | 2005-12-28 |
CN1735684A (zh) | 2006-02-15 |
ES2293057T3 (es) | 2008-03-16 |
WO2004042037A1 (en) | 2004-05-21 |
MXPA05004804A (es) | 2005-12-05 |
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