KR20170121194A - 세포 내로의 보툴리눔 신경독소의 특이적 흡수를 향상시키는 방법 - Google Patents
세포 내로의 보툴리눔 신경독소의 특이적 흡수를 향상시키는 방법 Download PDFInfo
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Abstract
본 발명은 세포 내로의 신경독소 폴리펩티드의 특이적 흡수를 향상시키는 방법을 제공하며, 이 방법은 신경독소 중독에 민감한 세포를 신경독소 폴리펩티드와 함께, 상기 신경독소 폴리펩티드가 그의 생물학적 활성을 발휘할 수 있게 하는 시간 동안 그리고 그렇게 하는 조건 하에서 인큐베이션하여, 상기 세포 내로의 상기 신경독소 폴리펩티드의 특이적 흡수를 향상시키는 단계를 포함하며, 상기 인큐베이션은 하기 단계 중 적어도 하나를 포함한다: (i) 상기 세포의 K+ 매개 탈분극, (ii) 감소된 신경독소 폴리펩티드 제시(exposition) 시간 및/또는 (iii) 신경독소 폴리펩티드 제시 동안 상기 세포의 교반. 또한, 본 발명은 세포에서 신경독소 폴리펩티드의 생물학적 활성을 직접 결정하는 방법에 관한 것으로, 이 방법은 a) 신경독소 중독에 민감한 세포를 신경독소 폴리펩티드와 함께, 상기 신경독소 폴리펩티드가 그의 생물학적 활성을 발휘할 수 있게 하는 시간 동안 그리고 그렇게 하는 조건 하에서 인큐베이션하는 단계 - 상기 인큐베이션은 하기 단계 중 적어도 하나를 포함함: (i) 상기 세포의 K+ 매개 탈분극, (ii) 감소된 신경독소 폴리펩티드 제시 시간 및/또는 (iii) 신경독소 폴리펩티드 제시 동안 상기 세포의 교반 -; b) 상기 세포를 고정시키고, 선택적으로 표면활성제(detergent)를 사용하여 상기 세포를 투과화(permeabilize)하는 단계; c) 상기 세포를, 비-절단(non-cleaved) 기질과 신경독소 절단 기질에 특이적으로 결합하는 적어도 제1 포획 항체 및 상기 신경독소 절단 기질의 절단 부위에 특이적으로 결합하는 적어도 제2 포획 항체와, 상기 기질에 대한 상기 포획 항체의 결합을 가능하게 하는 조건 하에서 접촉시키는 단계; d) 상기 세포를, 상기 제1 포획 항체에 특이적으로 결합하는 적어도 제1 검출 항체와, 상기 제1 포획 항체에 대한 상기 제1 검출 항체의 결합을 가능하게 하는 조건 하에서 접촉시켜 제1 검출 복합체를, 그리고 상기 제2 포획 항체에 특이적으로 결합하는 적어도 제2 검출 항체와, 상기 제2 포획 항체에 대한 상기 제2 검출 항체의 결합을 가능하게 하는 조건 하에서 접촉시켜 제2 검출 복합체를 형성하는 단계; e) 단계 d)의 상기 제1 검출 복합체와 상기 제2 검출 복합체의 양을 결정하는 단계; 및 f) 상기 세포에서 상기 신경독소 폴리펩티드에 의해 절단된 기질의 양을 상기 제2 검출 복합체로 계산하여 상기 세포에서 상기 신경독소 폴리펩티드의 생물학적 활성을 결정하는 단계를 포함한다.
Description
본 발명은 세포 내로의 신경독소 폴리펩티드의 특이적 흡수를 향상시키는 방법을 제공하며, 이 방법은 신경독소 중독에 민감한 세포를 신경독소 폴리펩티드와 함께, 상기 신경독소 폴리펩티드가 그의 생물학적 활성을 발휘할 수 있게 하는 시간 동안 그리고 그렇게 하는 조건 하에서 인큐베이션하여, 상기 세포 내로의 상기 신경독소 폴리펩티드의 특이적 흡수를 향상시키는 단계를 포함하며, 상기 인큐베이션은 하기 단계 중 적어도 하나를 포함한다: (i) 상기 세포의 K+ 매개 탈분극, (ii) 감소된 신경독소 폴리펩티드 제시(exposition) 시간 및/또는 (iii) 신경독소 폴리펩티드 제시 동안 상기 세포의 교반. 또한, 본 발명은 세포에서 신경독소 폴리펩티드의 생물학적 활성을 직접 결정하는 방법에 관한 것으로, 이 방법은 a) 신경독소 중독에 민감한 세포를 신경독소 폴리펩티드와 함께, 상기 신경독소 폴리펩티드가 그의 생물학적 활성을 발휘할 수 있게 하는 시간 동안 그리고 그렇게 하는 조건 하에서 인큐베이션하는 단계 - 상기 인큐베이션은 하기 단계 중 적어도 하나를 포함함: (i) 상기 세포의 K+ 매개 탈분극, (ii) 감소된 신경독소 폴리펩티드 제시 시간 및/또는 (iii) 신경독소 폴리펩티드 제시 동안 상기 세포의 교반 -; b) 상기 세포를 고정시키고, 선택적으로 표면활성제(detergent)를 사용하여 상기 세포를 투과화(permeabilize)하는 단계; c) 상기 세포를, 비-절단(non-cleaved) 기질과 신경독소 절단 기질에 특이적으로 결합하는 적어도 제1 포획 항체 및 상기 신경독소 절단 기질의 절단 부위에 특이적으로 결합하는 적어도 제2 포획 항체와, 상기 기질에 대한 상기 포획 항체의 결합을 가능하게 하는 조건 하에서 접촉시키는 단계; d) 상기 세포를, 상기 제1 포획 항체에 특이적으로 결합하는 적어도 제1 검출 항체와, 상기 제1 포획 항체에 대한 상기 제1 검출 항체의 결합을 가능하게 하는 조건 하에서 접촉시켜 제1 검출 복합체를, 그리고 상기 제2 포획 항체에 특이적으로 결합하는 적어도 제2 검출 항체와, 상기 제2 포획 항체에 대한 상기 제2 검출 항체의 결합을 가능하게 하는 조건 하에서 접촉시켜 제2 검출 복합체를 형성하는 단계; e) 단계 d)의 상기 제1 검출 복합체와 상기 제2 검출 복합체의 양을 결정하는 단계; 및 f) 상기 세포에서 상기 신경독소 폴리펩티드에 의해 절단된 기질의 양을 상기 제2 검출 복합체로 계산하여 상기 세포에서 상기 신경독소 폴리펩티드의 생물학적 활성을 결정하는 단계를 포함한다.
클로스트리디움 보툴리눔(Clostridium botulinum) 및 클로스트리디움 테타니(Clostridium tetani)는 매우 강력한 신경독소, 즉, 보툴리눔 독소 (BoNT) 및 파상풍 독소 (TeNT)를 각각 생성시킨다. 이러한 클로스트리움 신경독소 (Clostridial neurotoxin, CNT)는 신경 세포에 특이적으로 결합하여 신경전달물질 방출을 방해한다. 각각의 독소는 비활성의 처리되지 않은 대략 150 kDa 단일 사슬 단백질로 합성된다. 번역후 처리는 이황화물 다리의 형성 및 세균 프로테아제(들)에 의한 제한된 단백분해 (닉형성(nicking))를 포함한다. 활성 신경독소는 이황화물 결합에 의해 연결된 대략 50 kDa의 N-말단 경쇄와 대략 100 kDa의 중쇄인 2개의 사슬로 이루어진다. CNT는 구조적으로 그리고 기능적으로 3개의 도메인, 즉, 촉매 경쇄, 전좌 도메인 (N-말단 절반)을 포함하는 중쇄 및 수용체 결합 도메인 (C-말단 절반)으로 이루어진다 (예를 들어, 문헌[Krieglstein 1990, Eur. J. Biochem. 188, 39]; 문헌[Krieglstein 1991, Eur. J. Biochem. 202, 41]; 문헌[Krieglstein 1994, J. Protein Chem. 13, 49] 참조). 보툴리눔 신경독소는 150 kDa 신경독소 단백질 및 회합된 비독성 단백질을 포함하는 분자 복합체로 합성된다. 복합체 크기는 클로스트리디움 균주 및 별개의 신경독소 혈청형에 따라 300 kDa로부터 500 kDa을 초과하여 900 kDa의 범위로 상이하다. 이러한 복합체 중의 비독성 단백질은 신경독소를 안정화시키며, 분해로부터 이를 보호한다 (문헌[Silberstein 2004, Pain Practice 4, S19 ― S26] 참조).
클로스트리디움 보툴리눔은 보툴리눔 신경독소 A 내지 G (BoNT/A 내지 BoNT/G)로 명명되는 7개의 항원적으로 별개인 혈청형을 분비한다. 모든 혈청형은 클로스트리디움 테타니에 의해 분비되는 관련 파상풍 신경독소 (TeNT)와 함께, Zn2+-엔도프로테아제(endoprotease)이며, 이는 SNARE 단백질을 절단함으로써 시냅스 세포외배출(synaptic exocytosis)을 블로킹한다 (문헌[Couesnon, 2006, Microbiology, 152, 759] 참조). CNT는 보툴리누스중독 및 파상풍에서 관찰되는 이완성 근육 마비(flaccid muscular paralysis)를 일으킨다 (문헌[Fischer 2007, PNAS 104, 10447] 참조). 최근에, 새로운 보툴리눔 독소 유형, 즉, BoNT/H가 확인되었다 (문헌[Barash and Arnon, J. Infect. Dis. (2014), 209 (2): 183-191] 및 문헌[Dover, Barash, Hill, Xie and Arnon, J. Infect. Dis. (2014), 209(2): 192-202] 참조).
독성 효과에도 불구하고, 보툴리눔 독소 복합체는 다수의 질병에서 치료제로 사용되어 왔다. 보툴리눔 독소 혈청형 A는 1989년에 미국에서 사시증(strabism), 안검연축(blepharospasm) 및 다른 장애의 치료를 위한 인체 사용에 대해 승인받았다. 이것은 보툴리눔 독소 A (BoNT/A) 단백질 제제로서, 예를 들어, 상표명 BOTOX (Allergan, Inc.)로 또는 상표명 DYSPORT/RELOXIN (Ipsen, Ltd)로 구매가능하다. 개선된 무복합체 보툴리눔 독소 A 제제는 상표명 XEOMIN (Merz Pharma GmbH & Co. KGaA)으로 구매가능하다. 치료적 적용을 위해, 제제는 치료될 근육에 직접 주사된다. 생리적 pH에서, 독소가 단백질 복합체로부터 방출되어, 원하는 약리학적 효과가 일어난다. 보툴리눔 독소의 효과는 단지 일시적인데, 이는 보툴리눔 독소의 반복 투여가 치료 효과를 유지하는 데 필요할 수 있는 이유이다.
클로스트리디움 신경독소는 수의근력(voluntary muscle strength)을 약화시키며, 사시증, 경부 근긴장이상을 비롯한 국소 근긴장이상 및 양성 본태성 안검연축에 대한 효과적인 치료제이다. 이것은 편측안면연축(hemifacial spasm) 및 국소 경직(focal spasticity)을 완화시키고, 더욱이 위장 장애, 다한증 및 미용 주름 교정(cosmetic wrinkle correction)과 같은 광범위한 다른 적응증에 효과적인 것으로 추가로 밝혀졌다(문헌[Jost 2007, Drugs 67, 669] 참조).
클로스트리디움 신경독소의 제조 과정 동안, 상기 신경독소의 정량적 및 정성적 결정뿐만 아니라 생물학적 활성 신경독소 폴리펩티드의 품질 제어도 특히 중요하다. 또한, 정부 기관은 간단하고 신뢰성 있으며 검증된 보툴리눔 독소 활성 검정만을 인정한다. 현재, 치사율 시험인 마우스 LD50 생물학적 검정이 제약 업체가 그의 제제의 효력을 분석하는 데 사용하는 "최적 표준(gold standard)"을 유지하고 있다 (문헌[Arnon et al. (2001), JAMA 285, 1059-1070] 참조). 그러나, 최근 몇 년 동안, 동물 시험에 대한 필요성, 및 이러한 유형의 동물 기반 검정과 관련된 모든 단점, 비용 및 윤리적 우려를 줄이기 위한 대안적인 접근법을 찾으려는 상당한 노력이 기울여져 왔다. 또한, 규제 당국은 보툴리눔 신경독소의 효력 시험에 하기 3가지 "R" 원칙을 적용하도록 제약 회사를 참여시키고 있다: "줄이고(Reduce), 개량하고(Refine), 대체하라(Replace)" (문헌[Straughan, Altern. Lab. Anim. (2006), 34, 305-313] 참조). 결과적으로, 살아있는 동물을 사용하는 방법에 대한 합리적인 대안을 제공하기 위해 세포 기반 시험 시스템이 개발되었다. 그러나, 지금까지 단지 3가지의 세포 시험 시스템만이 신경독소 생물학적 활성의 결정에 이용가능하며, 이들은 신경독소 폴리펩티드에 충분히 감수성인 것으로 밝혀졌다. 이들 세포 기반 시험 시스템은 시험관내(in vitro)에서 분화된 설치류 배아로부터 단리된 1차 뉴런 (문헌[Pellett et al. (2011), Biochem. Biophys. Res. Commun. 404, 388-392]), 신경 분화 유도 만능성 줄기 세포 (문헌[Whitemarsh et al. (2012), Toxicol. Sci. 126, 426-35]) 및 SiMa 세포주의 서브클론 (국제특허 공개 WO 2010/105234 A1호)의 사용을 포함한다.
그러나, 1차 뉴런의 단리는 동물의 치사를 필요로 하며, 수고롭고 시간이 많이 걸린다. 또한, 다양한 1차 뉴런을 사용하는 시험 시스템은 큰 변동을 나타낸다. 유사하게, 신경 분화 유도 만능성 줄기 세포의 생성은 어렵고 시간이 많이 걸린다. 또한, 이러한 세포의 보관은 아주 문제가 많다. 종양 세포주를 사용하는 검정은 자주 BoNT에 충분히 감수성이지 않다. 더욱이, 상기 종양 세포주에 대해서는 복잡한 분화 프로토콜이 요구되며, 이는 상기 세포주를 사용하는 검정의 높은 실패율 및/또는 큰 변동을 초래한다.
상기에 비추어, 신경독소 폴리펩티드 활성의 결정을 위한 추가 시험 시스템이 매우 요망된다.
따라서, 본 발명의 기저를 이루는 기술적인 문제는 전술한 필요성에 부응하는 수단 및 방법의 제공으로 볼 수 있다. 그 기술적 문제는 청구범위 및 이하 본 명세서에 특징지어져 있는 실시 형태에 의해 해결된다.
일 태양에서, 본 발명은 세포 내로의 신경독소 폴리펩티드의 특이적 흡수를 향상시키는 방법에 관한 것으로, 이 방법은,
신경독소 중독에 민감한 세포를 신경독소 폴리펩티드와 함께, 상기 신경독소 폴리펩티드가 그의 생물학적 활성을 발휘할 수 있게 하는 시간 동안 그리고 그렇게 하는 조건 하에서 인큐베이션하여, 상기 세포 내로의 상기 신경독소 폴리펩티드의 특이적 흡수를 향상시키는 단계를 포함하며, 상기 인큐베이션은 하기 단계 중 적어도 하나를 포함한다: (i) 상기 세포의 K+ 매개 탈분극, (ii) 감소된 신경독소 폴리펩티드 제시 시간 및/또는 (iii) 신경독소 폴리펩티드 제시 동안 상기 세포의 교반. 바람직하게는, 이 방법은 시험관내 방법이다.
클로스트리디움 신경독소 폴리펩티드는 시냅스 말단 내에서 신경전달물질 방출을 블로킹하도록 작용한다. 신경독소는 신경막 수용체에 결합하고, 엔도솜 유사 구획 내로 흡수되어, pH 의존성 전좌 과정을 통해 엔도솜막에 침투함으로써 뉴런에 진입한다. 일단 시냅스 세포질 내에 존재하면, 클로스트리디움 신경독소는 시냅스 소포 융합에 필요한 이의 상응하는 SNARE 단백질 기질을 절단한다.
더 구체적으로는, 클로스트리디움 신경독소는 전시냅스(pre-synaptic) 신경 말단으로부터 신경전달물질의 분비를 특이적으로 억제한다는 것을 특징으로 한다. 말초 뉴런에 대한 선택성은 SV2 및 GT1b와 같은 다양한 수용체의 인식에 의해 매개된다. 예를 들어, 전시냅스 신경 말단 내로의 BoNT/A의 특이적 흡수는 고친화성 수용체와 저친화성 수용체의 조합을 수반하는 엄격히 제어되는 다단계 과정이다. 강글리오시드 GT1b에 대한 결합은 초기 결합 단계를 매개하고, 이를 통해 BoNT/A를 세포 표면 상에 농축시킨다. 일단 막에 고정되면, 원형질막 내에서의 측방향 이동이 BoNT/A와, SV2 또는 FGFR3과 같은 추가의 (단백질) 수용체와의 분자간 상호작용을 촉진시킨다. BoNT/A에 대한 수용체는 수용체 결합 도메인의 C-말단 부분 내에 결합 포켓(binding pocket)을 갖는 강글리오시드 GT1b이다. APR 수용체 모델에 따르면, 전시냅스 막의 마이크로도메인(microdomain)에 클러스터링된 일련의 전시냅스 수용체 (APR)가 BoNT/A를 비롯한 신경독소의 특이적 흡수를 담당한다. 강글리오시드 GT1b에 대한 결합은 초기 결합 단계를 매개하고 BoNT/A를 세포 표면 상에 농축시킨다. 일단 막에 고정되면, 원형질막 내에서의 측방향 이동이 BoNT/A와, 시냅스 소포 (Synaptic Vesicle, SV) 당단백질 2의 3가지 동형(isoform)인 SV2A (ENSG00000159164), SV2B (ENSG00000185518) 및 SV2C (ENSG00000122012)를 비롯한 단백질 수용체와의 분자간 상호작용을 촉진하며, 이들 수용체는 전시냅스 막에 대한 시냅스 소포의 융합 후 외부 원형질막 상에 노출된다. BoNT/A는 SV2의 네 번째 루미날 도메인(luminal domain) (LD4)을 특이적으로 인식한다. SV2와 상호작용하는 BoNT/A 결합 도메인의 특정 서열은 아직 확인되지 않았다. 당화된 SV2A, SV2B 및 SV2C가 또한 BoNT/F에 대한 수용체로 확인되었으며, 당화된 SV2A 및 SV2B는 BoNT/E에 대한 수용체로 확인되었다. BoNT/D는 2개의 강글리오시드 결합 부위를 통해 뉴런에 진입하는 것으로 보고되었는데, 하나의 부위는 BoNT/A, BoNT/B, BoNT/E, BoNT/F 및 BoNT/G에서 이전에 확인된 위치에 존재하고, 다른 부위는 TeNT의 두 번째 강글리오시드 결합 포켓과 유사하다. 최근에, 또한 BoNT/D가 SV2 (3가지 모든 동형)를 사용하여 해마 뉴런에 진입하는 것으로 밝혀졌지만, BoNT/D는 BoNT/A 및 BoNT/E와는 별개의 메커니즘을 통해 SV2와 결합하였다. SV2A와 SV2B가 또한 중추 뉴런 내로의 TeNT의 결합 및 진입을 매개하는 것으로 보고되었다 (문헌[Jacky et al., PLoS Pathog. 2013 May; 9(5): e1003369] 및 그 문헌에 인용된 참고문헌 참조).
신경독소의 생리적 효과는 수용체의 결합과 신경독소 경쇄의 전좌에 후속하는 SNARE 복합체의 단백질 절단에 기초한다. 클로스트리디움 신경독소의 생물학적 활성의 결정은 상기 신경독소 단백질의 특징규명에서 중요한 측면이며, 특히 클로스트리디움 신경독소 함유 제품의 허가(clearance)를 위해 규제 당국에 의해 요구된다. 따라서, 클로스트리디움 신경독소의 생물학적 활성의 측정을 위한 신뢰성 있는 시험은 클로스트리디움 신경독소를 함유하는 제품의 연구, 개발 및 마케팅을 위한 기초이다. 또한, 세포 기반 시험 시스템은 지금까지 지배적이었던 동물 시험을 윤리적인 이유로 대체할 것이다. 이러한 세포 기반 시험 시스템을 확립하기 위해서는, 클로스트리디움 신경독소에 대한 신경 세포 또는 세포주의 충분한 고감수성이 필수적이다.
클로스트리디움 신경독소 중독에 민감한 세포 내로의 클로스트리디움 신경독소 폴리펩티드의 특이적 흡수가 하기 단계 중 적어도 하나에 의해 증가될 수 있다는 것이 본 발명자들에 의해 유리하게 발견되었다: (i) 세포의 K+ 매개 탈분극, (ii) 감소된 신경독소 폴리펩티드 제시 시간 또는 (iii) 신경독소 폴리펩티드 제시 동안 세포의 교반. 동시에, 신경독소 폴리펩티드 또는 이의 분해 생성물의 비특이적 흡수는 이러한 조치에 의해 감소될 수 있다. 특히, 언급된 신경독소 또는 이의 분해 생성물의 비특이적 세포 흡수는 세포가 신경독소와 함께 인큐베이션되는 시간의 감소에 의해 감소된다. 세포의 K+ 매개 탈분극은 신경독소의 특이적 흡수를 자극한다. 또한, 신경독소 중독 시 세포의 교반은 신경막에 인접한 수용체부위 농도(biophase concentration)에 영향을 미치고, 이에 따라 세포 내로의 신경독소의 비특이적 흡수를 감소시킬뿐만 아니라 특이적 흡수를 증가시킬 수 있다. 상응하는 데이터는 하기 실시예에 제시되어 있다. 또한, 도 1은 스트레스 처리(stressed) 샘플이 기준 검정인 마우스 LD50 생물학적 검정에 필적하는 감쇠 반응속도론을 나타내는 3가지의 세포 기반 검정례의 비교를 도시한다
따라서, 본 발명의 방법의 일 태양에서, 신경독소 폴리펩티드 또는 이의 분해 생성물의 비특이적 세포 흡수는 감소된다.
또한, 본 발명은, 예를 들어 보툴리눔 신경독소의 안정성 보관의 결과로서의 분해에 의한, 손상된 분자에 대한 선택성을 포함한다. 신경전달물질의 방출이 K+ 매개 탈분극에 의해 유도됨에 따라, 이어지는 소포의 재흡수 증가는 GT1b 및/또는 SV2 단백질 패밀리 구성원과 같은 수용체에 대한 결합에 의한 특이적 흡수를 포함한다. 손상된 분자는 수용체에 대한 더 약한 결합을 나타내거나 결합을 나타내지 않을 수 있다. 진탕(shaking)과 같은 물리적인 영향에 대해서도 마찬가지이다. 손상된 분자의 덜 안정한 결합은 진탕에 의해 심지어 감소될 것이다.
신경독소 중독에 민감한 세포 내로의 신경독소 폴리펩티드의 특이적 흡수를 향상시키기 위해, 세포를 신경독소 폴리펩티드와, 신경독소 폴리펩티드가 그의 생물학적 활성을 발휘할 수 있게 하는 시간 동안 그리고 그렇게 하는 조건 하에서 인큐베이션한다. 그러한 시간 및 세포 배양 조건은 당업계에 공지되어 있다. 본 발명의 방법에서, 세포 배양 조건은 하기 단계 중 적어도 하나를 포함한다: (i) 세포의 K+ 매개 탈분극, (ii) 감소된 신경독소 폴리펩티드 제시 시간 또는 (iii) 신경독소 폴리펩티드 제시 동안 세포의 교반. 본 발명의 방법은 또한 언급된 단계 중 두 단계, 예를 들어 단계 (i)과 단계 (ii), 단계 (i)과 단계 (iii), 단계 (ii)와 단계 (iii), 또는 단계 (i) 내지 단계 (iii)의 세 단계 모두를 포함할 수 있다. 세포 배양 조건은 각각의 하기 단계, 즉, (i) 세포의 K+ 매개 탈분극, (ii) 감소된 신경독소 폴리펩티드 제시 시간 및 (iii) 신경독소 폴리펩티드 제시 동안 세포의 교반을 포함하는 것이 바람직하다.
통상, 당업계에서 신경독소 활성 검정에 사용되는 세포 배양 배지는 약 5 mM의 K+를 함유한다. 뉴런은 통상 배지로부터 세포 내로 K+ 이온을 그리고 세포액으로부터 원형질막을 통해 세포의 외부로 Na+ 이온을 능동 수송함으로써 이온 구배를 확립한다. 결과는 막 전위인데, 이는 세포에 의해 엄격히 조절되며, 세포들 사이의 통신을 비롯한 여러 가지 다양한 세포 과정의 기초가 된다. 원형질막의 특정 이온 투과도의 갑작스러운 변화 또는 막의 어느 한 쪽에서의 이온 조성의 급격한 변경은 탈분극이라 일컬어지는 막 전위의 변화를 가져온다 세포의 K+ 매개 탈분극은 세포 배양 배지 내의 증가된 K+ 농도, 예를 들어 약 10 mM, 20 mM, 30 mM, 40 mM, 50 mM 또는 55 mM의 추가 K+ 농도에서 수행할 수 있다. 본 발명의 방법에서 최종 K+ 농도는 약 15 mM, 25 mM, 30 mM, 35 mM, 40 mM, 45 mM, 50 mM, 55 mM 또는 60 mM K+일 수 있다. K+ 매개 탈분극을 위한 시간은 적어도 약 30분, 1시간, 1시간 30분, 2시간, 2시간 30분, 3시간 또는 심지어 그 이상이다.
세포의 K+ 매개 탈분극 및/또는 신경독소 폴리펩티드 제시는 강글리오시드 GT1b의 존재 하에 수행할 수 있다. GT1b는 약 5 μM, 10 μM, 15 μM, 20 μM, 25 μM, 30 μM, 35 μM, 40 μM, 45 μM, 50 μM, 55 μM 또는 60 μM, 바람직하게는 약 15 μM 내지 약 50 μM, 더 바람직하게는 약 20 μM의 농도로 사용할 수 있다.
당업계에서 사용되는 신경독소 폴리펩티드 제시 시간은 통상 약 4시간 내지 약 96시간, 자주 약 72시간이다. 감소된 신경독소 폴리펩티드 제시 시간은 적어도 24 시간 내지 96시간 미만 동안, 바람직하게는 적어도 48시간, 적어도 60시간, 그리고 최대 72시간 동안 신경독소 폴리펩티드를 사용한 세포의 중독이다.
신경독소 폴리펩티드 제시 동안 세포의 교반은 당업계에 공지된 수단 및 방법, 예를 들어 자석 교반기, 회전 스피너 플라스크(rotating spinner flask) 또는 진탕기를 이용한 세포의 진탕을 사용하여 수행할 수 있다. 세포의 교반은 조직 플라스크로부터의 세포의 탈착을 회피하는 적절한 세포 배양 배지 유속(medium flow rate)에서 수행한다. 배지의 적합한 평균 유속은, 예를 들어, 약 25 cm/분 내지 약 300 cm/분이다.
전술한 세포의 K+ 매개 탈분극을 또한 GT1b 및 신경독소 폴리펩티드의 존재 하에 수행한 후, 교반 하에서 추가 시간, 예를 들어 약 24시간, 36시간, 48시간, 60시간 또는 72시간 동안 신경독소 폴리펩티드 제시를 수행할 수 있다.
또한, 신경독소 폴리펩티드가 없는 상태의 인큐베이션 시간이 신경독소 폴리펩티드 제시보다 선행되는 것이 고찰된다. 예를 들어, 신경독소 폴리펩티드가 없는 상태의 인큐베이션 시간은 약 6시간, 12시간, 18시간, 24시간, 30시간, 36시간, 42시간, 48시간, 54시간 또는 60시간, 바람직하게는 약 16시간 내지 약 48시간일 수 있다.
본 발명의 방법의 추가의 바람직한 실시 형태는 하기 실시예로부터 도출될 수 있다.
본 명세서에 지칭되는 바와 같이, 용어 "신경독소 폴리펩티드" 또는 간략하게 "신경독소" 또는 "독소"는 클로스트리디움 신경독소, 즉, 클로스트리디움 보툴리눔 및 클로스트리디움 테타니 신경독소, 특히 보툴리눔 신경독소 (BoNT) 및 파상풍 신경독소 (TeNT)를 의미한다. 더 구체적으로는, 상기 용어는 BoNT/A, BoNT/B, BoNT/C1, BoNT/D, BoNT/E, BoNT/F, BoNT/G, BoNT/H (문헌[Barash and Arnon, J. Infect. Dis. (2014), 209 (2): 183-191]) 및 파상풍 신경독소 (TeNT)뿐만 아니라 이의 서브타입(subtype)을 포함한다. 예를 들어, BoNT/A의 서브타입은 BoNT/A1, BoNT/A2, BoNT/A3, BoNT/A4 및 BoNT/A5를 포함한다. BoNT/B 서브타입은, 예를 들어, BoNT/B1, BoNT/B2, BoNT/B3, BoNT/B4, BoNT/B5, BoNT/B6, BoNT/B7 및 BoNT/B8을 포함한다. BoNT/C 서브타입은, 예를 들어, BoNT/Cl-1 및 BoNT/Cl-2를 포함한다. 또한, BoNT/D-C 서브타입이 포함된다. BoNT/E 서브타입은, 예를 들어, BoNT/E1, BoNT/E2, BoNT/E3, BoNT/E4, BoNT/E5, BoNT/E6, BoNT/E7, BoNT/E8 및 BoNT/E9를 포함한다. 또한, BoNT/F 서브타입은, 예를 들어, BoNT/F1, BoNT/F2, BoNT/F3, BoNT/F4, BoNT/F5, BoNT/F6 및 BoNT/F7을 포함한다. 추가의 서브타입은, 예를 들어, Hill 등의 문헌[J Bacteriol. 2007 Feb; 189(3): 818-32. Epub 2006 Nov 17.]에 기재되어 있으며, 그 개시 내용은 본 명세서에 참고로 포함된다. 신경독소 폴리펩티드, 특히 그의 경쇄 및 중쇄는 보툴리눔 신경독소의 항원적으로 상이한 혈청형 또는 상기 나타낸 서브타입 중 하나로부터 유도가능하다. 일 태양에서, 신경독소 폴리펩티드의 상기 경쇄 및 중쇄는 하기로 이루어진 군으로부터 선택된 신경독소의 경쇄 및 중쇄이다: BoNT/A, BoNT/B, BoNT/C1, BoNT/D, BoNT/E, BoNT/F, BoNT/G, BoNT/H 또는 TeNT. 다른 태양에서, 상기 신경독소 폴리펩티드를 인코딩(encoding)하는 폴리뉴클레오티드는 서열 번호 1 (BoNT/A), 서열 번호 3 (BoNT/B), 서열 번호 5 (BoNT/C1), 서열 번호 7 (BoNT/D), 서열 번호 9 (BoNT/E), 서열 번호 11 (BoNT/F), 서열 번호 13 (BoNT/G) 또는 서열 번호 15 (TeNT)로 제시된 바와 같은 핵산 서열을 포함한다. 더욱이, 일 태양에서, 서열 번호 2 (BoNT/A), 서열 번호 4 (BoNT/B), 서열 번호 6 (BoNT/C1), 서열 번호 8 (BoNT/D), 서열 번호 10 (BoNT/E), 서열 번호 12 (BoNT/F), 서열 번호 14 (BoNT/G) 또는 서열 번호 16 (TeNT) 중 어느 하나로 제시된 바와 같은 아미노산 서열을 인코딩하는 핵산 서열을 포함하는 폴리뉴클레오티드가 포함된다. 또한, 본 발명의 방법의 일 태양에서, 서열 번호 2 (BoNT/A), 서열 번호 4 (BoNT/B), 서열 번호 6 (BoNT/C1), 서열 번호 8 (BoNT/D), 서열 번호 10 (BoNT/E), 서열 번호 12 (BoNT/F), 서열 번호 14 (BoNT/G) 및 서열 번호 16 (TeNT)으로 이루어진 군으로부터 선택된 아미노산 서열을 포함하거나 이로 이루어진 신경독소 폴리펩티드가 포함된다. 또한, 예를 들어, 문헌[Dover, N. et al., (2014), J Infect Dis 209(2): 192-202]에 제시된 바와 같은 최근 기술된 BoNT/H의 상응하는 핵산 및 아미노산 서열이 포함된다.
다른 태양에서, 상기 폴리뉴클레오티드는 전술한 폴리뉴클레오티드 또는 폴리펩티드의 변이체이다. 변이체는 전술한 클로스트리디움 신경독소 동형 또는 서브타입과 같은 자연 발생적 신경독소 폴리뉴클레오티드 또는 폴리펩티드일 수 있다. 예를 들어, 보툴리눔 신경독소의 각 혈청형 내에는 아미노산 서열이 다소 상이한 그리고 이러한 단백질을 인코딩하는 핵산이 또한 다소 상이한 자연 발생적 보툴리눔 신경독소 변이체가 존재할 수 있음이 당업자에 의해 인식된다.
변이체는 또한 비-자연 발생적(non-naturally occurring) 신경독소 폴리펩티드일 수 있다. 본 명세서에 사용되는 바와 같이, 클로스트리디움 신경독소의 "비-자연 발생적 변이체"라는 용어는, 제한 없이, 유전 공학 또는 재조합 방법에 의해, 예를 들어 무작위 돌연변이유발 또는 합리적 설계를 사용하여 생성된 클로스트리디움 신경독소, 효소 활성, 예를 들어 내부단백분해 효소(endoproteolytic enzyme) 또는 외부단백분해 효소(exoproteolytic enzyme)에 의해 변형된 클로스트리디움 신경독소의 효소 변형 변이체, 또는 화학 합성에 의해 생성된 클로스트리디움 신경독소를 비롯한 인위적 조작의 도움으로 생성된 클로스트리디움 신경독소를 의미한다. "유전자 조작"은 클로스트리디움 신경독소를 인코딩하는 유전자 또는 DNA 또는 mRNA와 같은 각각의 핵산을 변형시킴으로써 임의의 혈청형/서브타입의 천연 클로스트리디움 신경독소를 변형시키는 당업계에 공지된 방법을 지칭한다. 신경독소 폴리펩티드를 인코딩하는 폴리뉴클레오티드 또는 신경독소 폴리펩티드의 유전 공학을 위한 재조합 방법은 당업계에 잘 기술되어 있다 (예를 들어, 문헌[Sambrook, J. & Russell, D. (2001). Molecular Cloning: a Laboratory Manual, 3rd edn. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory] 참조).
더욱이, 다른 태양에서, 본 명세서에 지칭되는 바와 같이 자연 발생적 또는 비-자연 발생적 변이체 폴리뉴클레오티드는 서열 번호 1, 서열 번호 3, 서열 번호 5, 서열 번호 7, 서열 번호 9, 서열 번호 11, 서열 번호 13 또는 서열 번호 15 중 어느 하나에 제시된 바와 같은 핵산 서열 또는 문헌[Dover, N. et al., (2014), J Infect Dis 209(2): 192-202]에 제시된 바와 같은 BoNT/H의 핵산 서열과 적어도 40%, 적어도 50%, 적어도 60%, 적어도 70%, 적어도 75%, 적어도 80%, 적어도 85%, 적어도 90%, 적어도 95%, 적어도 96%, 적어도 97%, 적어도 98% 또는 적어도 99% 동일한 핵산 서열 변이체, 또는 서열 번호 2, 서열 번호 4, 서열 번호 6, 서열 번호 8, 서열 번호 10, 서열 번호 12, 서열 번호 14 또는 서열 번호 16 중 어느 하나에 제시된 바와 같은 아미노산 서열 또는 문헌[Dover, N. et al., (2014), J Infect Dis 209(2): 192-202]에 제시된 바와 같은 BoNT/H의 아미노산 서열과 적어도 40%, 적어도 50%, 적어도 60%, 적어도 70%, 적어도 75%, 적어도 80%, 적어도 85%, 적어도 90%, 적어도 95%, 적어도 96%, 적어도 97%, 적어도 98% 또는 적어도 99% 동일한 아미노산 서열을 인코딩하는 핵산 서열 변이체를 포함한다. 본 명세서에 사용되는 바와 같이, 용어 "동일한"은 두 핵산 서열 또는 두 아미노산 서열 사이의 동일한 아미노산의 수를 결정함으로써 특징지어지는 서열 동일성을 지칭하며, 여기서 서열들은 최대 순서 일치가 얻어지도록 정렬된다. 이는, 예를 들어, BLASTP, BLASTN 또는 FASTA와 같은 컴퓨터 프로그램으로 체계화된 공개된 기법 또는 방법을 사용하여 계산할 수 있다 (문헌[Altschul 1990, J Mol Biol 215, 403]). 일 태양에서, 동일성 퍼센트 값은 전체 아미노산 서열, 예를 들어 신경독소 폴리펩티드의 경쇄 또는 중쇄 또는 둘 모두에 대하여 계산한다. 다양한 서열을 비교하기 위해 다양한 알고리즘을 기반으로 하는 일련의 프로그램이 당업자에게 이용가능하다. 이와 관련하여, Needleman과 Wunsch 또는 Smith와 Waterman의 알고리즘이 특히 신뢰성 있는 결과를 제공한다. 서열 정렬을 수행하기 위해, GCG 소프트웨어 패킷(software packet) (미국 53711 위스콘신주 매디슨 사이언스 드라이브 575 소재의 Genetics Computer Group 1991)의 일부인, 프로그램 PileUp (문헌[Higgins 1989, CABIOS 5, 151]) 또는 프로그램 Gap 및 BestFit (문헌[Needleman 1970, J Mol Biol 48; 443]; 문헌[Smith 1981, Adv Appl Math 2, 482])를 사용할 수 있다. 본 발명의 다른 태양에서, 퍼센트 (%)로 상기 열거된 서열 동일성 값은 전체 서열 영역에 대하여 프로그램 GAP을 하기 설정으로 사용하여 결정될 것이며: 갭 중량: 50, 길이 중량: 3, 평균 일치: 10.000 및 평균 불일치: 0.000, 달리 명시되지 않는 한, 이 설정이 항상 서열 정렬을 위한 표준 설정으로 사용될 것이다. 일 태양에서, 전술한 변이체 폴리뉴클레오티드 각각은 각각의 신경독소 폴리펩티드, 즉, BoNT/A, BoNT/B, BoNT/C1, BoNT/D, BoNT/E, BoNT/F, BoNT/G, BoNT/H 또는 파상풍 신경독소 (TeNT)의 본 명세서에 정의된 생물학적 특성 중 하나 이상을, 그리고 다른 태양에서는 이들 특성 모두를 보유하는 폴리펩티드를 인코딩한다. 당업자는 단백분해 활성화 후에만 완전한 생물학적 활성이 유지된다는 것을 인식하겠지만, 처리되지 않은 전구체가 일부 생물학적 기능을 발휘하거나 부분적으로 활성일 수 있음이 고려된다. 클로스트리디움 신경독소의 생물학적 활성을 평가하는 생체내(in vivo) 검정은, Pearce 등의 문헌[Pearce 1994, Toxicol. Appl. Pharmacol. 128: 69-77] 및 Dressler 등의 문헌([Dressler 2005, Mov. Disord. 20:1617-1619], 문헌[Keller 2006, Neuroscience 139: 629-637])에 기술된 바와 같은 마우스 LD50 검정 및 생체외(ex vivo) 마우스 편측횡격막 검정(mouse hemidiaphragm assay)을 포함한다. 생물학적 활성은 통상 마우스 유닛 (Mouse Unit, MU)으로 표현된다. 본 명세서에 사용되는 바와 같이, 1 MU는 복강내 주사 후 특정 마우스 집단의 50%를 치사시키는 신경독소 성분의 양, 즉, 마우스 i.p. LD50이다. 추가의 태양에서, 변이체 폴리뉴클레오티드는 개선된 또는 변경된 생물학적 특성을 갖는 신경독소를 인코딩할 수 있는데, 예를 들어 이것은 효소 인식을 위해 개선된 절단 부위를 포함할 수 있고/있거나 수용체 결합, 내재화, 엔도솜막을 가로질러 세포액 내로의 전좌 또는 SNARE 단백질 패밀리의 상응하는 기질의 내부단백분해 절단을 위해 개선될 수 있다.
비-자연 발생적 클로스트리디움 신경독소 변이체의 비제한적인 예는, 예를 들어, 보존성 클로스트리디움 신경독소 변이체를 포함한다. 본 명세서에 사용되는 바와 같이, 용어 "보존성 클로스트리디움 신경독소 변이체"는 적어도 하나의 아미노산이 다른 아미노산에 의해 치환된 클로스트리디움 신경독소, 또는 본 명세서의 다른 곳에 제시된 바와 같은 기준 클로스트리디움 신경독소 서열의 본래의 아미노산, 예를 들어, 서열 번호 2, 서열 번호 4, 서열 번호 6, 서열 번호 8, 서열 번호 10, 서열 번호 12, 서열 번호 14 또는 서열 번호 16으로 제시된 아미노산 서열 또는 문헌[Dover, N. et al., (2014), J Infect Dis 209(2): 192-202]에 제시된 바와 같은 BoNT/H의 아미노산 서열의 특성과 유사한 적어도 하나의 특성을 갖는 아미노산 유사체를 의미한다. 변이체는 기준 서열과 비교하여 1개, 2개, 3개, 4개, 5개 또는 심지어 그 이상의 보존성 아미노산 치환을 가질 수 있다. 변이체는 기준 클로스트리디움 신경독소 서열과 필적하는 또는 심지어 그에 비해 개선된 특성을 가질 것이다. 특성의 예는, 제한 없이, 유사한 크기, 토포그래피(topography), 전하, 소수성, 친수성, 친지성, 공유 결합 능력, 수소 결합 능력, 물리화학적 특성 등, 또는 이들의 임의의 조합을 포함한다. 바람직하게는, 특성은 본 명세서의 다른 곳에 정의된 바와 같은 생물학적 특성, 즉, (a) 수용체 결합, (b) 내재화, (c) 엔도솜막을 가로질러 세포액 내로의 전좌, 및/또는 (d) 시냅스 소포막 융합에 관여하는 단백질의 내부단백분해 절단이다. 보존성 클로스트리디움 신경독소 변이체는 그 보존성 클로스트리디움 신경독소 변이체의 기초가 되는 기준 클로스트리디움 신경독소와 실질적으로 동일한 방식으로 기능할 수 있으며, 본 발명의 임의의 태양에서 기준 클로스트리디움 신경독소 대신 사용할 수 있다. 본 명세서에 기재된 클로스트리디움 신경독소는 전형적으로 자연 발생적 아미노산 잔기를 함유할 것이지만, 일부의 경우에는 비-자연 발생적 아미노산 잔기도 존재할 수 있다. 따라서, 특정 아미노산 또는 펩티드의 구조를 모방하는 비-아미노산 화학 구조를 포함할 수 있는, 소위 "펩티드 모방체(peptide mimetic)" 및 "펩티드 유사체"를 본 발명의 맥락 내에서 사용할 수도 있다. 이러한 모방체 또는 유사체는 대체로, 유사한 크기, 전하 또는 소수성과 같은 물리적 특징, 및 그의 천연 펩티드 대응물에서 발견되는 적절한 공간 배향을 나타내는 것으로 특징지어진다. 펩티드 모방체 화합물의 특정 예는 당업계에 잘 공지되어 있는 바와 같이 하나 이상의 아미노산 사이의 아미드 결합이, 예를 들어, 탄소-탄소 결합 또는 다른 비-아미드 결합에 의해 대체된 화합물이다 (예를 들어, 문헌[Sawyer, in Peptide Based Drug Design, pp. 378-422, ACS, Washington D.C. 1995] 참조).
본 명세서에 사용되는 바와 같이, 신경독소 폴리펩티드 변이체는 화학적으로 변형된 신경독소 폴리펩티드를 추가로 포함한다. 본 명세서에 사용되는 바와 같이, "화학적 변형"은 대체로, 화학 반응 등으로 임의의 혈청형 또는 서브타입의 천연 또는 재조합 클로스트리디움 신경독소를 변형시키는 당업계에 공지된 방법을 지칭하며, 이는 특히, 클로스트리디움 신경독소의 아미노산의 치환, 결실, 삽입, 첨가 또는 번역후 변형을 지칭한다. 화학적으로 변형된 신경독소 폴리펩티드는 피루브산화(pyruvation), 인산화, 황산화, 지질화, 페길화, 당화 및/또는 아미노산 또는, 예를 들어 약 2개 내지 약 500개의 아미노산을 포함하는 폴리펩티드의 화학적 첨가에 의해 변형된 것일 수 있다. 예를 들어, 히알루론산 또는 폴리비닐피롤리돈 또는 폴리에틸렌글리콜 또는 이들의 혼합물을 신경독소 폴리펩티드 내로 혼입시킴으로써, 클로스트리디움 신경독소, 또는 화학적 변형 또는 유전자 조작에 의해 클로스트리디움 독소로부터 유도된 독소를 안정화시킬 수 있다.
본 발명의 방법에 사용될 수 있는 클로스트리디움 신경독소의 다른 비-자연 발생적 변이체는 하이브리드 클로스트리디움 신경독소이다. 일 태양에서, 하이브리드 클로스트리디움 신경독소는 클로스트리디움 신경독소 중쇄와 경쇄의 조합을 포함하며, 그 경쇄와 중쇄는 동일한 혈청형 또는 서브타입을 갖지 않는다.
클로스트리디움 신경독소의 이러한 화학적, 효소적 또는 유전자적으로 변형된 변이체를 제조하는 방법, 및 이러한 변이체가 (a) 수용체 결합, (b) 내재화, (c) 엔도솜막을 가로질러 세포액 내로의 전좌, 및/또는 (d) 시냅스 소포막 융합에 관여하는 단백질의 내부단백분해 절단과 같은 본 명세서에 지칭된 생물학적 특성을 유지하는지의 여부를 확인하는 방법은 당업자에게 잘 공지되어 있다 (예를 들어, 문헌[Sambrook, loc. cit] 참조).
본 명세서에 사용되는 바와 같이, 용어 "신경독소 폴리펩티드의 생물학적 활성"은 신경독소 폴리펩티드에 특징적인 생물학적 특성, 즉, (a) 수용체 결합, (b) 내재화, (c) 엔도솜막을 가로질러 세포액 내로의 전좌, 및/또는 (d) 시냅스 소포막 융합에 관여하는 단백질의 내부단백분해 절단을 의미한다. 본 명세서에 사용되는 바와 같이, 신경독소 폴리펩티드는 상기 언급된 특성 a) 내지 d) 중 적어도 하나, 바람직하게는 시냅스 소포막 융합에 관여하는 단백질의 내부단백분해 절단, 또는 a) 내지 d)에 열거된 2가지 또는 3가지 또는 4가지 모두의 생물학적 특성을 나타내는 것으로 고찰된다. 신경독소 폴리펩티드의 생물학적 활성을 결정하는 검정은 당업계에 잘 공지되어 있으며, 본 명세서의 다른 곳에도 기재되어 있다 (예를 들어, 문헌[Pellett et al. (2011), Biochem. Biophys. Res. Commun. 404, 388-392]; 문헌[Whitemarsh et al. (2012), Toxicol. Sci. 126, 426-35] 참조).
SNAP-25는 BoNT/A, BoNT/C1 및 BoNT/E의 공지된 기질이고 그에 의해 절단된다. VAMP/시냅토브레빈(Synaptobrevin)은 BoNT/B, BoNT/D, BoNT/F, BoNT/G 및 TeNT의 기질이고 그에 의해 절단되는 반면, 신택신(Syntaxin)은 BoNT/C1의 기질이고 그에 의해 절단된다. 언급된 기질 및 상응하는 핵산과 아미노산 서열은 당업계에 잘 공지되어 있다 (예를 들어, 국제특허 공개 WO 2014/207109호 참조).
본 명세서에 사용되는 바와 같이, 용어 "세포"는, 예를 들어, BoNT/A와 같은 신경독소에 의한 신경독소 중독에 민감한 임의의 진핵 세포, 또는 신경독소를 흡수할 수 있는 임의의 진핵 세포를 지칭한다. 본 발명의 태양은 확립된 세포주로부터의 세포를 부분적으로 포함한다. 용어 "세포"는 다양한 유기체로부터의 세포, 예를 들어 뮤린(murine), 래트, 돼지, 소, 말, 붉은털원숭이(rhesus), 영장류 및 인간 세포; 다양한 세포 유형으로부터의 세포, 예를 들어 신경 세포 및 비-신경 세포를 포함하며, 불균일한 세포 집단, 조직 또는 유기체로부터 단리되거나 그의 일부일 수 있다. 본 명세서에 사용되는 바와 같이, 용어 "확립된 세포주"는 "불멸 세포주" 또는 "형질전환 세포주"와 동의어이며, 유기체, 조직 또는 기관 공급원으로부터 유래된 세포 집단의 무한 증식(indefinite propagation)을 위해 선택된 세포의 세포 배양물을 지칭한다. 정의상, 확립된 세포주는 1차 세포의 세포 배양물을 배제한다. 본 명세서에 사용되는 바와 같이, 용어 "1차 세포"는 신선한 조직 또는 기관으로부터 직접 수집된 세포이며, 무한 증식할 잠재성을 갖지 않는다. 예를 들어, 1차 신경 세포를 본 발명의 방법에 사용할 수 있다. 확립된 세포주는 세포의 불균일한 집단 또는 세포의 균일한 집단을 포함할 수 있다. 단일 세포로부터 유래된 확립된 세포주는 클론 세포주라 지칭된다. 확립된 세포주는 세포가 전체 세포 메커니즘을 거치는 데 필요한 모든 성분을 내인적으로 발현하는 것일 수 있는데, 이때 전체 세포 메커니즘에서는 BoNT/A와 같은 신경독소가 SNAP-25와 같은 기질을 단백분해 절단하고, 신경독소 수용체에 대한 신경독소의 결합, 예를 들어 BoNT/A 수용체에 대한 BoNT/A의 결합, 신경독소/수용체 복합체의 내재화, 세포내 소포로부터 세포질 내로의 신경독소 경쇄의 전좌 및 신경독소 기질의 단백분해 절단을 포함한다. 대안적으로, 확립된 세포주는 세포가 전체 세포 메커니즘을 거치는 데 필요한 적어도 하나의 성분을 외인성 공급원으로부터 도입한 것일 수 있는데, 이때 전체 세포 메커니즘에서는 BoNT/A와 같은 신경독소가 SNAP-25와 같은 기질을 단백분해 절단하고, 수용체에 대한 신경독소의 결합, 예를 들어 BoNT/A 수용체에 대한 BoNT/A의 결합, 신경독소/수용체 복합체의 내재화, 세포내 소포로부터 세포질 내로의 신경독소 경쇄의 전좌 및 신경독소 기질의 단백분해 절단을 포함한다. 또한, 유전자 조작 세포주로 지칭되는 경우, 그러한 확립된 세포주로부터의 세포는, 예를 들어, 외인성 FGFR2, 외인성 FGFR3, 외인성 SV2, SNAP-25와 같은 외인성 신경독소 기질, 또는 이들의 임의의 조합을 발현할 수 있다.
본 명세서에 사용되는 바와 같이, "세포 배양"은 가장 넓은 의미로 동물 또는 인간으로부터의 세포의 분리 및 유리한 인공 환경에서의 이의 후속 성장을 지칭한다. 세포는 조직으로부터 직접 분리되어 배양 전에 효소적 또는 기계적 수단에 의해 탈응집될 수 있거나, 이미 확립된 세포주 또는 세포 계통으로부터 유래될 수 있다. 1차 배양은, 세포가 조직으로부터 단리되어 적절한 조건 하에서 이용가능한 기질의 전부를 점유할 때까지, 즉, 컨플루언스(confluence)에 도달할 때까지 증식된 후의 배양의 단계를 지칭한다. 이 단계에서, 세포를 계대 배양해야 하는데, 즉, 신선한 성장 배지가 있는 새로운 용기로 옮겨서 계대하여 지속적인 성장을 위한 더 많은 공간을 제공한다. 정상적인 세포는 통상 이의 증식 능력을 상실하기 전에 제한된 횟수로만 분열하는데, 이는 노화로 알려진 유전자적으로 결정되는 사건이며, 이러한 세포주는 유한한 것으로 알려져 있다. 그러나, 일부 세포주는 형질전환이라 일컬어지는 과정을 통해 불멸 상태가 되는데, 이는 자발적으로 발생할 수 있거나 화학적으로 또는 바이러스에 의해 유도될 수 있다. 유한한 세포주가 형질전환을 거쳐서 무한히 분열하는 능력을 획득한 경우, 이것은 연속 세포주가 된다. 배양 조건은 각 세포 유형에 대해 매우 다양하지만, 세포가 배양되는 인공 환경은 변함없이 하기가 담긴 적합한 용기로 이루어진다: 필수 영양소 (아미노산, 탄수화물, 비타민, 무기질), 성장 인자, 호르몬, 가스 (O2, CO2)를 공급하는 기질 또는 배지, 조절되는 물리화학적 환경 (pH, 삼투압, 온도) 등. 대부분의 세포는 고정 의존성(anchorage-dependent)이며, 배양되는 동안 고체 또는 반고체 기질에 붙어 있어야 하는 (부착 배양 또는 단층 배양) 반면, 다른 세포는 배양 배지에서 부유 상태로 성장할 수 있다 (현탁 배양).
본 명세서에 나타낸 바와 같이, 용어 "신경독소 중독에 민감한 세포(들)"는 전체 세포 메커니즘을 거칠 수 있는 세포를 의미하는데, 이때 전체 세포 메커니즘에서는 신경독소 폴리펩티드 (예를 들어, BoNT/A)가 신경독소 기질 (예를 들어, BoNT/A 기질인 SNAP-25)을 절단하고, 상응하는 수용체에 대한 신경독소 폴리펩티드의 결합 (예를 들어, BoNT/A 수용체에 대한 BoNT/A의 결합), 신경독소/수용체 복합체의 내재화, 세포내 소포로부터 세포질 내로의 신경독소 경쇄의 전좌 및 신경독소 기질의 단백분해 절단을 포함한다. 따라서, 본 명세서에 사용되는 바와 같이, "신경독소 중독에 민감한 세포"는 신경독소 감수성 세포를 의미한다. 언급된 용어는 세포 또는 세포주, 예를 들어 단리된 1차 세포 또는 이의 세포주 또는 확립된 세포주의 세포 또는 확립된 세포주, 예를 들어 본 명세서의 다른 곳에 정의된 바와 같은 신경모세포종 세포 또는 신경모세포종 세포주와 같은 신경 세포로 분화할 수 있는 종양 세포 또는 종양 세포주를 포함한다. 예를 들어, 상기 신경모세포종 세포주는 DSMZ로부터 구매가능한 SiMa 세포주 (ACC 164)일 수 있다. 세포주 SiMa의 특정 클론은 또한 국제특허 공개 WO 2010/105234호에 개시되어 있다. 본 발명의 방법에 사용될 수 있는 다른 신경모세포종 세포주는 ATCC 또는 DSMZ로부터 하기 ATCC 또는 DSMZ 번호로 입수할 수 있다: 세포주 N1E-115는 CRL-2263으로, 세포주 Neuro2a는 CCL-131로, 세포주 SH-SY5Y는 CRL-2266으로, 세포주 PC12는 CRL-1721로, 세포주 MHH-NB-11은 ACC 157 (DSMZ)로 그리고 세포주 SK-N-BE(2)는 CRL-2271로. 신경독소 중독에 민감한 다른 종양 세포는 P-19 세포 (뮤린 배아 암종 세포주) (DSMZ 번호 ACC 316)이다. 일부 태양에서, 예를 들어 활성 검정의 경우, 상기 세포를 신경 세포로 분화시키는 것이 필요할 수 있다. 이러한 분화 방법은 문헌에 잘 기술되어 있다. 신경독소 중독에 민감한 세포에는 유도 만능성 줄기 세포 (iPS) 유래 뉴런, 바람직하게는 인간 유도 만능성 줄기 세포 (iPS) 유래 뉴런이 추가로 포함된다 (예를 들어, 문헌[Whitemarsh et al. (2012), loc. cit] 참조). 이러한 인간 iPS 유래 뉴런은 또한, 예를 들어, Cellular Dynamics로부터 구매가능하다. iPS 세포를 생성시키는 방법은, 예를 들어, Yu 등의 문헌[ Science 2009 May 8; 324(5928): 797-801. Epub 2009], 국제특허 공개 WO 2011/056971호 및 국제특허 공개 WO 2011/025852호에 기술되어 있다. 일부 태양에서, iPS는 적합한 방법, 예를 들어 국제특허 공개 WO 2012/135621호 및 미국 특허 출원 공개 제2010/0279403호 및 미국 특허 출원 공개 제2010/0216181호에 기술된 방법을 사용하여 뉴런으로 분화시킨다.
본 명세서에 사용되는 바와 같이, 용어 "분화", "분화하는" 또는 "분화된"은 특수화되지 않은 또는 비교적 덜 특수화된 세포가 비교적 더 특수화되는 과정을 의미한다. 세포 개체발생의 맥락에서, 형용사 "분화된"은 상대적인 용어이다. 따라서, "분화된 세포"는 비교되는 세포보다 특정 발달 경로를 따라 추가로 진행된 세포이다. 분화된 세포는, 예를 들어, 최종 분화된 세포, 즉, 유기체의 다양한 조직 및 기관에서 특수화된 기능을 획득하고 유사분열 후일 수 있지만 그러하지 않아도 되는, 완전 특수화된 세포일 수 있다. 예를 들어, iCell® 뉴런은 인간 iPS 세포로부터 최종 분화되며, 신경 특징 및 기능을 나타낸다. 다른 예에서, 분화된 세포는 분화 계열 내의 전구 세포일 수도 있으며, 이는 추가로 증식 및/또는 분화할 수 있다. 유사하게는, 세포는 이와 비교되는 세포보다 특정 발달 경로를 따라 추가로 진행된 경우 "비교적 더 특수화된" 것인데, 따라서 비교되는 세포는 "특수화되지 않은" 또는 "비교적 덜 특수화된" 것으로 간주된다. 비교적 더 특수화된 세포는, 하나 이상의 입증가능한 표현형 특징, 예를 들어 특정 세포 성분 또는 생성물, 예컨대 RNA, 단백질, 특정 세포 마커 또는 다른 물질의 존재, 부재 또는 발현 수준, 특정 생화학적 경로의 활성, 형태학적 외관, 증식 능력 및/또는 반응속도론, 분화 잠재력 및/또는 분화 신호에 대한 반응 등에서 특수화되지 않은 세포 또는 비교적 덜 특수화된 세포와 상이할 수 있으며, 이때 이러한 특징들은 상기 발달 경로를 따른 비교적 더 특수화된 세포의 추가 진행을 나타낸다. 세포를 신경 세포로 분화시키기 위한 세포 배양 조건은 본 명세서에 인용된 문헌으로부터 명백한 바와 같이 당업계에 잘 공지되어 있다.
또한, 신경독소 중독에 민감한 세포를 신경독소 폴리펩티드와 함께, 신경독소 폴리펩티드가 그의 생물학적 활성을 발휘할 수 있게 하는 시간 동안 그리고 그렇게 하는 조건 하에서 인큐베이션하기 위한 세포 배양 조건은 당업계에 잘 기술되어 있으며, 본 명세서에 언급된 간행물로부터도 도출할 수 있다.
본 명세서에 사용되는 바와 같이, 용어 "신경독소 폴리펩티드의 특이적 흡수"는 신경독소 폴리펩티드가 그의 특정 신경막 수용체(들), 예를 들어 SV2, 강글리오시드, GD1a, BoNT/B에 대한 시냅토태그민(Synaptotagmin) II, 또는 BoNT/D/-C에 대한 시냅토태그민 I에 결합하고, 엔도솜 유사 구획 내로 흡수되어, pH 의존성 전좌 과정을 통해 엔도솜막에 침투함으로써 뉴런에 진입하는 과정을 의미한다. 따라서, 언급된 용어는 a) 신경독소 폴리펩티드의 수용체 결합, b) 신경독소 폴리펩티드의 내재화, 및 c) 엔도솜막을 가로질러 세포액 내로의 신경독소 폴리펩티드의 전좌를 포함한다. 당업자에 의해 인식되는 바와 같이, 신경독소 감수성 세포는 바람직하게는 신경독소를 먼저 흡수할 수 있고, 이어서 상기 열거된 전체 세포 메커니즘을 거친다. 본 명세서에 나타낸 바와 같이, 표현 "신경독소 폴리펩티드의 비-특이적 또는 비특이적 흡수"는 신경독소 폴리펩티드 또는 이의 분해 생성물이, 비-특이적 신경막 수용체(들)에 결합하거나, 예를 들어 음세포작용(pinocytosis)의 경우 우발적 공동 수송에 의한 것과 같은 비특이적 메커니즘을 통해 세포에 진입함으로써 뉴런에 진입하는 과정을 의미한다. 본 명세서에 사용되는 바와 같이, 신경독소 감수성 세포는, 예를 들어, 약 100 나노몰 (nM), 약 10 nM, 약 1 nM, 약 500 피코몰 (pM), 약 400 pM, 약 300 pM, 약 200 pM, 약 100 pM, 약 90 pM, 약 80 pM, 약 70 pM, 약 60 pM, 약 50 pM, 약 40 pM, 약 30 pM, 약 20 pM, 약 10 pM, 약 9 pM, 약 8 pM, 약 7 pM, 약 6 pM, 약 5 pM, 약 4 pM, 약 3 pM, 약 2 pM, 약 1 pM, 약 0.5 pM, 또는 약 0.1 pM의 신경독소 폴리펩티드 또는 지시된 값들 중 하나의 값 미만의 신경독소 폴리펩티드를 흡수할 수 있다. 100 pM 초과의 EC50 값이 문헌에 보고되어 있다. 정의상, 신경독소 중독에 민감한 세포는 적어도 하나의 신경독소 수용체와 적어도 하나의 신경독소 기질을 발현해야 하거나 이를 발현하도록 조작되어야 한다. 신경독소에 대한 수용체 및 기질은 당업계에 기술되어 있으며, 본 명세서의 다른 곳에 언급되어 있다. 따라서, 상기 세포는 바람직하게는 본 명세서에 정의된 바와 같은 생물학적으로 활성인 또는 성숙한 신경독소 폴리펩티드에 민감하다. 바람직하게는, 본 명세서에 사용되는 바와 같이, 신경독소 감수성 세포는, 예를 들어, 약 1 nM 이하, 500 pM 이하, 약 400 pM 이하, 약 300 pM 이하, 약 200 pM 이하, 약 100 pM 이하, 약 90 pM 이하, 약 80 pM 이하, 약 70 pM 이하, 약 60 pM 이하, 약 50 pM 이하, 약 40 pM 이하, 약 30 pM 이하, 약 20 pM 이하, 약 10 pM 이하, 약 9 pM 이하, 약 8 pM 이하, 약 7 pM 이하, 약 6 pM 이하, 약 5 pM 이하, 약 4 pM 이하, 약 3 pM 이하, 약 2 pM 이하, 약 1 pM 이하, 약 0.9 pM 이하, 약 0.8 pM 이하, 약 0.7 pM 이하, 약 0.6 pM 이하, 약 0.5 pM 이하, 약 0.4 pM 이하, 약 0.3 pM 이하, 약 0.2 pM 이하, 또는 심지어 약 0.1 pM 이하로 신경독소 중독에 민감하다. 당업계에 공지된 바와 같이, "반수 최대 유효 농도(half maximal effective concentration) (EC50)"는 어떤 특정 노출 시간 후에 기준치(baseline)와 최대치 사이의 중간인 반응을 유도하는 약물, 항체 또는 독성물질의 농도를 지칭한다. 이는 통상 약물 효력의 척도로 사용된다. 따라서, 연속적(graded) 용량 반응 곡선의 EC50은 최대 효과의 50%가 관찰되는 화합물의 농도를 나타낸다. 불연속적(quantal) 용량 반응 곡선의 EC50은 노출 기간 후에 집단의 50%가 반응을 나타내는 화합물의 농도를 나타낸다. 신경독소 중독에 민감하고/하거나 신경독소 흡수 능력을 갖는 세포 또는 세포주, 즉, 본 명세서에 정의된 바와 같은 신경독소 감수성 세포의 확인 방법은 당업계에 공지되어 있다 (예를 들어, 미국 특허 출원 공개 제2012/0122128 A1호 참조). 일 태양에서, 신경독소 폴리펩티드의 생물학적 활성은 전술한 모든 생물학적 특성으로 인해 발생한다. 신경독소의 생물학적 활성의 결정에 사용될 수 있는, 신경독소에 대해 충분한 고감수성을 갖는 소수의 세포 기반 검정만이 지금까지 종래 기술에 기술되어 있으며, 이는 본 명세서의 다른 곳에 나타낸 바와 같다.
본 명세서에 사용되는 바와 같이, 용어 "향상시키는"은 (i) 세포의 K+ 매개 탈분극, (ii) 감소된 신경독소 폴리펩티드 제시 시간 및 (iii) 신경독소 폴리펩티드 제시 동안 세포의 교반을 사용하지 않는 클로스트리디움 신경독소 중독과 비교하여 세포 내로의 신경독소 폴리펩티드의 특이적 흡수가 개선 또는 증가됨을 의미한다. 세포 내로의 신경독소 폴리펩티드의 특이적 흡수는, (i) 세포의 K+ 매개 탈분극, (ii) 감소된 신경독소 폴리펩티드 제시 시간 및 (iii) 신경독소 폴리펩티드 제시 동안 세포의 교반을 포함하지 않는 세포 배양 조건을 사용하는 방법과 비교하여 바람직하게는 적어도 1.5배, 적어도 2배, 적어도 3배, 적어도 4배, 적어도 5배, 적어도 6배, 적어도 7배, 적어도 8배, 적어도 9배 또는 심지어 적어도 10배 증가된다. 대체로, 당업계에 기술된 방법은 약 5 mM의 최종 K+ 농도를 사용하고, 약 72시간의 신경독소 폴리펩티드 제시 시간을 사용하고, 세포의 교반은 사용하지 않는다. 상기 조치 (i), (ii) 및/또는 (iii)이 세포 내로의 신경독소의 특이적 흡수를 개선시킬 뿐만 아니라 세포 내로의 언급된 신경독소 또는 분해 생성물의 비특이적 흡수의 감소를 가져온다는 것이 본 발명자들에 의해 발견되었다. 세포 내로의 신경독소 폴리펩티드의 비특이적 흡수는, (i) 세포의 K+ 매개 탈분극, (ii) 감소된 신경독소 폴리펩티드 제시 시간 및/또는 (iii) 신경독소 폴리펩티드 제시 동안 세포의 교반을 포함하지 않는 세포 배양 조건을 사용하는 방법과 비교하여 바람직하게는 적어도 1.5배, 적어도 2배, 적어도 3배, 적어도 4배, 적어도 5배, 적어도 6배, 적어도 7배, 적어도 8배, 적어도 9배 또는 심지어 적어도 10배 감소된다. 세포 내로의 신경독소 폴리펩티드의 특이적 또는 비특이적 흡수를 측정하는 수단 및 방법은 문헌 및 본 명세서에 잘 기재되어 있으며, 하기 실시예에 추가로 제시되어 있다. 예를 들어, 신경 세포 배양에서 SNAP-25 단백분해에 대한 BoNT/A, BoNT/C 및 BoNT/E 신경독소 노출의 효과를 신경독소 전좌의 지표로 사용할 수 있다. 신경 세포에서 신택신 단백분해에 대한 BoNT/C 신경독소 노출 그리고 VAMP 단백분해에 대한 BoNT/E, BoNT/D 및 BoNT/G 신경독소 노출에 대해서도 마찬가지이다.
본 발명의 방법의 추가의 태양에서, 전술한 본 발명의 방법 다음으로 세포에서 신경독소 폴리펩티드의 생물학적 활성을 결정하는 방법이 이어진다.
하기 실시예에서 입증된 바와 같이, 세포의 K+ 매개 탈분극, 감소된 신경독소 폴리펩티드 제시 시간 및/또는 신경독소 폴리펩티드 제시 동안 세포의 교반을 사용하여 세포 내로의 클로스트리디움 신경독소 폴리펩티드의 특이적 흡수를 증가시킴으로써, 세포 기반 효력 검정이 유리하게 개선될 수 있다. 동시에, 세포 내로의 언급된 신경독소 또는 분해 생성물의 비특이적 흡수의 감소가 관찰될 수 있다.
예를 들어, SH-SY5Y 또는 Neuro2a 세포, 배아 닭 뉴런, 척수 또는 후근 신경절로부터의 1차 뉴런 (문헌[Pellett et al. (2011), Biochem. Biophys. Res. Commun. 404, 388 392]), 웨스턴 블롯 판독(Western blot read-out)에 의존하는 배아 줄기 세포 유래 뉴런 (문헌[Whitemarsh et al. (2012), Toxicol. Sci. 126, 426-35]), 또는 분화된 인간 신경모세포종 SiMa 세포를 사용하는 경쇄 검정 (ELISA), Endopep-MS, FRET, HPLC-UPLC, DARET 또는 세포 기반 검정과 같은, 신경독소 폴리펩티드의 생물학적 활성을 결정하기 위한 다수의 검정이 당업계에 기술되어 있다 (예를 들어, 문헌[, E. et al., (2012). PLoS One 7 (11)] 참조).
제2 태양에서, 본 발명은 세포에서 신경독소 폴리펩티드의 생물학적 활성을 직접 결정하는 방법을 제공하며, 이 방법은,
a)
신경독소 중독에 민감한 세포를 신경독소 폴리펩티드와 함께, 상기 신경독소 폴리펩티드가 그의 생물학적 활성을 발휘할 수 있게 하는 시간 동안 그리고 그렇게 하는 조건 하에서 인큐베이션하는 단계 - 상기 인큐베이션은 하기 단계 중 적어도 하나를 포함함: (i) 상기 세포의 K+ 매개 탈분극, (ii) 감소된 신경독소 폴리펩티드 제시 시간 및/또는 (iii) 신경독소 폴리펩티드 제시 동안 상기 세포의 교반 -;
b)
상기 세포를 고정시키고, 선택적으로 표면활성제를 사용하여 상기 세포를 투과화하는 단계;
c)
상기 세포를, 비-절단 기질과 신경독소 절단 기질에 특이적으로 결합하는 적어도 제1 포획 항체 및 상기 신경독소 절단 기질의 절단 부위에 특이적으로 결합하는 적어도 제2 포획 항체와, 상기 기질에 대한 상기 포획 항체의 결합을 가능하게 하는 조건 하에서 접촉시키는 단계;
d)
상기 세포를, 상기 제1 포획 항체에 특이적으로 결합하는 적어도 제1 검출 항체와, 상기 제1 포획 항체에 대한 상기 제1 검출 항체의 결합을 가능하게 하는 조건 하에서 접촉시켜 제1 검출 복합체를, 그리고 상기 제2 포획 항체에 특이적으로 결합하는 적어도 제2 검출 항체와, 상기 제2 포획 항체에 대한 상기 제2 검출 항체의 결합을 가능하게 하는 조건 하에서 접촉시켜 제2 검출 복합체를 형성하는 단계;
e)
단계 d)의 상기 제1 검출 복합체와 상기 제2 검출 복합체의 양을 결정하는 단계; 및
f)
상기 세포에서 상기 신경독소 폴리펩티드에 의해 절단된 기질의 양을 상기 제2 검출 복합체로 계산하여 상기 세포에서 상기 신경독소 폴리펩티드의 생물학적 활성을 결정하는 단계를 포함한다.
바람직하게는, 이 방법은 시험관내 방법이다. 본 발명의 이 방법은 세포에서 신경독소 폴리펩티드의 생물학적 활성을 직접 결정할 수 있게 한다. 이는 당업계에 기술된 방법에서와 같은 세포의 용해 및 세포 용해물로부터의 절단된 신경독소 기질의 단리 또는 농축이 더 이상 필요하지 않음을 의미한다. 예를 들어, 당업계의 웨스턴 블롯 분석 기반 검정의 경우, 신경독소 기질은 SDS 폴리아크릴아미드 겔에서 각각의 샘플의 성분들의 분리 및 농축에 의해 농축된다. 당업계에 기술된 ECL 샌드위치 ELISA의 경우, 신경독소 기질의 농축은 세포 용해물이 첨가되는 미세역가 플레이트 상의 절단된 신경독소 기질에 특이적으로 결합하는 항체를 사용하여 수행된다. 절단된 신경독소 기질은 언급된 항체의 결합에 의해 용해물로부터 단리되며, 이는 상기 절단된 클로스트리디움 신경독소 기질의 농축을 가져온다.
대조적으로, 본 발명의 이 방법에서는 절단된 신경독소 기질, 예를 들어 SNAP 25를 세포에서 직접 검출할 수 있다. 이를 위해, 본 명세서의 다른 곳에 더욱 상세히 정의된 바와 같은 신경독소 중독에 민감한 세포를 신경독소 폴리펩티드와, 신경독소 폴리펩티드가 그의 생물학적 활성을 발휘할 수 있게 하는 시간 동안 그리고 그렇게 하는 조건 하에서 인큐베이션한다. 인큐베이션은 본 명세서의 다른 곳에 제시된 바와 같이 세포의 K+ 매개 탈분극, 감소된 신경독소 폴리펩티드 제시 시간 및/또는 신경독소 폴리펩티드 제시 동안 세포의 교반을 포함한다. 이러한 조치는 신경독소의 특이적 세포 흡수를 향상시키는 동시에, 세포 내로의 신경독소 또는 분해 생성물의 비특이적 흡수를 감소시킨다. 다음 단계에서는, 예를 들어, 고정제, 예컨대 메탄올, 에탄올, 아세톤, 포름알데하이드 또는 언급된 고정제의 혼합물을 첨가하여 세포를 고정시킨다. 선택적으로, Triton X-100, Tween 20, 사포닌, 디지토닌(Digitonin) 또는 n-옥틸-β-글루코피라노시드와 같은 적어도 하나의 표면활성제를 사용하여 세포를 투과화할 수 있다. 표면활성제는 PBS와 같은 적절한 완충액에 포함될 수 있다. 그 후, 세포를, 비-절단 기질과 신경독소 절단 기질에 특이적으로 결합하는 적어도 제1 포획 항체 및 신경독소 절단 기질의 절단 부위에 특이적으로 결합하는 적어도 제2 포획 항체와, 상기 기질에 대한 상기 포획 항체의 결합을 가능하게 하는 조건 하에서 접촉시킨다. 이때, 제1 포획 항체는, 비-절단 신경독소 기질 및 신경독소 절단 신경독소 기질 둘 모두에 존재하는 적절한 에피토프에 특이적으로 결합함으로써, 세포에서 신경독소 기질의 총 함량 또는 총량을 결정할 수 있다. 제2 포획 항체는, 예를 들어 신경독소 기질의 신경독소 절단 부위에 특이적으로 결합함으로써, 절단된 신경독소 기질에만 존재하는 에피토프를 인식하여 이에 특이적으로 결합한다. 대안적으로, 세포를 상기 제1 포획 항체와 제2 포획 항체의 혼합물과 접촉시킬 수 있는데, 즉, 세포를 언급된 조건 하에서 적어도 제1 포획 항체 및 적어도 제2 포획 항체와 동시에 접촉시킨다. 다음 단계에서는, 세포를, 제1 포획 항체에 특이적으로 결합하는 적어도 제1 검출 항체와, 상기 제1 포획 항체에 대한 상기 제1 검출 항체의 결합을 가능하게 하는 조건 하에서 접촉시켜 제1 검출 복합체를 형성한다. 후속 단계에서는, 세포를, 제2 포획 항체에 특이적으로 결합하는 적어도 제2 검출 항체와, 상기 제2 포획 항체에 대한 상기 제2 검출 항체의 결합을 가능하게 하는 조건 하에서 접촉시켜 제2 검출 복합체를 형성한다. 대안적으로, 세포를, 상기 제1 검출 항체와 제2 검출 항체의 혼합물과 접촉시킬 수 있는데, 즉, 세포를 언급된 조건 하에서 적어도 제1 검출 항체 및 적어도 제2 검출 항체와 동시에 접촉시킨다. 대안적으로, 세포의 투과화 후에, 언급된 조건 하에서, 세포를 상기 제1 포획 항체와 제2 포획 항체 및 상기 제1 검출 항체와 제2 검출 항체의 혼합물과 동시에 접촉시킬 수 있다. 다음 단계에서는, 제1 검출 복합체와 제2 검출 복합체의 양을 결정한다. 최종적으로, 상기 세포에서 상기 신경독소 폴리펩티드에 의해 절단된 기질의 양을 제2 검출 복합체로 계산한다. 그렇게 하여, 상기 신경독소 폴리펩티드의 생물학적 활성을 세포에서 직접 결정한다.
하기에서, 본 발명의 이 방법을 더 상세하게 설명한다. 세포 배양을 위해, 본 명세서에 정의된 바와 같은 신경독소 중독에 민감한 세포, 예를 들어 신경 세포, SiMa 세포 또는 iPS 유래 뉴런을 먼저 96-웰 미세역가 플레이트 상에 시딩(seeding)한다. SiMa 세포는, 예를 들어, 국제특허 공개 WO 2010/105234호에 개시된 절차에 따라 신경 표현형으로 분화시키고, iPS 유래 뉴런은, 예를 들어, 국제특허 공개 WO 2012/135621호에 기술된 검정에 따라 신경 표현형으로 분화시킨다. 이어서, 세포를 BoNT/A와 같은 신경독소 폴리펩티드와 함께, 신경독소 폴리펩티드가 그의 생물학적 활성을 발휘할 수 있게 하는 시간 동안 그리고 그렇게 하는 조건 하에서 인큐베이션한다. 인큐베이션은 본 명세서의 다른 곳에 기재된 바와 같이 세포의 K+ 매개 탈분극, 감소된 신경독소 폴리펩티드 제시 시간 및/또는 신경독소 폴리펩티드 제시 동안 세포의 교반을 포함한다.
후속 단계에서는, ELISA 검정 전에, 세포를 미세역가 플레이트 상에 고정시킨다. 세포를 고정시키기 위해, 예를 들어 빙랭 메탄올 (-20℃)을 20℃에서 20분 동안 세포에 첨가할 수 있다.
ELISA 검정을 수행하기 위해, 세포를 먼저 세척한다. 세척 완충액으로서, 예를 들어 10 mM PBS 완충액 (pH 7.4) 중의 0.1% Triton X-100을 사용할 수 있다. 그 후, 10 mM PBS (pH 7.4) 중의 0.6% H2O2와 같은 켄칭 완충액(quenching buffer)으로 내인성 프로테아제를 켄칭시킨 다음, 다른 세척 단계를 수행한다. 다음 단계에서는, 예를 들어, 0.05% Triton X-100 및 10 mM PBS 완충액 (pH 7.4) 중의 2% BSA와 같은 적절한 블로킹 완충액으로 미세역가 플레이트 상의 자유 결합 부위를 블로킹한다. 이어서, 적절한 표면활성제를 사용하여 세포를 투과화한다. 투과화 완충액으로서, 예를 들어 10 mM PBS 완충액 중의 0.5% Triton X-100을 이용할 수 있다. 투과화는 세포에 형성된 공극을 통한 항체의 확산을 가능하게 한다. 그 후, 상기 언급된 바와 같이 세척 완충액으로 세포를 세척한다.
다음 단계에서는, 투과화된 세포를, 예를 들어, 2가지 상이한 항체의 혼합물과 함께 인큐베이션한다. 혼합물은 비-절단 기질과 신경독소 절단 기질에 특이적으로 결합하는 제1 포획 항체 및 신경독소 절단 기질의 절단 부위에 특이적으로 결합하는 제2 포획 항체를 포함한다. 상기 제1 포획 항체와 제2 포획 항체는 또한 순차적으로 적용할 수 있다. 예를 들어, 제1 포획 항체는 비-절단 SNAP 25와 신경독소 절단 SNAP 25 둘 모두에 특이적으로 결합하여, 세포에서 SNAP-25의 총량 또는 총 함량의 정량화를 가능하게 할 수 있다. 또한, 이 제1 포획 항체는 평가 시에 세포에서 절단된 SNAP 25의 양을 정규화하는 데 사용할 수 있다. 제2 포획 항체는 신경독소 절단 기질의 절단 부위에 특이적으로 결합하여, BoNT/A 절단 SNAP 25와 같은 절단된 신경독소 기질의 결정 및 검출을 가능하게 한다.
본 발명의 방법에서 총 신경독소 기질 및 신경독소 절단 신경독소 기질의 후속 검출은 미세역가 플레이트 또는 세포 배양 접시 상에서 직접, 즉, 세포 내에서 수행할 수 있다. 따라서, 유리하게도, 본 발명의 방법에서는, 당업계에 기술된 방법에서와 같은 세포 추출물을 준비하고 세포 용해물로부터 신경독소 기질을 단리하고/하거나 농축시키는 것이 필요 없다. 그 후, 세포를 세척하여 각각의 항원에 결합하지 않은 과량의 항체를 제거한다. 후속 단계에서는, 투과화된 세포를 적어도 제1 검출 항체 및 적어도 제2 검출 항체와 접촉시킨다. 상기 항체들은 혼합물로서, 즉, 동시에 또는 순차적으로 적용할 수 있다. 제1 검출 항체는 제1 포획 항체에 특이적으로 결합한다. 그렇게 하여, 제1 검출 복합체가 형성된다. 제1 검출 항체는 제1 포획 항체의 유래가 되는 종에 대하여 유도될 수 있다. 예를 들어, 만약 토끼 다클론성 항-SNAP 25 항체 S9684 (Sigma)를 비-절단 기질 SNAP-25와 BoNT/A 절단 기질 SNAP-25에 특이적으로 결합하는 제1 포획 항체로 사용한다면, 항-토끼 알칼리성 포스파타제 접합 항체를 제1 검출 항체로 사용할 수 있다. 제2 검출 항체는 제2 포획 항체에 특이적으로 결합한다. 그렇게 하여, 제2 검출 복합체가 형성된다. 제2 검출 항체는 제2 포획 항체의 유래가 되는 종에 대하여 유도될 수 있다. 예를 들어, 만약 국제특허 공개 WO 2014/207109호에 기술된 마우스 단클론성 항체 (mAb) 20-2-5를 BoNT/A 절단 SNAP-25에 특이적으로 결합하는 제2 포획 항체로 사용한다면, 항-마우스 양고추냉이 퍼옥시다제 (HRP) 접합 항체를 제2 검출 항체로 사용할 수 있다. 본 발명의 방법에 사용되는 바와 같은 각각의 제1 포획 항체 및 제2 포획 항체의 특이적 검출을 가능하게 하기 위해 제1 검출 항체 및 제2 검출 항체는 상이한 효소와 접합된다는 것이 당업자에게 명백하다. 예를 들어, 본 명세서의 다른 곳에 기재된 바와 같은 HRP 기반 검출은 BoNT/A 절단 SNAP 25에 대해 사용하고, 알칼리성 포스파타제 기반 검출은 총 (BoNT/A 절단 및 비-절단) SNAP 25에 대해 사용할 수 있다. 그 후, 세포를 다시 세척한다. 후속 단계에서는, 형광생성 HRP 기질을 세포에 첨가한다. HRP 기질로서, 예를 들어 Amplex UltraRed (Invitrogen)를 사용할 수 있는데, 이는 540 nm에서 여기되고 600 nm에서 방출된다. HRP 기질과의 인큐베이션은 양고추냉이 퍼옥시다제에 의한 기질의 충분한 전환에 충분한 시간 동안 수행한다. HRP 기질과의 인큐베이션에 후속하여, 예를 들어 AP 기질인 DiFMUP (6,8-다이플루오로-4-메틸움벨리페릴 포스페이트; 여기 360 nm; 방출 450 nm)를 HRP 기질에 첨가하고, 세포를 상기 두 기질의 혼합물과 함께 인큐베이션한다. 상기 AP 기질과의 인큐베이션은 알칼리성 포스파타제에 의한 기질의 충분한 전환을 가능하게 하는 시간 동안 수행한다. 당업계에 공지된 바와 같이, 기질은, 검출 한계의 정의에 따라, 측정된 신호가 적어도 블랭크(blank)의 평균 값 + 평균의 3 표준 편차만큼 크도록 충분한 양으로 전환되어야 한다. 검출 한계는 문헌에 기술된 바와 같이 결정할 수 있다 (예를 들어, 문헌[Armbruster and Pry, Clinical Biochem. Rev. 2008, 29 (Supplement 1): S49-S52] 참조). 알칼리성 포스파타제의 최적 pH가 알칼리성 영역에 있기 때문에, 상응하는 기질 완충액은 강알칼리성이다. 알칼리성 포스파타제 기질이 HRP 기질에 첨가되는 경우, 양고추냉이 퍼옥시다제의 반응은 알칼리성 pH에 의해 중지되고, 알칼리성 포스파타제는 DiFMUP를 전환시킨다. 전환된 HRP 기질은 알칼리성 pH에 의해 영향을 받지 않는다. 최종적으로, 두 기질의 형광을 하기와 같이 측정한다:
당업자에 의해 인식되는 바와 같이, 이러한 형광생성 기질들만이 본 발명의 방법에서 제1 포획 항체와 제2 포획 항체의 검출에 적절한데, 이들은 사용된 기질들의 상이한 여기/방출 파장을 나타낸다. 이 경우에만, 이들은 각 항원, 즉, 총 신경독소 기질 (예컨대, 비-절단 SNAP 25 및 신경독소 절단 SNAP 25) 및 절단된 신경독소 기질 (예컨대, 신경독소 절단 SNAP 25)의 특이적 검출을 가능하게 한다. 그렇게 하여, 모든 웰 또는 세포 배양 접시에서 동시에 신경독소 기질의 총 함량 및 절단된 신경독소 기질의 함량을 정량화할 수 있다. 이에 비추어, 유리하게는 본 발명의 방법을 자동화할 수 있다. 본 명세서의 다른 곳에 제시된 바와 같이, 본 발명의 방법을 위해 선택된 형광생성 기질은 여기/방출 스펙트럼 사이에 충분한 이동(shift)을 나타내어서 각각의 기질의 특이적 검출을 가능하게 한다는 것이 고찰된다. 이 요건은, 예를 들어, HRP 기질인 Amplex 및 그의 유도체에 대하여 그리고 AP 기질인 DiFMUP에 대하여 충족된다. 최적의 경우에, 사용된 형광생성 기질의 여기/방출 스펙트럼 사이에는 중첩이 없지만, 사용된 형광생성 기질의 여기 스펙트럼의 피크 영역에서 최대 30%의 중첩이 허용가능하다는 것을 경험하였다. 본 발명의 이 방법에 관한 추가의 세부 사항은, 예를 들어, 국제특허 공개 WO 2014/207109호에 기술되어 있다.
당업자에 의해 추가로 인식되는 바와 같이, 본 발명의 방법은 세포에서 신경독소 폴리펩티드에 의해 절단된 신경독소 기질의 직접적인 검출 및 정량화를 가능하게 하여, 상기 세포에서 상기 신경독소 폴리펩티드의 생물학적 활성을 결정한다. 유리하게는, 본 발명의 방법은, 당업계에 공지된 방법에 필요한, 세포 용해물 또는 추출물의 준비 및 세포 용해물/추출물로부터의 절단된 신경독소 기질의 단리 또는 농축을 필요로 하지 않는다. 이의 결과로서, 샘플 재료를 절약할 수 있다. 또한, 본 발명의 방법에 의해 샘플 준비 및 샘플 개수를 줄일 수 있는데, 이는 샘플 중의 총 신경독소 기질의 양 및 절단된 신경독소 기질의 양을 동시에 결정할 수 있기 때문이다. 당업계에 기술된 검정에서는, 둘 모두의 항원, 즉, 총 신경독소 기질 및 절단된 신경독소 기질을 서로 개별적으로 검출하기 위해 샘플을 세분화해야 한다. 본 발명의 방법은 샘플의 세분화를 불필요하게 한다. 그렇게 하여, 샘플의 세분화로 인한 비균일성을 회피할 수 있고, 샘플 재료를 절약할 수 있다. 또한, 당업계에 기술된 검정에서는 항원이 분해될 수 있는데, 이는 절단된 신경독소 기질의 검출을 왜곡시킬 수 있다. 이는, 당업계에 기술된 검정에서는 세포를 표면활성제 함유 용해 완충액과 함께 인큐베이션하지만, 이러한 완충액은 신경독소 폴리펩티드 또는 다른 내인성 프로테아제를 비활성화시킬 수 없어서 샘플의 더 오랜 보관 시에 신경독소 기질의 분해를 초래할 수 있기 때문이다. 상기 검정에서 세포 용해물의 사용이 요구됨으로 인해 종래 기술에 기술된 ECL 샌드위치 ELISA에서는 더 강한 용해 완충액을 사용할 수 없다. 이는 상기 언급된 항원의 응집이 세포 배양 접시 또는 미세역가 플레이트의 플라스틱 표면에 대한 항원의 비특이적 흡착을 초래할 수 있고, 이는 이어서 적절한 항체에 의한 항원의 검출을 방해하기 때문이다. 항원 검출을 위한 항체가 용해물과 역시 접촉하게 되므로, 항체도 응집될 수 있다. 이 경우, 항원의 신뢰성 있고 정확한 검출은 더 이상 가능하지 않다. 본 발명자들은 당업계에 기술된 신경독소의 생물학적 활성의 검출을 위한 웨스턴 블롯 검정을 사용함으로써 그러한 분해 반응을 경험하였다. 20℃에서 용해물의 더 오랜 보관 시, 신선한 용해물 샘플과 비교하여, 총 SNAP-25의 검출 신호는 강하게 감소된 것으로 나타났고, 절단된 신경독소 기질 SNAP 25 대 비-절단 신경독소 기질 SNAP 25의 비는 동결 동안 분해 과정으로 인해 이동하였다. 세포를 세포 배양 접시에 직접 고정시킴으로써 신경독소 기질의 분해 및/또는 샘플의 불안정성을 회피할 수 있다는 것이 본 발명자들에 의해 발견되었는데, 이는 신경독소 기질과 신경독소 또는 다른 내인성 프로테아제 둘 모두가 세포 배양 접시 상에서의 응집에 의해 즉시 비활성화되기 때문이다. 이는, 예를 들어, 메탄올 또는 당업계에 공지된 다른 고정액 또는 고정제, 예를 들어 에탄올, 아세톤, 포름알데하이드 또는 이들의 혼합물 또는 본 명세서에 기재된 다른 고정제에 의한 세포의 고정을 사용하여 달성할 수 있다. 이러한 고정 방법을 사용한, 예를 들어, 모(parental) SiMa 세포 (인간 신경모세포종 세포; DSMZ 번호: ACC 164) 및 iPS 유래 뉴런 (문헌[Whitemarsh et al. (2012), Toxicol. Sci. 126, 426-35])의 안정성 분석은 신선한 세포 배양 접시와 냉장고에서 7일 동안 보관된 세포 배양 접시 사이에 어떠한 차이도 보여주지 않았다.
본 발명의 방법에서 제1 포획 항체로서 사용될 수 있는, 비-절단 기질과 신경독소 절단 기질에 특이적으로 결합하는 적합한 항체는, 예를 들어, 토끼 다클론성 항-SNAP-25 항체인 S9684 (Sigma), 토끼 다클론성 항-SNAP25 항체인 PA5-19708 (Pierce Antibodies), 토끼 다클론성 항-SNAP25 항체인 PA5-19701 (Pierce Antibodies), 또는 토끼 단클론성 항-SNAP25 항체인 ab108990 (Abcam)을 포함한다.
본 발명의 방법에서 제2 포획 항체로서 이용될 수 있는, 신경독소 절단 기질의 절단 부위에 특이적으로 결합하는 적절한 항체는, 예를 들어, 마우스 단클론성 항체 클론 20-2-5 (국제특허 공개 WO 2014/207109호), 유럽 특허 제14199282.6호에 기술된 마우스 단클론성 항체, 마우스 단클론성 항체 MC-6053 (클론 4F3-2C1, R&D Systems), MAB4733 (Abnova), orb26633 (Biorbyt), 또는 GWB-T00279 (Genway)를 포함한다.
제1 검출 항체와 제2 검출 항체로서 사용될 수 있는 적합한 검출 항체는 당업계에 공지되어 있다. 예를 들어, 제1 검출 항체는 알칼리성 포스파타제 (AP) 접합 항체, 양고추냉이 퍼옥시다제 (HRP) 접합 항체 또는 형광 염료에 접합된 항체일 수 있다. 제2 검출 항체로서, 예를 들어 알칼리성 포스파타제 (AP) 접합 항체, 양고추냉이 퍼옥시다제 (HRP) 접합 항체, 글루코스 옥시다제 접합 항체, 티로시나제 접합 항체 또는 β-갈락토시다제 항체를 사용할 수 있다. 바람직하게는, 본 발명의 방법에 사용되는 경우 제1 검출 항체와 제2 검출 항체는 서로 상이하다.
본 명세서에 사용되는 바와 같이, 단수 형태는 문맥상 달리 명백히 지시되지 않는 한 단수 및 복수의 지시대상 둘 모두를 포함한다. 예로서, "세포"는 1개의 세포 또는 1개 초과의 세포를 지칭한다.
본 명세서에 사용되는 바와 같이, 용어 "약"은 명시된 항목, 숫자, 백분율 또는 용어의 값을 수식하는 경우 명시된 항목, 숫자, 백분율 또는 용어의 값의 ± 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, 1% 또는 0%의 범위를 지칭한다. ± 10%의 범위가 바람직하다.
본 명세서에 사용되는 바와 같이, 용어 "포함하는", "포함한다" 및 "구성되는"은 "함유하는" 또는 "함유한다"와 동의어이고, 포괄적이거나 제한을 두지 않은 것이며, 추가의 나열되지 않은 구성원, 요소 또는 방법 단계를 배제하지 않는다. 명백하게, 용어 "포함하는"은 용어 "로 이루어진"을 포함한다. 더 구체적으로는, 본 명세서에 사용되는 바와 같이, 용어 "포함하다"는 청구항이 모든 열거된 요소 또는 방법 단계를 포함하지만 추가의 언급되지 않은 요소 또는 방법 단계를 또한 포함할 수 있음을 의미한다. 예를 들어, 단계 a), 단계 b) 및 단계 c)를 포함하는 방법은 이의 가장 좁은 의미에서 단계 a), 단계 b) 및 단계 c)로 이루어진 방법을 포함한다. 문구 "로 이루어진"은 조성물 (또는 장치, 또는 방법)이 나열된 요소 (또는 단계)만을 가지며 그 이상은 가지지 않음을 의미한다. 대조적으로, 용어 "포함한다"는 단계 a), 단계 b) 및 단계 c) 이외에 추가의 단계, 예를 들어 단계 d) 및 단계 e)를 포함하는 방법도 포함할 수 있다.
만약 "1 내지 5 마이크로몰의 농도"와 같은 수치 범위가 본 명세서에 사용된다면, 그 범위는 1 마이크로몰 및 5 마이크로몰뿐만 아니라 1 마이크로몰과 5 마이크로몰 사이의 임의의 수치, 예를 들어 2 마이크로몰, 3 마이크로몰 및 4 마이크로몰도 포함한다.
본 명세서에 사용되는 바와 같이, 용어 "시험관내"는 동물 또는 인간 신체 외부 또는 이의 밖에 있음을 의미한다. 본 명세서에 사용되는 바와 같이, 용어 "시험관내"는 "생체외"를 포함하는 것으로 이해되어야 한다. 용어 "생체외"는 전형적으로 동물 또는 인간 신체로부터 분리되어 신체 외부에서, 예를 들어 배양 용기에서 유지 또는 증식되는 조직 또는 세포를 지칭한다. 본 명세서에 사용되는 바와 같이, 용어 "생체내"는 동물 또는 인간 신체의 내부 또는 이의 안에 있음을 의미한다.
본 발명의 방법의 추가의 태양에서, 세포의 K+ 매개 탈분극은 약 20 mM 내지 약 55 mM의 추가 K+ 농도에서 적어도 2시간 동안 수행한다.
통상, 당업계에서 사용되는 세포 배양 배지는 5 mM의 K+를 함유한다. 따라서, 본 발명의 방법에서 최종 K+ 농도는 바람직하게는 약 25 mM 내지 약 60 mM의 K+이다.
본 발명의 방법의 또 다른 추가의 태양에서, 세포의 K+ 매개 탈분극 및/또는 신경독소 폴리펩티드 제시는 GT1b의 존재 하에 수행한다.
본 발명의 방법의 다른 태양에서, GT1b는 15 내지 50 μM, 바람직하게는 20 μM의 농도로 사용한다.
본 발명의 방법의 추가의 태양에서, 감소된 신경독소 폴리펩티드 제시 시간은 적어도 24 시간 내지 96시간 미만 동안, 바람직하게는 적어도 48시간 내지 최대 72시간 동안 신경독소 폴리펩티드에 대한 세포의 제시이다.
본 발명의 방법의 추가의 태양에서, 신경독소 폴리펩티드 제시 동안 세포의 교반은 자석 교반기 또는 회전 스피너 플라스크 또는 세포의 진탕으로 달성한다. 세포의 교반은 적절한 세포 배양 배지 유속, 바람직하게는 약 25 cm/분 내지 약 300 cm/분, 더욱 바람직하게는 약 25 cm/분 내지 약 150 cm/분의 평균 배지 유속으로 수행한다.
본 발명의 방법의 추가의 태양에서, 세포의 K+ 매개 탈분극을 20 μM의 GT1b 및 신경독소 폴리펩티드의 존재 하에 적어도 약 20 mM 내지 약 55 mM의 추가 K+ 농도에서 적어도 2시간 동안 수행하고, 이어서 교반 하에서 추가 70시간 동안 신경독소 폴리펩티드 제시를 수행한다.
본 발명의 방법의 추가의 태양에서, 신경독소 폴리펩티드가 없는 상태의 인큐베이션 시간이 신경독소 폴리펩티드 제시보다 선행된다.
본 발명의 방법의 추가의 태양에서, 신경독소 폴리펩티드가 없는 상태의 인큐베이션 시간은 16시간 내지 48시간이다.
본 발명의 방법의 추가의 태양에서, 방법은 형광 방법이다.
본 발명의 방법의 추가의 태양에서, 신경독소 폴리펩티드는 본 명세서의 다른 곳에 정의된 바와 같은 BoNT/A, BoNT/B, BoNT/C1, BoNT/D, BoNT/E, BoNT/F, BoNT/G, BoNT/F, BoNT/G, BoNT/H 또는 TeNT, 또는 이의 서브타입이다.
본 발명의 방법의 추가의 태양에서, 기질은 VAMP/시냅토브레빈, SNAP-25 또는 신택신이다.
본 발명의 방법의 추가의 태양에서, 세포는 1차 신경 세포, 신경 세포로 분화할 수 있는 종양 세포, 예를 들어 신경모세포종 세포, P19 세포 또는 유도 만능성 줄기 세포 (IPS) 유래 뉴런으로 이루어진 군으로부터 선택된 신경 세포 또는 신경 분화 세포이다.
본 발명의 방법의 추가의 바람직한 실시 형태는 하기 실시예로부터 도출될 수 있다.
도면은 하기를 도시한다:
도 1: 스트레스 처리(stressed) 의약품 샘플의 활성 상실에서의 반응속도론. BoNT/A를 함유하는 의약품 샘플을 70℃에서 최대 4주 동안 보관하였다. 0주, 1주, 2주 및 4주 후에 샘플을 꺼내어 마우스 LD50 생물학적 검정뿐만 아니라 다양한 프로토콜을 사용하는 세포 기반 검정 (CBA)으로 분석하였다. x축 상에는 주 단위의 보관 시간이 주어져 있으며, y축 상에는 상대 효력이 주어져 있다. 시작 지점에서의 효력을 100%로 설정하고, 연속적인 시험 시점을 시작 지점을 기준으로 나타낸다. LD50 생물학적 검정에 대한 값은 마름모꼴로 나타나 있다. K+ 탈분극을 사용하는 세포 기반 검정 프로토콜은 사각형으로 나타나 있고, 8시간의 독소 인큐베이션 시간에 이어서 64시간의 무독소 상태의 인큐베이션 시간을 사용하는 프로토콜은 삼각형으로 나타나 있고, 72시간 인큐베이션 시간 동안 진탕을 사용하는 프로토콜은 원으로 나타나 있다. 변형되지 않은 CBA 프로토콜은 선 기호로 나타나 있다. 요컨대, 도 1은 스트레스 처리 샘플이 기준 검정인 마우스 LD50 생물학적 검정에 필적하는 감쇠 반응속도론을 나타내는 3가지의 세포 기반 검정례의 비교를 도시한다
본 발명을 이제 하기 실시예에 의해 예시할 것이지만, 이는 본 발명의 범주를 한정하는 것으로 해석되지 않아야 한다.
실시예:
실시예 1: 이중 형광 세포 기반 BoNT/A 활성 ELISA
세포의 고정
1. 배지/독소 용액을 제거한다. 100 μL/웰의 빙랭 메탄올 (-20℃)을 첨가하고, -20℃에서 20분 동안 인큐베이션한다.
주: 모든 후속 단계는 실온에서 수행한다.
세포 고정 후:
1. 메탄올 용액을 제거하고, 100 μL/웰의 PBS 완충액을 첨가한다. 더 오랜 보관 (1일 초과)을 위해서는, 300 μL/웰의 PBS 완충액을 첨가하고 플레이트를 파라필름(parafilm)으로 밀봉해야 한다. 플레이트는 냉장고에 보관해야 한다.
2. PBS 완충액을 제거하고, 세포를 200 μL/웰의 PBS 완충액으로 3회 세척한다. 각 단계는 부드럽게 진탕시키면서 1분 동안 수행해야 한다.
3. PBS 완충액을 제거하고, 100 μL/웰의 켄칭 완충액을 첨가하고, 부드럽게 진탕시키면서 20분 동안 인큐베이션한다.
4. 켄칭 완충액을 제거하고, 부드럽게 진탕시키면서 세포를 300 μL/웰의 PBS 완충액으로 3분 동안 1회 세척한다.
5. PBS 완충액을 제거하고, 200 μL/웰의 블로킹 완충액을 첨가하고, 부드럽게 진탕시키면서 1시간 동안 인큐베이션한다.
6. 블로킹 완충액을 제거하고, 100 μL의 1차 항체 혼합물 (블로킹 완충액 중의 항체 희석물)을 각 웰에 첨가한다. 부드럽게 진탕시키면서 밤새 (16 내지 18시간) 인큐베이션한다. 세포를 하기 2가지 1차 항체와 함께 동시에 인큐베이션한다: BoNT/A 절단 SNAP-25에 특이적인 마우스 항체 및 SNAP-25를 인식하는 다클론성 토끼 항체 (정규화를 위해 SNAP 25의 총량을 결정하기 위한 항체).
7. 1차 항체 혼합물을 분리시키고, 세포를 200 μL의 PBS 완충액으로 4회 세척한다. 각 단계는 부드럽게 진탕시키면서 3분 동안 수행해야 한다.
8. PBS 완충액을 제거하고, 100 μL의 2차 항체 혼합물, 즉, HRP 접합 항-마우스 및 AP 접합 항-토끼 2차 항체 (블로킹 완충액 중의 항체 희석물)를 각 웰에 첨가하고, 부드럽게 진탕시키면서 2.5 내지 3시간 동안 인큐베이션한다.
9. 2차 항체 혼합물을 분리시키고, 세포를 200 μL/웰의 PBS 완충액으로 5회 세척한 다음, 300 μL/웰의 HEPES 완충액으로 1회 세척 단계를 수행한다. 각 세척 단계는 부드럽게 진탕시키면서 3분 동안 수행해야 한다.
10. 플레이트로부터 HEPES 완충액을 제거하고, 양고추냉이 퍼옥시다제에 대한 형광생성 기질 (HRP 기질) 75 μL를 각 웰에 첨가한다. 부드럽게 진탕시키면서 50분 동안 인큐베이션한다. 플레이트를 직사광으로부터 보호한다.
11. 알칼리성 포스파타제에 대한 형광생성 기질 (AP 기질) 75 μL를 각 웰에 첨가하고, 부드럽게 진탕시키면서 추가 50분 동안 인큐베이션한다. 플레이트를 직사광으로부터 보호한다.
12. 형광 플레이트 판독기를 사용하여 플레이트를 판독한다:
540 nm에서 여기; 600 nm에서 방출.
360 nm에서 여기; 450 nm에서 방출.
13. 계산
정규화를 위해, 절단된 SNAP-25에 대한 RFU 값 (600 nm에서의 형광)을 각 웰에서 총 SNAP-25의 RFU (450 nm)에 대해 정규화한다. 도표에서 더 나은 RFU의 표현을 위해, 하기 방정식을 사용하여 모든 값에 계수 1000을 곱한다:
후속하여, 각 표준물 또는 샘플에 대해 생성된 RFU 값의 평균을 구한다.
시약 준비
PBS 완충액 (10 mM):
인산염 완충 식염수 (Sigma, # P5368) (pH 7.4)
켄칭 완충액:
10 mM PBS 완충액 (pH 7.4) 중의 0.6% H2O2
블로킹 완충액:
0.05% Triton X-100 + 10 mM PBS 완충액 (pH 7.4) 중의 2% BSA
HEPES 완충액:
50 mM HEPES (pH 7.4)
HRP 기질:
50 mM HEPES (pH 7.4)
0.007% H2O2
150 pM Amplex UltraRed
AP 기질:
25 mM 다이에탄올아민 (pH 9.8)
2 mM MgCl2
100 μL M DiFMUP
실시예 2: 세포 내로의 클로스트리디움 신경독소 폴리펩티드의 특이적 흡수의 향상
a) CDI (Cellular Dynamics International) 사용자 매뉴얼에 따라, iCell® 뉴런을 해동시키고 4가지 상이한 세포 배치(batch)로부터의 96 웰 플레이트 상에 플레이팅하였다. 플레이팅한 지 24시간(h) 후, 배지를 사용자 매뉴얼에 기재된 바와 같이 신선한 유지 배지로 교체하였다.
추가 72시간의 인큐베이션 시간 후, 배지를 제거하고, 다양한 농도의 BoNT/A 및 총 30 mM의 농도의 K+ 이온 (즉, 그대로의 배지와 비교하여 25 mM의 추가 K+)을 함유하는 신선한 배지로 교체하였다. 2시간 후, 고(high) K+ 배지를 제거하고, 다양한 농도의 BoNT/A를 함유하는 신선한 배지를 세포에 첨가하였다.
추가 70시간 후, 배지를 흡인시키고, 세포를 고정시키고, 실시예 1에 기재된 바와 같이 ELISA 판독을 수행하였다. 이 프로토콜의 결과는 도 1에 사각형으로 나타나 있다.
b) CDI 사용자 매뉴얼에 따라, iCell® 뉴런을 해동시키고 4가지 상이한 세포 배치로부터의 96 웰 플레이트 상에 플레이팅하였다. 플레이팅한 지 24시간(h) 후, 배지를 사용자 매뉴얼에 기재된 바와 같이 신선한 유지 배지로 교체하였다.
추가 72시간의 인큐베이션 시간 후, 배지를 제거하고, 다양한 농도의 BoNT/A를 함유하는 신선한 배지로 교체하였다. 8시간 후, BoNT/A 함유 배지를 제거하고, BoNT/A가 없는 신선한 배지를 세포에 첨가하였다.
추가 64시간 후, 배지를 흡인시키고, 세포를 고정시키고, 실시예 1에 기재된 바와 같이 ELISA 판독을 수행하였다. 이 프로토콜의 결과는 도 1에 삼각형으로 나타나 있다.
c) CDI 사용자 매뉴얼에 따라, iCell® 뉴런을 해동시키고 4가지 상이한 세포 배치로부터의 96 웰 플레이트 상에 플레이팅하였다. 플레이팅한 지 24시간(h) 후, 배지를 사용자 매뉴얼에 기재된 바와 같이 신선한 유지 배지로 교체하였다.
추가 72시간의 인큐베이션 시간 후, 배지를 제거하고, 다양한 농도의 BoNT/A를 함유하는 신선한 배지로 교체하였다. 세포를 인큐베이터의 플레이트 진탕기에 놓고, 독소 제시 시간 동안 300 cm/분의 평균 유속으로 진탕시켰다.
추가 72시간 후, 배지를 흡인시키고, 세포를 고정시키고, 실시예 1에 기재된 바와 같이 ELISA 판독을 수행하였다. 이 프로토콜의 결과는 도 1에 원으로 나타나 있다.
d) CDI 사용자 매뉴얼에 따라, iCell® 뉴런을 해동시키고 4가지 상이한 세포 배치로부터의 96 웰 플레이트 상에 플레이팅하였다. 플레이팅한 지 24시간(h) 후, 배지를 사용자 매뉴얼에 기재된 바와 같이 신선한 유지 배지로 교체하였다.
추가 72시간의 인큐베이션 시간 후, 배지를 제거하고, 다양한 농도의 BoNT/A를 함유하는 신선한 배지로 교체하였다.
추가 72시간 후, 배지를 흡인시키고, 세포를 고정시키고, 실시예 1에 기재된 바와 같이 ELISA 판독을 수행하였다. 이 프로토콜의 결과는 도 1에 선으로 나타나 있다.
결론:
요약하면, 세포의 K+ 매개 탈분극, 감소된 신경독소 폴리펩티드 제시 시간 또는 신경독소 폴리펩티드 제시 동안 세포의 교반은 마우스 LD50 생물학적 검정과 비교할 때 실시예 1의 세포 기반 검정의 반응속도론을 나타내는 필적하는 안정성을 촉진시킨다.
SEQUENCE LISTING
<110> Merz Pharma GmbH & Co.KGaA
<120> Methods for Enhancing the specific Uptake of Botulinum Neurotoxins into Cells
<130> MP12983PC
<160> 16
<170> PatentIn version 3.5
<210> 1
<211> 3891
<212> DNA
<213> Clostridium botulinum
<400> 1
atgccatttg ttaataaaca atttaattat aaagatcctg taaatggtgt tgatattgct 60
tatataaaaa ttccaaatgc aggacaaatg caaccagtaa aagcttttaa aattcataat 120
aaaatatggg ttattccaga aagagataca tttacaaatc ctgaagaagg agatttaaat 180
ccaccaccag aagcaaaaca agttccagtt tcatattatg attcaacata tttaagtaca 240
gataatgaaa aagataatta tttaaaggga gttacaaaat tatttgagag aatttattca 300
actgatcttg gaagaatgtt gttaacatca atagtaaggg gaataccatt ttggggtgga 360
agtacaatag atacagaatt aaaagttatt gatactaatt gtattaatgt gatacaacca 420
gatggtagtt atagatcaga agaacttaat ctagtaataa taggaccctc agctgatatt 480
atacagtttg aatgtaaaag ctttggacat gaagttttga atcttacgcg aaatggttat 540
ggctctactc aatacattag atttagccca gattttacat ttggttttga ggagtcactt 600
gaagttgata caaatcctct tttaggtgca ggcaaatttg ctacagatcc agcagtaaca 660
ttagcacatg aacttataca tgctggacat agattatatg gaatagcaat taatccaaat 720
agggttttta aagtaaatac taatgcctat tatgaaatga gtgggttaga agtaagcttt 780
gaggaactta gaacatttgg gggacatgat gcaaagttta tagatagttt acaggaaaac 840
gaatttcgtc tatattatta taataagttt aaagatatag caagtacact taataaagct 900
aaatcaatag taggtactac tgcttcatta cagtatatga aaaatgtttt taaagagaaa 960
tatctcctat ctgaagatac atctggaaaa ttttcggtag ataaattaaa atttgataag 1020
ttatacaaaa tgttaacaga gatttacaca gaggataatt ttgttaagtt ttttaaagta 1080
cttaacagaa aaacatattt gaattttgat aaagccgtat ttaagataaa tatagtacct 1140
aaggtaaatt acacaatata tgatggattt aatttaagaa atacaaattt agcagcaaac 1200
tttaatggtc aaaatacaga aattaataat atgaatttta ctaaactaaa aaattttact 1260
ggattgtttg aattttataa gttgctatgt gtaagaggga taataacttc taaaactaaa 1320
tcattagata aaggatacaa taaggcatta aatgatttat gtatcaaagt taataattgg 1380
gacttgtttt ttagtccttc agaagataat tttactaatg atctaaataa aggagaagaa 1440
attacatctg atactaatat agaagcagca gaagaaaata ttagtttaga tttaatacaa 1500
caatattatt taacctttaa ttttgataat gaacctgaaa atatttcaat agaaaatctt 1560
tcaagtgaca ttataggcca attagaactt atgcctaata tagaaagatt tcctaatgga 1620
aaaaagtatg agttagataa atatactatg ttccattatc ttcgtgctca agaatttgaa 1680
catggtaaat ctaggattgc tttaacaaat tctgttaacg aagcattatt aaatcctagt 1740
cgtgtttata catttttttc ttcagactat gtaaagaaag ttaataaagc tacggaggca 1800
gctatgtttt taggctgggt agaacaatta gtatatgatt ttaccgatga aactagcgaa 1860
gtaagtacta cggataaaat tgcggatata actataatta ttccatatat aggacctgct 1920
ttaaatatag gtaatatgtt atataaagat gattttgtag gtgctttaat attttcagga 1980
gctgttattc tgttagaatt tataccagag attgcaatac ctgtattagg tacttttgca 2040
cttgtatcat atattgcgaa taaggttcta accgttcaaa caatagataa tgctttaagt 2100
aaaagaaatg aaaaatggga tgaggtctat aaatatatag taacaaattg gttagcaaag 2160
gttaatacac agattgatct aataagaaaa aaaatgaaag aagctttaga aaatcaagca 2220
gaagcaacaa aggctataat aaactatcag tataatcaat atactgagga agagaaaaat 2280
aatattaatt ttaatattga tgatttaagt tcgaaactta atgagtctat aaataaagct 2340
atgattaata taaataaatt tttgaatcaa tgctctgttt catatttaat gaattctatg 2400
atcccttatg gtgttaaacg gttagaagat tttgatgcta gtcttaaaga tgcattatta 2460
aagtatatat atgataatag aggaacttta attggtcaag tagatagatt aaaagataaa 2520
gttaataata cacttagtac agatatacct tttcagcttt ccaaatacgt agataatcaa 2580
agattattat ctacatttac tgaatatatt aagaatatta ttaatacttc tatattgaat 2640
ttaagatatg aaagtaatca tttaatagac ttatctaggt atgcatcaaa aataaatatt 2700
ggtagtaaag taaattttga tccaatagat aaaaatcaaa ttcaattatt taatttagaa 2760
agtagtaaaa ttgaggtaat tttaaaaaat gctattgtat ataatagtat gtatgaaaat 2820
tttagtacta gcttttggat aagaattcct aagtatttta acagtataag tctaaataat 2880
gaatatacaa taataaattg tatggaaaat aattcaggat ggaaagtatc acttaattat 2940
ggtgaaataa tctggacttt acaggatact caggaaataa aacaaagagt agtttttaaa 3000
tacagtcaaa tgattaatat atcagattat ataaacagat ggatttttgt aactatcact 3060
aataatagat taaataactc taaaatttat ataaatggaa gattaataga tcaaaaacca 3120
atttcaaatt taggtaatat tcatgctagt aataatataa tgtttaaatt agatggttgt 3180
agagatacac atagatatat ttggataaaa tattttaatc tttttgataa ggaattaaat 3240
gaaaaagaaa tcaaagattt atatgataat caatcaaatt caggtatttt aaaagacttt 3300
tggggtgatt atttacaata tgataaacca tactatatgt taaatttata tgatccaaat 3360
aaatatgtcg atgtaaataa tgtaggtatt agaggttata tgtatcttaa agggcctaga 3420
ggtagcgtaa tgactacaaa catttattta aattcaagtt tgtatagggg gacaaaattt 3480
attataaaaa aatatgcttc tggaaataaa gataatattg ttagaaataa tgatcgtgta 3540
tatattaatg tagtagttaa aaataaagaa tataggttag ctactaatgc atcacaggca 3600
ggcgtagaaa aaatactaag tgcattagaa atacctgatg taggaaatct aagtcaagta 3660
gtagtaatga agtcaaaaaa tgatcaagga ataacaaata aatgcaaaat gaatttacaa 3720
gataataatg ggaatgatat aggctttata ggatttcatc agtttaataa tatagctaaa 3780
ctagtagcaa gtaattggta taatagacaa atagaaagat ctagtaggac tttgggttgc 3840
tcatgggaat ttattcctgt agatgatgga tggggagaaa ggccactgta a 3891
<210> 2
<211> 1296
<212> PRT
<213> Clostridium botulinum
<400> 2
Met Pro Phe Val Asn Lys Gln Phe Asn Tyr Lys Asp Pro Val Asn Gly
1 5 10 15
Val Asp Ile Ala Tyr Ile Lys Ile Pro Asn Ala Gly Gln Met Gln Pro
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Val Lys Ala Phe Lys Ile His Asn Lys Ile Trp Val Ile Pro Glu Arg
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Asp Thr Phe Thr Asn Pro Glu Glu Gly Asp Leu Asn Pro Pro Pro Glu
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Ala Lys Gln Val Pro Val Ser Tyr Tyr Asp Ser Thr Tyr Leu Ser Thr
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Asp Asn Glu Lys Asp Asn Tyr Leu Lys Gly Val Thr Lys Leu Phe Glu
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Arg Ile Tyr Ser Thr Asp Leu Gly Arg Met Leu Leu Thr Ser Ile Val
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Arg Gly Ile Pro Phe Trp Gly Gly Ser Thr Ile Asp Thr Glu Leu Lys
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Val Ile Asp Thr Asn Cys Ile Asn Val Ile Gln Pro Asp Gly Ser Tyr
130 135 140
Arg Ser Glu Glu Leu Asn Leu Val Ile Ile Gly Pro Ser Ala Asp Ile
145 150 155 160
Ile Gln Phe Glu Cys Lys Ser Phe Gly His Glu Val Leu Asn Leu Thr
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Arg Asn Gly Tyr Gly Ser Thr Gln Tyr Ile Arg Phe Ser Pro Asp Phe
180 185 190
Thr Phe Gly Phe Glu Glu Ser Leu Glu Val Asp Thr Asn Pro Leu Leu
195 200 205
Gly Ala Gly Lys Phe Ala Thr Asp Pro Ala Val Thr Leu Ala His Glu
210 215 220
Leu Ile His Ala Gly His Arg Leu Tyr Gly Ile Ala Ile Asn Pro Asn
225 230 235 240
Arg Val Phe Lys Val Asn Thr Asn Ala Tyr Tyr Glu Met Ser Gly Leu
245 250 255
Glu Val Ser Phe Glu Glu Leu Arg Thr Phe Gly Gly His Asp Ala Lys
260 265 270
Phe Ile Asp Ser Leu Gln Glu Asn Glu Phe Arg Leu Tyr Tyr Tyr Asn
275 280 285
Lys Phe Lys Asp Ile Ala Ser Thr Leu Asn Lys Ala Lys Ser Ile Val
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Gly Thr Thr Ala Ser Leu Gln Tyr Met Lys Asn Val Phe Lys Glu Lys
305 310 315 320
Tyr Leu Leu Ser Glu Asp Thr Ser Gly Lys Phe Ser Val Asp Lys Leu
325 330 335
Lys Phe Asp Lys Leu Tyr Lys Met Leu Thr Glu Ile Tyr Thr Glu Asp
340 345 350
Asn Phe Val Lys Phe Phe Lys Val Leu Asn Arg Lys Thr Tyr Leu Asn
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Phe Asp Lys Ala Val Phe Lys Ile Asn Ile Val Pro Lys Val Asn Tyr
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Thr Ile Tyr Asp Gly Phe Asn Leu Arg Asn Thr Asn Leu Ala Ala Asn
385 390 395 400
Phe Asn Gly Gln Asn Thr Glu Ile Asn Asn Met Asn Phe Thr Lys Leu
405 410 415
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Ser Pro Ser Glu Asp Asn Phe Thr Asn Asp Leu Asn Lys Gly Glu Glu
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Ile Thr Ser Asp Thr Asn Ile Glu Ala Ala Glu Glu Asn Ile Ser Leu
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Asp Leu Ile Gln Gln Tyr Tyr Leu Thr Phe Asn Phe Asp Asn Glu Pro
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Lys Val Asn Lys Ala Thr Glu Ala Ala Met Phe Leu Gly Trp Val Glu
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Gln Leu Val Tyr Asp Phe Thr Asp Glu Thr Ser Glu Val Ser Thr Thr
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Asp Lys Ile Ala Asp Ile Thr Ile Ile Ile Pro Tyr Ile Gly Pro Ala
625 630 635 640
Leu Asn Ile Gly Asn Met Leu Tyr Lys Asp Asp Phe Val Gly Ala Leu
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Ile Phe Ser Gly Ala Val Ile Leu Leu Glu Phe Ile Pro Glu Ile Ala
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Ile Pro Val Leu Gly Thr Phe Ala Leu Val Ser Tyr Ile Ala Asn Lys
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Val Leu Thr Val Gln Thr Ile Asp Asn Ala Leu Ser Lys Arg Asn Glu
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Lys Trp Asp Glu Val Tyr Lys Tyr Ile Val Thr Asn Trp Leu Ala Lys
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Val Asn Thr Gln Ile Asp Leu Ile Arg Lys Lys Met Lys Glu Ala Leu
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Glu Asn Gln Ala Glu Ala Thr Lys Ala Ile Ile Asn Tyr Gln Tyr Asn
740 745 750
Gln Tyr Thr Glu Glu Glu Lys Asn Asn Ile Asn Phe Asn Ile Asp Asp
755 760 765
Leu Ser Ser Lys Leu Asn Glu Ser Ile Asn Lys Ala Met Ile Asn Ile
770 775 780
Asn Lys Phe Leu Asn Gln Cys Ser Val Ser Tyr Leu Met Asn Ser Met
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Ile Pro Tyr Gly Val Lys Arg Leu Glu Asp Phe Asp Ala Ser Leu Lys
805 810 815
Asp Ala Leu Leu Lys Tyr Ile Tyr Asp Asn Arg Gly Thr Leu Ile Gly
820 825 830
Gln Val Asp Arg Leu Lys Asp Lys Val Asn Asn Thr Leu Ser Thr Asp
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Ile Pro Phe Gln Leu Ser Lys Tyr Val Asp Asn Gln Arg Leu Leu Ser
850 855 860
Thr Phe Thr Glu Tyr Ile Lys Asn Ile Ile Asn Thr Ser Ile Leu Asn
865 870 875 880
Leu Arg Tyr Glu Ser Asn His Leu Ile Asp Leu Ser Arg Tyr Ala Ser
885 890 895
Lys Ile Asn Ile Gly Ser Lys Val Asn Phe Asp Pro Ile Asp Lys Asn
900 905 910
Gln Ile Gln Leu Phe Asn Leu Glu Ser Ser Lys Ile Glu Val Ile Leu
915 920 925
Lys Asn Ala Ile Val Tyr Asn Ser Met Tyr Glu Asn Phe Ser Thr Ser
930 935 940
Phe Trp Ile Arg Ile Pro Lys Tyr Phe Asn Ser Ile Ser Leu Asn Asn
945 950 955 960
Glu Tyr Thr Ile Ile Asn Cys Met Glu Asn Asn Ser Gly Trp Lys Val
965 970 975
Ser Leu Asn Tyr Gly Glu Ile Ile Trp Thr Leu Gln Asp Thr Gln Glu
980 985 990
Ile Lys Gln Arg Val Val Phe Lys Tyr Ser Gln Met Ile Asn Ile Ser
995 1000 1005
Asp Tyr Ile Asn Arg Trp Ile Phe Val Thr Ile Thr Asn Asn Arg
1010 1015 1020
Leu Asn Asn Ser Lys Ile Tyr Ile Asn Gly Arg Leu Ile Asp Gln
1025 1030 1035
Lys Pro Ile Ser Asn Leu Gly Asn Ile His Ala Ser Asn Asn Ile
1040 1045 1050
Met Phe Lys Leu Asp Gly Cys Arg Asp Thr His Arg Tyr Ile Trp
1055 1060 1065
Ile Lys Tyr Phe Asn Leu Phe Asp Lys Glu Leu Asn Glu Lys Glu
1070 1075 1080
Ile Lys Asp Leu Tyr Asp Asn Gln Ser Asn Ser Gly Ile Leu Lys
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Asp Phe Trp Gly Asp Tyr Leu Gln Tyr Asp Lys Pro Tyr Tyr Met
1100 1105 1110
Leu Asn Leu Tyr Asp Pro Asn Lys Tyr Val Asp Val Asn Asn Val
1115 1120 1125
Gly Ile Arg Gly Tyr Met Tyr Leu Lys Gly Pro Arg Gly Ser Val
1130 1135 1140
Met Thr Thr Asn Ile Tyr Leu Asn Ser Ser Leu Tyr Arg Gly Thr
1145 1150 1155
Lys Phe Ile Ile Lys Lys Tyr Ala Ser Gly Asn Lys Asp Asn Ile
1160 1165 1170
Val Arg Asn Asn Asp Arg Val Tyr Ile Asn Val Val Val Lys Asn
1175 1180 1185
Lys Glu Tyr Arg Leu Ala Thr Asn Ala Ser Gln Ala Gly Val Glu
1190 1195 1200
Lys Ile Leu Ser Ala Leu Glu Ile Pro Asp Val Gly Asn Leu Ser
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Gln Val Val Val Met Lys Ser Lys Asn Asp Gln Gly Ile Thr Asn
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Lys Cys Lys Met Asn Leu Gln Asp Asn Asn Gly Asn Asp Ile Gly
1235 1240 1245
Phe Ile Gly Phe His Gln Phe Asn Asn Ile Ala Lys Leu Val Ala
1250 1255 1260
Ser Asn Trp Tyr Asn Arg Gln Ile Glu Arg Ser Ser Arg Thr Leu
1265 1270 1275
Gly Cys Ser Trp Glu Phe Ile Pro Val Asp Asp Gly Trp Gly Glu
1280 1285 1290
Arg Pro Leu
1295
<210> 3
<211> 3876
<212> DNA
<213> Clostridium botulinum
<400> 3
atgccagtta caataaataa ttttaattat aatgatccta ttgataataa taatattatt 60
atgatggagc ctccatttgc gagaggtacg gggagatatt ataaagcttt taaaatcaca 120
gatcgtattt ggataatacc ggaaagatat acttttggat ataaacctga ggattttaat 180
aaaagttccg gtatttttaa tagagatgtt tgtgaatatt atgatccaga ttacttaaat 240
actaatgata aaaagaatat atttttacaa acaatgatca agttatttaa tagaatcaaa 300
tcaaaaccat tgggtgaaaa gttattagag atgattataa atggtatacc ttatcttgga 360
gatagacgtg ttccactcga agagtttaac acaaacattg ctagtgtaac tgttaataaa 420
ttaatcagta atccaggaga agtggagcga aaaaaaggta ttttcgcaaa tttaataata 480
tttggacctg ggccagtttt aaatgaaaat gagactatag atataggtat acaaaatcat 540
tttgcatcaa gggaaggctt cgggggtata atgcaaatga agttttgccc agaatatgta 600
agcgtattta ataatgttca agaaaacaaa ggcgcaagta tatttaatag acgtggatat 660
ttttcagatc cagccttgat attaatgcat gaacttatac atgttttaca tggattatat 720
ggcattaaag tagatgattt accaattgta ccaaatgaaa aaaaattttt tatgcaatct 780
acagatgcta tacaggcaga agaactatat acatttggag gacaagatcc cagcatcata 840
actccttcta cggataaaag tatctatgat aaagttttgc aaaattttag agggatagtt 900
gatagactta acaaggtttt agtttgcata tcagatccta acattaatat taatatatat 960
aaaaataaat ttaaagataa atataaattc gttgaagatt ctgagggaaa atatagtata 1020
gatgtagaaa gttttgataa attatataaa agcttaatgt ttggttttac agaaactaat 1080
atagcagaaa attataaaat aaaaactaga gcttcttatt ttagtgattc cttaccacca 1140
gtaaaaataa aaaatttatt agataatgaa atctatacta tagaggaagg gtttaatata 1200
tctgataaag atatggaaaa agaatataga ggtcagaata aagctataaa taaacaagct 1260
tatgaagaaa ttagcaagga gcatttggct gtatataaga tacaaatgtg taaaagtgtt 1320
aaagctccag gaatatgtat tgatgttgat aatgaagatt tgttctttat agctgataaa 1380
aatagttttt cagatgattt atctaaaaac gaaagaatag aatataatac acagagtaat 1440
tatatagaaa atgacttccc tataaatgaa ttaattttag atactgattt aataagtaaa 1500
atagaattac caagtgaaaa tacagaatca cttactgatt ttaatgtaga tgttccagta 1560
tatgaaaaac aacccgctat aaaaaaaatt tttacagatg aaaataccat ctttcaatat 1620
ttatactctc agacatttcc tctagatata agagatataa gtttaacatc ttcatttgat 1680
gatgcattat tattttctaa caaagtttat tcattttttt ctatggatta tattaaaact 1740
gctaataaag tggtagaagc aggattattt gcaggttggg tgaaacagat agtaaatgat 1800
tttgtaatcg aagctaataa aagcaatact atggataaaa ttgcagatat atctctaatt 1860
gttccttata taggattagc tttaaatgta ggaaatgaaa cagctaaagg aaattttgaa 1920
aatgcttttg agattgcagg agccagtatt ctactagaat ttataccaga acttttaata 1980
cctgtagttg gagccttttt attagaatca tatattgaca ataaaaataa aattattaaa 2040
acaatagata atgctttaac taaaagaaat gaaaaatgga gtgatatgta cggattaata 2100
gtagcgcaat ggctctcaac agttaatact caattttata caataaaaga gggaatgtat 2160
aaggctttaa attatcaagc acaagcattg gaagaaataa taaaatacag atataatata 2220
tattctgaaa aagaaaagtc aaatattaac atcgatttta atgatataaa ttctaaactt 2280
aatgagggta ttaaccaagc tatagataat ataaataatt ttataaatgg atgttctgta 2340
tcatatttaa tgaaaaaaat gattccatta gctgtagaaa aattactaga ctttgataat 2400
actctcaaaa aaaatttgtt aaattatata gatgaaaata aattatattt gattggaagt 2460
gcagaatatg aaaaatcaaa agtaaataaa tacttgaaaa ccattatgcc gtttgatctt 2520
tcaatatata ccaatgatac aatactaata gaaatgttta ataaatataa tagcgaaatt 2580
ttaaataata ttatcttaaa tttaagatat aaggataata atttaataga tttatcagga 2640
tatggggcaa aggtagaggt atatgatgga gtcgagctta atgataaaaa tcaatttaaa 2700
ttaactagtt cagcaaatag taagattaga gtgactcaaa atcagaatat catatttaat 2760
agtgtgttcc ttgattttag cgttagcttt tggataagaa tacctaaata taagaatgat 2820
ggtatacaaa attatattca taatgaatat acaataatta attgtatgaa aaataattcg 2880
ggctggaaaa tatctattag gggtaatagg ataatatgga ctttaattga tataaatgga 2940
aaaaccaaat cggtattttt tgaatataac ataagagaag atatatcaga gtatataaat 3000
agatggtttt ttgtaactat tactaataat ttgaataacg ctaaaattta tattaatggt 3060
aagctagaat caaatacaga tattaaagat ataagagaag ttattgctaa tggtgaaata 3120
atatttaaat tagatggtga tatagataga acacaattta tttggatgaa atatttcagt 3180
atttttaata cggaattaag tcaatcaaat attgaagaaa gatataaaat tcaatcatat 3240
agcgaatatt taaaagattt ttggggaaat cctttaatgt acaataaaga atattatatg 3300
tttaatgcgg ggaataaaaa ttcatatatt aaactaaaga aagattcacc tgtaggtgaa 3360
attttaacac gtagcaaata taatcaaaat tctaaatata taaattatag agatttatat 3420
attggagaaa aatttattat aagaagaaag tcaaattctc aatctataaa tgatgatata 3480
gttagaaaag aagattatat atatctagat ttttttaatt taaatcaaga gtggagagta 3540
tatacctata aatattttaa gaaagaggaa gaaaaattgt ttttagctcc tataagtgat 3600
tctgatgagt tttacaatac tatacaaata aaagaatatg atgaacagcc aacatatagt 3660
tgtcagttgc tttttaaaaa agatgaagaa agtactgatg agataggatt gattggtatt 3720
catcgtttct acgaatctgg aattgtattt gaagagtata aagattattt ttgtataagt 3780
aaatggtact taaaagaggt aaaaaggaaa ccatataatt taaaattggg atgtaattgg 3840
cagtttattc ctaaagatga agggtggact gaataa 3876
<210> 4
<211> 1291
<212> PRT
<213> Clostridium botulinum
<400> 4
Met Pro Val Thr Ile Asn Asn Phe Asn Tyr Asn Asp Pro Ile Asp Asn
1 5 10 15
Asn Asn Ile Ile Met Met Glu Pro Pro Phe Ala Arg Gly Thr Gly Arg
20 25 30
Tyr Tyr Lys Ala Phe Lys Ile Thr Asp Arg Ile Trp Ile Ile Pro Glu
35 40 45
Arg Tyr Thr Phe Gly Tyr Lys Pro Glu Asp Phe Asn Lys Ser Ser Gly
50 55 60
Ile Phe Asn Arg Asp Val Cys Glu Tyr Tyr Asp Pro Asp Tyr Leu Asn
65 70 75 80
Thr Asn Asp Lys Lys Asn Ile Phe Leu Gln Thr Met Ile Lys Leu Phe
85 90 95
Asn Arg Ile Lys Ser Lys Pro Leu Gly Glu Lys Leu Leu Glu Met Ile
100 105 110
Ile Asn Gly Ile Pro Tyr Leu Gly Asp Arg Arg Val Pro Leu Glu Glu
115 120 125
Phe Asn Thr Asn Ile Ala Ser Val Thr Val Asn Lys Leu Ile Ser Asn
130 135 140
Pro Gly Glu Val Glu Arg Lys Lys Gly Ile Phe Ala Asn Leu Ile Ile
145 150 155 160
Phe Gly Pro Gly Pro Val Leu Asn Glu Asn Glu Thr Ile Asp Ile Gly
165 170 175
Ile Gln Asn His Phe Ala Ser Arg Glu Gly Phe Gly Gly Ile Met Gln
180 185 190
Met Lys Phe Cys Pro Glu Tyr Val Ser Val Phe Asn Asn Val Gln Glu
195 200 205
Asn Lys Gly Ala Ser Ile Phe Asn Arg Arg Gly Tyr Phe Ser Asp Pro
210 215 220
Ala Leu Ile Leu Met His Glu Leu Ile His Val Leu His Gly Leu Tyr
225 230 235 240
Gly Ile Lys Val Asp Asp Leu Pro Ile Val Pro Asn Glu Lys Lys Phe
245 250 255
Phe Met Gln Ser Thr Asp Ala Ile Gln Ala Glu Glu Leu Tyr Thr Phe
260 265 270
Gly Gly Gln Asp Pro Ser Ile Ile Thr Pro Ser Thr Asp Lys Ser Ile
275 280 285
Tyr Asp Lys Val Leu Gln Asn Phe Arg Gly Ile Val Asp Arg Leu Asn
290 295 300
Lys Val Leu Val Cys Ile Ser Asp Pro Asn Ile Asn Ile Asn Ile Tyr
305 310 315 320
Lys Asn Lys Phe Lys Asp Lys Tyr Lys Phe Val Glu Asp Ser Glu Gly
325 330 335
Lys Tyr Ser Ile Asp Val Glu Ser Phe Asp Lys Leu Tyr Lys Ser Leu
340 345 350
Met Phe Gly Phe Thr Glu Thr Asn Ile Ala Glu Asn Tyr Lys Ile Lys
355 360 365
Thr Arg Ala Ser Tyr Phe Ser Asp Ser Leu Pro Pro Val Lys Ile Lys
370 375 380
Asn Leu Leu Asp Asn Glu Ile Tyr Thr Ile Glu Glu Gly Phe Asn Ile
385 390 395 400
Ser Asp Lys Asp Met Glu Lys Glu Tyr Arg Gly Gln Asn Lys Ala Ile
405 410 415
Asn Lys Gln Ala Tyr Glu Glu Ile Ser Lys Glu His Leu Ala Val Tyr
420 425 430
Lys Ile Gln Met Cys Lys Ser Val Lys Ala Pro Gly Ile Cys Ile Asp
435 440 445
Val Asp Asn Glu Asp Leu Phe Phe Ile Ala Asp Lys Asn Ser Phe Ser
450 455 460
Asp Asp Leu Ser Lys Asn Glu Arg Ile Glu Tyr Asn Thr Gln Ser Asn
465 470 475 480
Tyr Ile Glu Asn Asp Phe Pro Ile Asn Glu Leu Ile Leu Asp Thr Asp
485 490 495
Leu Ile Ser Lys Ile Glu Leu Pro Ser Glu Asn Thr Glu Ser Leu Thr
500 505 510
Asp Phe Asn Val Asp Val Pro Val Tyr Glu Lys Gln Pro Ala Ile Lys
515 520 525
Lys Ile Phe Thr Asp Glu Asn Thr Ile Phe Gln Tyr Leu Tyr Ser Gln
530 535 540
Thr Phe Pro Leu Asp Ile Arg Asp Ile Ser Leu Thr Ser Ser Phe Asp
545 550 555 560
Asp Ala Leu Leu Phe Ser Asn Lys Val Tyr Ser Phe Phe Ser Met Asp
565 570 575
Tyr Ile Lys Thr Ala Asn Lys Val Val Glu Ala Gly Leu Phe Ala Gly
580 585 590
Trp Val Lys Gln Ile Val Asn Asp Phe Val Ile Glu Ala Asn Lys Ser
595 600 605
Asn Thr Met Asp Lys Ile Ala Asp Ile Ser Leu Ile Val Pro Tyr Ile
610 615 620
Gly Leu Ala Leu Asn Val Gly Asn Glu Thr Ala Lys Gly Asn Phe Glu
625 630 635 640
Asn Ala Phe Glu Ile Ala Gly Ala Ser Ile Leu Leu Glu Phe Ile Pro
645 650 655
Glu Leu Leu Ile Pro Val Val Gly Ala Phe Leu Leu Glu Ser Tyr Ile
660 665 670
Asp Asn Lys Asn Lys Ile Ile Lys Thr Ile Asp Asn Ala Leu Thr Lys
675 680 685
Arg Asn Glu Lys Trp Ser Asp Met Tyr Gly Leu Ile Val Ala Gln Trp
690 695 700
Leu Ser Thr Val Asn Thr Gln Phe Tyr Thr Ile Lys Glu Gly Met Tyr
705 710 715 720
Lys Ala Leu Asn Tyr Gln Ala Gln Ala Leu Glu Glu Ile Ile Lys Tyr
725 730 735
Arg Tyr Asn Ile Tyr Ser Glu Lys Glu Lys Ser Asn Ile Asn Ile Asp
740 745 750
Phe Asn Asp Ile Asn Ser Lys Leu Asn Glu Gly Ile Asn Gln Ala Ile
755 760 765
Asp Asn Ile Asn Asn Phe Ile Asn Gly Cys Ser Val Ser Tyr Leu Met
770 775 780
Lys Lys Met Ile Pro Leu Ala Val Glu Lys Leu Leu Asp Phe Asp Asn
785 790 795 800
Thr Leu Lys Lys Asn Leu Leu Asn Tyr Ile Asp Glu Asn Lys Leu Tyr
805 810 815
Leu Ile Gly Ser Ala Glu Tyr Glu Lys Ser Lys Val Asn Lys Tyr Leu
820 825 830
Lys Thr Ile Met Pro Phe Asp Leu Ser Ile Tyr Thr Asn Asp Thr Ile
835 840 845
Leu Ile Glu Met Phe Asn Lys Tyr Asn Ser Glu Ile Leu Asn Asn Ile
850 855 860
Ile Leu Asn Leu Arg Tyr Lys Asp Asn Asn Leu Ile Asp Leu Ser Gly
865 870 875 880
Tyr Gly Ala Lys Val Glu Val Tyr Asp Gly Val Glu Leu Asn Asp Lys
885 890 895
Asn Gln Phe Lys Leu Thr Ser Ser Ala Asn Ser Lys Ile Arg Val Thr
900 905 910
Gln Asn Gln Asn Ile Ile Phe Asn Ser Val Phe Leu Asp Phe Ser Val
915 920 925
Ser Phe Trp Ile Arg Ile Pro Lys Tyr Lys Asn Asp Gly Ile Gln Asn
930 935 940
Tyr Ile His Asn Glu Tyr Thr Ile Ile Asn Cys Met Lys Asn Asn Ser
945 950 955 960
Gly Trp Lys Ile Ser Ile Arg Gly Asn Arg Ile Ile Trp Thr Leu Ile
965 970 975
Asp Ile Asn Gly Lys Thr Lys Ser Val Phe Phe Glu Tyr Asn Ile Arg
980 985 990
Glu Asp Ile Ser Glu Tyr Ile Asn Arg Trp Phe Phe Val Thr Ile Thr
995 1000 1005
Asn Asn Leu Asn Asn Ala Lys Ile Tyr Ile Asn Gly Lys Leu Glu
1010 1015 1020
Ser Asn Thr Asp Ile Lys Asp Ile Arg Glu Val Ile Ala Asn Gly
1025 1030 1035
Glu Ile Ile Phe Lys Leu Asp Gly Asp Ile Asp Arg Thr Gln Phe
1040 1045 1050
Ile Trp Met Lys Tyr Phe Ser Ile Phe Asn Thr Glu Leu Ser Gln
1055 1060 1065
Ser Asn Ile Glu Glu Arg Tyr Lys Ile Gln Ser Tyr Ser Glu Tyr
1070 1075 1080
Leu Lys Asp Phe Trp Gly Asn Pro Leu Met Tyr Asn Lys Glu Tyr
1085 1090 1095
Tyr Met Phe Asn Ala Gly Asn Lys Asn Ser Tyr Ile Lys Leu Lys
1100 1105 1110
Lys Asp Ser Pro Val Gly Glu Ile Leu Thr Arg Ser Lys Tyr Asn
1115 1120 1125
Gln Asn Ser Lys Tyr Ile Asn Tyr Arg Asp Leu Tyr Ile Gly Glu
1130 1135 1140
Lys Phe Ile Ile Arg Arg Lys Ser Asn Ser Gln Ser Ile Asn Asp
1145 1150 1155
Asp Ile Val Arg Lys Glu Asp Tyr Ile Tyr Leu Asp Phe Phe Asn
1160 1165 1170
Leu Asn Gln Glu Trp Arg Val Tyr Thr Tyr Lys Tyr Phe Lys Lys
1175 1180 1185
Glu Glu Glu Lys Leu Phe Leu Ala Pro Ile Ser Asp Ser Asp Glu
1190 1195 1200
Phe Tyr Asn Thr Ile Gln Ile Lys Glu Tyr Asp Glu Gln Pro Thr
1205 1210 1215
Tyr Ser Cys Gln Leu Leu Phe Lys Lys Asp Glu Glu Ser Thr Asp
1220 1225 1230
Glu Ile Gly Leu Ile Gly Ile His Arg Phe Tyr Glu Ser Gly Ile
1235 1240 1245
Val Phe Glu Glu Tyr Lys Asp Tyr Phe Cys Ile Ser Lys Trp Tyr
1250 1255 1260
Leu Lys Glu Val Lys Arg Lys Pro Tyr Asn Leu Lys Leu Gly Cys
1265 1270 1275
Asn Trp Gln Phe Ile Pro Lys Asp Glu Gly Trp Thr Glu
1280 1285 1290
<210> 5
<211> 3843
<212> DNA
<213> Clostridium botulinum
<400> 5
atgccaataa caattaacaa ctttaattat tcagatcctg ttgataataa aaatatttta 60
tatttagata ctcatttaaa tacattagct aatgagcctg aaaaagcctt tcgcattata 120
gggaatatat gggtaatacc cgatagattt tcaagagatt ctaatccaaa tttaaataaa 180
cctcctcgag ttacaagccc taaaagtggt tattatgatc ctaattattt gagtactgat 240
tctgaaaaag atacattttt aaaagaaatt ataaagttat ttaaaagaat taactctaga 300
gaaataggag aagaattaat atatagactt gcaacagaca taccctttcc tgggaataac 360
aatactccaa ttaatacttt tgattttgat gtagatttta acagtgttga tgttaaaact 420
agacaaggta acaactgggt taaaactggt agtataaatc ctagtgttat aataactgga 480
cctagagaaa acattataga cccagaaact tctacgttta aattaactaa caatactttt 540
gcggcacaag aaggatttgg tgctttatca ataatttcaa tatcacctag atttatgcta 600
acatatagta atgcaactaa taatgtagga gagggtagat tttctaagtc tgaattttgc 660
atggatccaa tactaatttt aatgcatgaa cttaatcatg caatgcataa tttatatgga 720
atagctatac caaatgatca aagaatttca tctgtaacta gtaatatttt ttattctcaa 780
tataaggtga aattagagta tgcagaaata tatgcatttg gaggtccaac tatagacctt 840
attcctaaaa gtgcaaggaa atattttgag gaaaaggcat tggattatta tagatccata 900
gctaaaagac ttaatagtat aactactgca aatccttcaa gctttaataa atatatagga 960
gaatataaac agaaacttat tagaaagtat agattcgtag tagaatcttc aggtgaagtt 1020
gcagtagatc gtaataagtt tgctgagtta tataaagaac ttacacaaat atttacagaa 1080
tttaactacg ctaaaatata taatgtacaa aataggaaaa tatatctttc aaatgtatat 1140
actccggtta cggcaaatat attagacgat aatgtttatg atatacaaaa tggatttaac 1200
atacctaaaa gtaatttaaa tgtactattt atgggtcaaa atttatctcg aaatccagca 1260
ttaagaaaag tcaatcctga aaatatgctt tatttattta caaaattttg ccataaagca 1320
atagatggta gatcattata taataaaaca ttagattgta gagagctttt agttaaaaat 1380
actgacttac cctttatagg tgatattagt gatatcaaaa ctgatatatt tttaagcaaa 1440
gatattaatg aagaaactga agttatagac tatccggaca atgtttcagt ggatcaagtt 1500
attctcagta agaatacctc agaacatgga caactagatt tattataccc tattattgaa 1560
ggtgagagtc aagtattacc gggagagaat caagtctttt atgataatag aactcaaaat 1620
gttgattatt tgaattctta ttattaccta gaatctcaaa aactaagtga taatgttgaa 1680
gattttactt ttacgacatc aattgaggaa gctttggata atagtggaaa agtatatact 1740
tactttccta aactagctga taaagtaaat acgggtgttc aaggtggttt atttttaatg 1800
tgggcaaatg atgtagttga agattttact acaaatattc taagaaaaga tacattagat 1860
aaaatatcag atgtatcagc tattattccc tatataggac ctgcattaaa tataagtaat 1920
tctgtaagaa ggggaaattt tactgaagca tttgcagtta ccggtgtaac tattttatta 1980
gaagcgtttc aagaatttac aatacctgca cttggtgcat ttgtgattta tagtaaggtt 2040
caagaaagaa acgagattat taaaactata gataattgtt tagaacaaag gattaaaaga 2100
tggaaagatt catatgaatg gatgatagga acgtggttat ccaggattac tactcaattt 2160
aataatataa gttatcaaat gtatgattct ttaaattatc aggcagatgc aatcaaagat 2220
aaaatagatt tagaatataa aaaatactca ggaagtgata aagaaaatat aaaaagtcaa 2280
gttgaaaatt taaaaaatag tttagatata aaaatctcgg aagcaatgaa taatataaat 2340
aaatttatac gagaatgttc tgtaacatac ttatttaaaa atatgctccc taaagtaatt 2400
gatgaattaa ataagtttga tttaaaaact aaaacagaat taattaatct tatagatagt 2460
cataatatta ttctagttgg tgaagtagat agattaaaag caaaagtaaa tgagagtttt 2520
gaaaatacaa taccctttaa tattttttca tatactaata attctttatt aaaagatata 2580
attaatgaat atttcaatag tattaatgat tcaaaaattt tgagcttaca aaacaaaaaa 2640
aatgctttag tggatacatc aggatataat gcagaagtga ggctagaagg tgatgttcaa 2700
gttaatacga tatatacaaa tgattttaaa ttaagtagtt caggagataa aattatagta 2760
aatttaaata ataatatttt atatagcgct atttatgaga actctagtgt tagtttttgg 2820
attaagatat ctaaagattt aactaattct cataatgaat atacaataat taatagtata 2880
aaacaaaatt ctgggtggaa attatgtatt aggaatggca atatagaatg gattttacaa 2940
gatattaata gaaagtataa aagtttaatt tttgattata gtgaatcatt aagtcataca 3000
ggatatacaa ataaatggtt ttttgttact ataactaata atataatggg gtatatgaaa 3060
ctttatataa atggagaatt aaagcagagt gaaagaattg aagatttaaa tgaggttaag 3120
ttagataaaa ccatagtatt tggaatagat gagaatatag atgagaatca gatgctttgg 3180
attagagatt ttaatatttt ttctaaagaa ttaagcaatg aagatattaa tattgtatat 3240
gagggacaaa tattaagaaa tgttattaaa gattattggg gaaatccttt gaagtttgat 3300
acagaatatt atattattaa tgataattat atagataggt atatagcacc taaaagtaat 3360
atacttgtac ttgttcagta tccagataga tctaaattat atactggaaa tcctattact 3420
attaaatcag tatctgataa gaatccttat agtagaattt taaatggaga taatataatg 3480
tttcatatgt tatataatag tgggaaatat atgataataa gagatactga tacaatatat 3540
gcaatagaag gaagagagtg ttcaaaaaat tgtgtatatg cattaaaatt acagagtaat 3600
ttaggtaatt atggtatagg tatatttagt ataaaaaata ttgtatctca aaataaatat 3660
tgtagtcaaa ttttctctag ttttatgaaa aatacaatgc ttctagcaga tatatataaa 3720
ccttggagat tttcttttga aaatgcatac acgccagttg cagtaactaa ttatgagaca 3780
aaactattat caacttcatc tttttggaaa tttatttcta gggatccagg atgggtagag 3840
taa 3843
<210> 6
<211> 1280
<212> PRT
<213> Clostridium botulinum
<400> 6
Met Pro Ile Thr Ile Asn Asn Phe Asn Tyr Ser Asp Pro Val Asp Asn
1 5 10 15
Lys Asn Ile Leu Tyr Leu Asp Thr His Leu Asn Thr Leu Ala Asn Glu
20 25 30
Pro Glu Lys Ala Phe Arg Ile Ile Gly Asn Ile Trp Val Ile Pro Asp
35 40 45
Arg Phe Ser Arg Asp Ser Asn Pro Asn Leu Asn Lys Pro Pro Arg Val
50 55 60
Thr Ser Pro Lys Ser Gly Tyr Tyr Asp Pro Asn Tyr Leu Ser Thr Asp
65 70 75 80
Ser Glu Lys Asp Thr Phe Leu Lys Glu Ile Ile Lys Leu Phe Lys Arg
85 90 95
Ile Asn Ser Arg Glu Ile Gly Glu Glu Leu Ile Tyr Arg Leu Ala Thr
100 105 110
Asp Ile Pro Phe Pro Gly Asn Asn Asn Thr Pro Ile Asn Thr Phe Asp
115 120 125
Phe Asp Val Asp Phe Asn Ser Val Asp Val Lys Thr Arg Gln Gly Asn
130 135 140
Asn Trp Val Lys Thr Gly Ser Ile Asn Pro Ser Val Ile Ile Thr Gly
145 150 155 160
Pro Arg Glu Asn Ile Ile Asp Pro Glu Thr Ser Thr Phe Lys Leu Thr
165 170 175
Asn Asn Thr Phe Ala Ala Gln Glu Gly Phe Gly Ala Leu Ser Ile Ile
180 185 190
Ser Ile Ser Pro Arg Phe Met Leu Thr Tyr Ser Asn Ala Thr Asn Asn
195 200 205
Val Gly Glu Gly Arg Phe Ser Lys Ser Glu Phe Cys Met Asp Pro Ile
210 215 220
Leu Ile Leu Met His Glu Leu Asn His Ala Met His Asn Leu Tyr Gly
225 230 235 240
Ile Ala Ile Pro Asn Asp Gln Arg Ile Ser Ser Val Thr Ser Asn Ile
245 250 255
Phe Tyr Ser Gln Tyr Lys Val Lys Leu Glu Tyr Ala Glu Ile Tyr Ala
260 265 270
Phe Gly Gly Pro Thr Ile Asp Leu Ile Pro Lys Ser Ala Arg Lys Tyr
275 280 285
Phe Glu Glu Lys Ala Leu Asp Tyr Tyr Arg Ser Ile Ala Lys Arg Leu
290 295 300
Asn Ser Ile Thr Thr Ala Asn Pro Ser Ser Phe Asn Lys Tyr Ile Gly
305 310 315 320
Glu Tyr Lys Gln Lys Leu Ile Arg Lys Tyr Arg Phe Val Val Glu Ser
325 330 335
Ser Gly Glu Val Ala Val Asp Arg Asn Lys Phe Ala Glu Leu Tyr Lys
340 345 350
Glu Leu Thr Gln Ile Phe Thr Glu Phe Asn Tyr Ala Lys Ile Tyr Asn
355 360 365
Val Gln Asn Arg Lys Ile Tyr Leu Ser Asn Val Tyr Thr Pro Val Thr
370 375 380
Ala Asn Ile Leu Asp Asp Asn Val Tyr Asp Ile Gln Asn Gly Phe Asn
385 390 395 400
Ile Pro Lys Ser Asn Leu Asn Val Leu Phe Met Gly Gln Asn Leu Ser
405 410 415
Arg Asn Pro Ala Leu Arg Lys Val Asn Pro Glu Asn Met Leu Tyr Leu
420 425 430
Phe Thr Lys Phe Cys His Lys Ala Ile Asp Gly Arg Ser Leu Tyr Asn
435 440 445
Lys Thr Leu Asp Cys Arg Glu Leu Leu Val Lys Asn Thr Asp Leu Pro
450 455 460
Phe Ile Gly Asp Ile Ser Asp Ile Lys Thr Asp Ile Phe Leu Ser Lys
465 470 475 480
Asp Ile Asn Glu Glu Thr Glu Val Ile Asp Tyr Pro Asp Asn Val Ser
485 490 495
Val Asp Gln Val Ile Leu Ser Lys Asn Thr Ser Glu His Gly Gln Leu
500 505 510
Asp Leu Leu Tyr Pro Ile Ile Glu Gly Glu Ser Gln Val Leu Pro Gly
515 520 525
Glu Asn Gln Val Phe Tyr Asp Asn Arg Thr Gln Asn Val Asp Tyr Leu
530 535 540
Asn Ser Tyr Tyr Tyr Leu Glu Ser Gln Lys Leu Ser Asp Asn Val Glu
545 550 555 560
Asp Phe Thr Phe Thr Thr Ser Ile Glu Glu Ala Leu Asp Asn Ser Gly
565 570 575
Lys Val Tyr Thr Tyr Phe Pro Lys Leu Ala Asp Lys Val Asn Thr Gly
580 585 590
Val Gln Gly Gly Leu Phe Leu Met Trp Ala Asn Asp Val Val Glu Asp
595 600 605
Phe Thr Thr Asn Ile Leu Arg Lys Asp Thr Leu Asp Lys Ile Ser Asp
610 615 620
Val Ser Ala Ile Ile Pro Tyr Ile Gly Pro Ala Leu Asn Ile Ser Asn
625 630 635 640
Ser Val Arg Arg Gly Asn Phe Thr Glu Ala Phe Ala Val Thr Gly Val
645 650 655
Thr Ile Leu Leu Glu Ala Phe Gln Glu Phe Thr Ile Pro Ala Leu Gly
660 665 670
Ala Phe Val Ile Tyr Ser Lys Val Gln Glu Arg Asn Glu Ile Ile Lys
675 680 685
Thr Ile Asp Asn Cys Leu Glu Gln Arg Ile Lys Arg Trp Lys Asp Ser
690 695 700
Tyr Glu Trp Met Ile Gly Thr Trp Leu Ser Arg Ile Thr Thr Gln Phe
705 710 715 720
Asn Asn Ile Ser Tyr Gln Met Tyr Asp Ser Leu Asn Tyr Gln Ala Asp
725 730 735
Ala Ile Lys Asp Lys Ile Asp Leu Glu Tyr Lys Lys Tyr Ser Gly Ser
740 745 750
Asp Lys Glu Asn Ile Lys Ser Gln Val Glu Asn Leu Lys Asn Ser Leu
755 760 765
Asp Ile Lys Ile Ser Glu Ala Met Asn Asn Ile Asn Lys Phe Ile Arg
770 775 780
Glu Cys Ser Val Thr Tyr Leu Phe Lys Asn Met Leu Pro Lys Val Ile
785 790 795 800
Asp Glu Leu Asn Lys Phe Asp Leu Lys Thr Lys Thr Glu Leu Ile Asn
805 810 815
Leu Ile Asp Ser His Asn Ile Ile Leu Val Gly Glu Val Asp Arg Leu
820 825 830
Lys Ala Lys Val Asn Glu Ser Phe Glu Asn Thr Ile Pro Phe Asn Ile
835 840 845
Phe Ser Tyr Thr Asn Asn Ser Leu Leu Lys Asp Ile Ile Asn Glu Tyr
850 855 860
Phe Asn Ser Ile Asn Asp Ser Lys Ile Leu Ser Leu Gln Asn Lys Lys
865 870 875 880
Asn Ala Leu Val Asp Thr Ser Gly Tyr Asn Ala Glu Val Arg Leu Glu
885 890 895
Gly Asp Val Gln Val Asn Thr Ile Tyr Thr Asn Asp Phe Lys Leu Ser
900 905 910
Ser Ser Gly Asp Lys Ile Ile Val Asn Leu Asn Asn Asn Ile Leu Tyr
915 920 925
Ser Ala Ile Tyr Glu Asn Ser Ser Val Ser Phe Trp Ile Lys Ile Ser
930 935 940
Lys Asp Leu Thr Asn Ser His Asn Glu Tyr Thr Ile Ile Asn Ser Ile
945 950 955 960
Lys Gln Asn Ser Gly Trp Lys Leu Cys Ile Arg Asn Gly Asn Ile Glu
965 970 975
Trp Ile Leu Gln Asp Ile Asn Arg Lys Tyr Lys Ser Leu Ile Phe Asp
980 985 990
Tyr Ser Glu Ser Leu Ser His Thr Gly Tyr Thr Asn Lys Trp Phe Phe
995 1000 1005
Val Thr Ile Thr Asn Asn Ile Met Gly Tyr Met Lys Leu Tyr Ile
1010 1015 1020
Asn Gly Glu Leu Lys Gln Ser Glu Arg Ile Glu Asp Leu Asn Glu
1025 1030 1035
Val Lys Leu Asp Lys Thr Ile Val Phe Gly Ile Asp Glu Asn Ile
1040 1045 1050
Asp Glu Asn Gln Met Leu Trp Ile Arg Asp Phe Asn Ile Phe Ser
1055 1060 1065
Lys Glu Leu Ser Asn Glu Asp Ile Asn Ile Val Tyr Glu Gly Gln
1070 1075 1080
Ile Leu Arg Asn Val Ile Lys Asp Tyr Trp Gly Asn Pro Leu Lys
1085 1090 1095
Phe Asp Thr Glu Tyr Tyr Ile Ile Asn Asp Asn Tyr Ile Asp Arg
1100 1105 1110
Tyr Ile Ala Pro Lys Ser Asn Ile Leu Val Leu Val Gln Tyr Pro
1115 1120 1125
Asp Arg Ser Lys Leu Tyr Thr Gly Asn Pro Ile Thr Ile Lys Ser
1130 1135 1140
Val Ser Asp Lys Asn Pro Tyr Ser Arg Ile Leu Asn Gly Asp Asn
1145 1150 1155
Ile Met Phe His Met Leu Tyr Asn Ser Gly Lys Tyr Met Ile Ile
1160 1165 1170
Arg Asp Thr Asp Thr Ile Tyr Ala Ile Glu Gly Arg Glu Cys Ser
1175 1180 1185
Lys Asn Cys Val Tyr Ala Leu Lys Leu Gln Ser Asn Leu Gly Asn
1190 1195 1200
Tyr Gly Ile Gly Ile Phe Ser Ile Lys Asn Ile Val Ser Gln Asn
1205 1210 1215
Lys Tyr Cys Ser Gln Ile Phe Ser Ser Phe Met Lys Asn Thr Met
1220 1225 1230
Leu Leu Ala Asp Ile Tyr Lys Pro Trp Arg Phe Ser Phe Glu Asn
1235 1240 1245
Ala Tyr Thr Pro Val Ala Val Thr Asn Tyr Glu Thr Lys Leu Leu
1250 1255 1260
Ser Thr Ser Ser Phe Trp Lys Phe Ile Ser Arg Asp Pro Gly Trp
1265 1270 1275
Val Glu
1280
<210> 7
<211> 3858
<212> DNA
<213> Clostridium botulinum
<400> 7
atgacatggc cagtaaaaga ttttaattat agtgatcctg ttaatgacaa tgatatatta 60
tatttaagaa taccacaaaa taagttaatt actacacctg taaaagcttt tatgattact 120
caaaatattt gggtaatacc agaaagattt tcatcagata ctaatccaag tttaagtaaa 180
ccgcctagac ctacttcaaa gtatcaaagt tattatgatc ctagttattt atctactgat 240
gagcaaaaag atacattttt aaaagggatt ataaaattat ttaaaagaat taatgaaaga 300
gatataggaa aaaaattaat aaattattta gtagttggtt caccttttat gggagattca 360
agtacgcctg aagatacatt tgattttaca cgtcatacta ctaatattgc agttgaaaag 420
tttgaaaatg gtagttggaa agtaacaaat attataacac caagtgtatt gatatttgga 480
ccacttccta atatattaga ctatacagca tcccttacat tgcaaggaca acaatcaaat 540
ccatcatttg aagggtttgg aacattatct atactaaaag tagcacctga atttttgtta 600
acatttagtg atgtaacatc taatcaaagt tcagctgtat taggcaaatc tatattttgt 660
atggatccag taatagcttt aatgcatgag ttaacacatt ctttgcatca attgtatgga 720
ataaatatac catctgataa aaggattcgt ccacaagtta gcgagggatt tttttctcaa 780
gatggaccca acgtacaatt tgaggaatta tacacatttg gaggatcaga tgttgaaata 840
atacctcaaa ttgaaagatt acaattaaga gaaaaagcat taggtcacta taaagatata 900
gcgaaaagac ttaataatat taataaaact attccttcta gttggagtag taatatagat 960
aaatataaaa aaatattttc tgaaaagtat aattttgata aagataatac aggaaatttt 1020
gttgtaaata ttgataaatt caatagctta tattcagact tgactaatgt tatgtcagaa 1080
gttgtttatt cttcgcaata taatgttaaa aacaggactc attatttttc aaagcattat 1140
ctacctgtat ttgcaaatat attagatgat aatatttata ctataataaa cggttttaat 1200
ttaacaacta aaggttttaa tatagaaaat tcgggtcaga atatagaaag gaatcctgca 1260
ctacaaaaac ttagttcaga aagtgtagta gatttgttta caaaagtatg tttaagatta 1320
acaagaaata gtagagatga ttcaacatgt attcaagtta aaaataatac attaccttat 1380
gtagctgata aagatagcat ttcacaagaa atatttgaaa gtcaaattat tacagatgag 1440
actaatgtag aaaattattc agataatttt tcattagatg aatctatttt agatgcaaaa 1500
gtccctacta atcctgaagc agtagatcca ctgttaccca atgttaatat ggaaccttta 1560
aatgttccag gtgaagaaga agtattttat gatgatatta ctaaagatgt tgattattta 1620
aactcttatt attatttgga agcccaaaaa ttaagtaata atgttgaaaa tattactctt 1680
acaacttcag ttgaagaagc attaggttat agcaataaga tatacacatt tttacctagc 1740
ttagctgaaa aagtgaataa aggtgttcaa gcaggtttat tcttaaattg ggcgaatgaa 1800
gtagttgagg attttactac aaatattatg aaaaaagata cattggataa aatatcagat 1860
gtatcagcca taattccata tataggacct gccttaaata taggaaattc agcattaagg 1920
ggaaacttta agcaagcatt tgcaacagct ggtgtagctt ttttgttaga aggatttcca 1980
gagtttacaa tacctgcact cggtgtattt accttttata gttctattca agaaagagag 2040
aaaattatta aaactataga aaattgttta gaacaaagag ttaagagatg gaaagattca 2100
tatcaatgga tggtatcaaa ttggttgtca agaattacta ctcgatttaa tcatataagt 2160
tatcaaatgt atgattcttt gagttatcag gcagatgcaa tcaaagctaa aatagattta 2220
gaatataaaa aatactcagg aagtgataaa gaaaatataa aaagtcaagt tgaaaattta 2280
aaaaatagtt tagatgtaaa aatctcggaa gcaatgaata atataaataa atttatacga 2340
gaatgttctg taacatactt atttaaaaat atgctcccta aagtaattga tgaattaaat 2400
aagtttgatt taaaaactaa aacagaatta attaatctta tagatagtca taatattatt 2460
ctagttggtg aagtagatag attaaaagca aaagtaaatg agagttttga aaatacaata 2520
ccctttaata ttttttcata tactaataat tctttattaa aagatatgat taatgaatat 2580
ttcaatagta ttaatgattc aaaaattttg agcttacaaa ataaaaaaaa tactttgatg 2640
gatacatcag gatataacgc agaagtgaga gtagaaggca atgttcagct taatccaata 2700
tttccatttg actttaaatt aggtagttca ggggatgata gaggtaaagt tatagtaacc 2760
cagaatgaaa atattgtata taatgctatg tatgaaagtt ttagtattag tttttggatt 2820
aggataaata aatgggtaag taatttacct ggatatacta taattgatag tgttaaaaat 2880
aactcaggtt ggagtatagg tattattagt aattttttag tgtttacttt aaaacaaaat 2940
gaaaatagtg aacaagatat aaactttagt tatgatatat caaagaatgc tgcgggatat 3000
aataaatggt tttttgtaac tattactacc aatatgatgg gaaatatgat gatttatata 3060
aatggaaaat taatagatac tataaaagtt aaagagttaa ctggaattaa ttttagcaaa 3120
actataacat ttcaaatgaa taaaattcca aatactggct taattacctc agattctgat 3180
aacatcaata tgtggataag ggatttttat atctttgcta aagaattaga tgataaagat 3240
attaatatat tatttaatag cttgcaatat actaatgttg taaaagatta ttggggaaat 3300
gatttaagat atgataaaga atattacatg attaacgtaa attatatgaa tagatatatg 3360
tctaaaaaag gcaatggaat tgtttttaat acacgtaaaa ataataatga cttcaatgaa 3420
ggatataaaa ttataataaa aagaattaga ggaaatacaa atgatactag agtacgagga 3480
gaaaatgtat tatattttaa tactacaatt gataacaaac aatatagttt aggtatgtat 3540
aaaccttcta gaaatctagg gactgattta gttccactag gtgcattgga tcaaccaatg 3600
gatgagatac gtaaatatgg ttcgtttata atacaaccat gcaatacttt tgattactat 3660
gcatcacaat tatttttgtc aagtaatgca acaacaaata ggcttggaat actatcaatt 3720
ggtagttata gtttcaaact tggagatgac tattggttta atcacgaata tttaattcct 3780
gttataaaaa tagagcatta tgcttcatta ttagaatcaa catcaactca ttgggttttt 3840
gtacctgcaa gtgaataa 3858
<210> 8
<211> 1285
<212> PRT
<213> Clostridium botulinum
<400> 8
Met Thr Trp Pro Val Lys Asp Phe Asn Tyr Ser Asp Pro Val Asn Asp
1 5 10 15
Asn Asp Ile Leu Tyr Leu Arg Ile Pro Gln Asn Lys Leu Ile Thr Thr
20 25 30
Pro Val Lys Ala Phe Met Ile Thr Gln Asn Ile Trp Val Ile Pro Glu
35 40 45
Arg Phe Ser Ser Asp Thr Asn Pro Ser Leu Ser Lys Pro Pro Arg Pro
50 55 60
Thr Ser Lys Tyr Gln Ser Tyr Tyr Asp Pro Ser Tyr Leu Ser Thr Asp
65 70 75 80
Glu Gln Lys Asp Thr Phe Leu Lys Gly Ile Ile Lys Leu Phe Lys Arg
85 90 95
Ile Asn Glu Arg Asp Ile Gly Lys Lys Leu Ile Asn Tyr Leu Val Val
100 105 110
Gly Ser Pro Phe Met Gly Asp Ser Ser Thr Pro Glu Asp Thr Phe Asp
115 120 125
Phe Thr Arg His Thr Thr Asn Ile Ala Val Glu Lys Phe Glu Asn Gly
130 135 140
Ser Trp Lys Val Thr Asn Ile Ile Thr Pro Ser Val Leu Ile Phe Gly
145 150 155 160
Pro Leu Pro Asn Ile Leu Asp Tyr Thr Ala Ser Leu Thr Leu Gln Gly
165 170 175
Gln Gln Ser Asn Pro Ser Phe Glu Gly Phe Gly Thr Leu Ser Ile Leu
180 185 190
Lys Val Ala Pro Glu Phe Leu Leu Thr Phe Ser Asp Val Thr Ser Asn
195 200 205
Gln Ser Ser Ala Val Leu Gly Lys Ser Ile Phe Cys Met Asp Pro Val
210 215 220
Ile Ala Leu Met His Glu Leu Thr His Ser Leu His Gln Leu Tyr Gly
225 230 235 240
Ile Asn Ile Pro Ser Asp Lys Arg Ile Arg Pro Gln Val Ser Glu Gly
245 250 255
Phe Phe Ser Gln Asp Gly Pro Asn Val Gln Phe Glu Glu Leu Tyr Thr
260 265 270
Phe Gly Gly Ser Asp Val Glu Ile Ile Pro Gln Ile Glu Arg Leu Gln
275 280 285
Leu Arg Glu Lys Ala Leu Gly His Tyr Lys Asp Ile Ala Lys Arg Leu
290 295 300
Asn Asn Ile Asn Lys Thr Ile Pro Ser Ser Trp Ser Ser Asn Ile Asp
305 310 315 320
Lys Tyr Lys Lys Ile Phe Ser Glu Lys Tyr Asn Phe Asp Lys Asp Asn
325 330 335
Thr Gly Asn Phe Val Val Asn Ile Asp Lys Phe Asn Ser Leu Tyr Ser
340 345 350
Asp Leu Thr Asn Val Met Ser Glu Val Val Tyr Ser Ser Gln Tyr Asn
355 360 365
Val Lys Asn Arg Thr His Tyr Phe Ser Lys His Tyr Leu Pro Val Phe
370 375 380
Ala Asn Ile Leu Asp Asp Asn Ile Tyr Thr Ile Ile Asn Gly Phe Asn
385 390 395 400
Leu Thr Thr Lys Gly Phe Asn Ile Glu Asn Ser Gly Gln Asn Ile Glu
405 410 415
Arg Asn Pro Ala Leu Gln Lys Leu Ser Ser Glu Ser Val Val Asp Leu
420 425 430
Phe Thr Lys Val Cys Leu Arg Leu Thr Arg Asn Ser Arg Asp Asp Ser
435 440 445
Thr Cys Ile Gln Val Lys Asn Asn Thr Leu Pro Tyr Val Ala Asp Lys
450 455 460
Asp Ser Ile Ser Gln Glu Ile Phe Glu Ser Gln Ile Ile Thr Asp Glu
465 470 475 480
Thr Asn Val Glu Asn Tyr Ser Asp Asn Phe Ser Leu Asp Glu Ser Ile
485 490 495
Leu Asp Ala Lys Val Pro Thr Asn Pro Glu Ala Val Asp Pro Leu Leu
500 505 510
Pro Asn Val Asn Met Glu Pro Leu Asn Val Pro Gly Glu Glu Glu Val
515 520 525
Phe Tyr Asp Asp Ile Thr Lys Asp Val Asp Tyr Leu Asn Ser Tyr Tyr
530 535 540
Tyr Leu Glu Ala Gln Lys Leu Ser Asn Asn Val Glu Asn Ile Thr Leu
545 550 555 560
Thr Thr Ser Val Glu Glu Ala Leu Gly Tyr Ser Asn Lys Ile Tyr Thr
565 570 575
Phe Leu Pro Ser Leu Ala Glu Lys Val Asn Lys Gly Val Gln Ala Gly
580 585 590
Leu Phe Leu Asn Trp Ala Asn Glu Val Val Glu Asp Phe Thr Thr Asn
595 600 605
Ile Met Lys Lys Asp Thr Leu Asp Lys Ile Ser Asp Val Ser Ala Ile
610 615 620
Ile Pro Tyr Ile Gly Pro Ala Leu Asn Ile Gly Asn Ser Ala Leu Arg
625 630 635 640
Gly Asn Phe Lys Gln Ala Phe Ala Thr Ala Gly Val Ala Phe Leu Leu
645 650 655
Glu Gly Phe Pro Glu Phe Thr Ile Pro Ala Leu Gly Val Phe Thr Phe
660 665 670
Tyr Ser Ser Ile Gln Glu Arg Glu Lys Ile Ile Lys Thr Ile Glu Asn
675 680 685
Cys Leu Glu Gln Arg Val Lys Arg Trp Lys Asp Ser Tyr Gln Trp Met
690 695 700
Val Ser Asn Trp Leu Ser Arg Ile Thr Thr Arg Phe Asn His Ile Ser
705 710 715 720
Tyr Gln Met Tyr Asp Ser Leu Ser Tyr Gln Ala Asp Ala Ile Lys Ala
725 730 735
Lys Ile Asp Leu Glu Tyr Lys Lys Tyr Ser Gly Ser Asp Lys Glu Asn
740 745 750
Ile Lys Ser Gln Val Glu Asn Leu Lys Asn Ser Leu Asp Val Lys Ile
755 760 765
Ser Glu Ala Met Asn Asn Ile Asn Lys Phe Ile Arg Glu Cys Ser Val
770 775 780
Thr Tyr Leu Phe Lys Asn Met Leu Pro Lys Val Ile Asp Glu Leu Asn
785 790 795 800
Lys Phe Asp Leu Lys Thr Lys Thr Glu Leu Ile Asn Leu Ile Asp Ser
805 810 815
His Asn Ile Ile Leu Val Gly Glu Val Asp Arg Leu Lys Ala Lys Val
820 825 830
Asn Glu Ser Phe Glu Asn Thr Ile Pro Phe Asn Ile Phe Ser Tyr Thr
835 840 845
Asn Asn Ser Leu Leu Lys Asp Met Ile Asn Glu Tyr Phe Asn Ser Ile
850 855 860
Asn Asp Ser Lys Ile Leu Ser Leu Gln Asn Lys Lys Asn Thr Leu Met
865 870 875 880
Asp Thr Ser Gly Tyr Asn Ala Glu Val Arg Val Glu Gly Asn Val Gln
885 890 895
Leu Asn Pro Ile Phe Pro Phe Asp Phe Lys Leu Gly Ser Ser Gly Asp
900 905 910
Asp Arg Gly Lys Val Ile Val Thr Gln Asn Glu Asn Ile Val Tyr Asn
915 920 925
Ala Met Tyr Glu Ser Phe Ser Ile Ser Phe Trp Ile Arg Ile Asn Lys
930 935 940
Trp Val Ser Asn Leu Pro Gly Tyr Thr Ile Ile Asp Ser Val Lys Asn
945 950 955 960
Asn Ser Gly Trp Ser Ile Gly Ile Ile Ser Asn Phe Leu Val Phe Thr
965 970 975
Leu Lys Gln Asn Glu Asn Ser Glu Gln Asp Ile Asn Phe Ser Tyr Asp
980 985 990
Ile Ser Lys Asn Ala Ala Gly Tyr Asn Lys Trp Phe Phe Val Thr Ile
995 1000 1005
Thr Thr Asn Met Met Gly Asn Met Met Ile Tyr Ile Asn Gly Lys
1010 1015 1020
Leu Ile Asp Thr Ile Lys Val Lys Glu Leu Thr Gly Ile Asn Phe
1025 1030 1035
Ser Lys Thr Ile Thr Phe Gln Met Asn Lys Ile Pro Asn Thr Gly
1040 1045 1050
Leu Ile Thr Ser Asp Ser Asp Asn Ile Asn Met Trp Ile Arg Asp
1055 1060 1065
Phe Tyr Ile Phe Ala Lys Glu Leu Asp Asp Lys Asp Ile Asn Ile
1070 1075 1080
Leu Phe Asn Ser Leu Gln Tyr Thr Asn Val Val Lys Asp Tyr Trp
1085 1090 1095
Gly Asn Asp Leu Arg Tyr Asp Lys Glu Tyr Tyr Met Ile Asn Val
1100 1105 1110
Asn Tyr Met Asn Arg Tyr Met Ser Lys Lys Gly Asn Gly Ile Val
1115 1120 1125
Phe Asn Thr Arg Lys Asn Asn Asn Asp Phe Asn Glu Gly Tyr Lys
1130 1135 1140
Ile Ile Ile Lys Arg Ile Arg Gly Asn Thr Asn Asp Thr Arg Val
1145 1150 1155
Arg Gly Glu Asn Val Leu Tyr Phe Asn Thr Thr Ile Asp Asn Lys
1160 1165 1170
Gln Tyr Ser Leu Gly Met Tyr Lys Pro Ser Arg Asn Leu Gly Thr
1175 1180 1185
Asp Leu Val Pro Leu Gly Ala Leu Asp Gln Pro Met Asp Glu Ile
1190 1195 1200
Arg Lys Tyr Gly Ser Phe Ile Ile Gln Pro Cys Asn Thr Phe Asp
1205 1210 1215
Tyr Tyr Ala Ser Gln Leu Phe Leu Ser Ser Asn Ala Thr Thr Asn
1220 1225 1230
Arg Leu Gly Ile Leu Ser Ile Gly Ser Tyr Ser Phe Lys Leu Gly
1235 1240 1245
Asp Asp Tyr Trp Phe Asn His Glu Tyr Leu Ile Pro Val Ile Lys
1250 1255 1260
Ile Glu His Tyr Ala Ser Leu Leu Glu Ser Thr Ser Thr His Trp
1265 1270 1275
Val Phe Val Pro Ala Ser Glu
1280 1285
<210> 9
<211> 3756
<212> DNA
<213> Clostridium botulinum
<400> 9
atgccaaaaa ttaatagttt taattataat gatcctgtta atgatagaac aattttatat 60
attaaaccag gcggttgtca agaattttat aaatcattta atattatgaa aaatatttgg 120
ataattccag agagaaatgt aattggtaca accccccaag attttcatcc gcctacttca 180
ttaaaaaatg gagatagtag ttattatgac cctaattatt tacaaagtga tgaagaaaag 240
gatagatttt taaaaatagt cacaaaaata tttaatagaa taaataataa tctttcagga 300
gggattttat tagaagaact gtcaaaagct aatccatatt tagggaatga taatactcca 360
gataatcaat tccatattgg tgatgcatca gcagttgaga ttaaattctc aaatggtagc 420
caagacatac tattacctaa tgttattata atgggagcag agcctgattt atttgaaact 480
aacagttcca atatttctct aagaaataat tatatgccaa gcaatcaccg ttttggatca 540
atagctatag taacattctc acctgaatat tcttttagat ttaatgataa ttgtatgaat 600
gaatttattc aagatcctgc tcttacatta atgcatgaat taatacattc attacatgga 660
ctatatgggg ctaaagggat tactacaaag tatactataa cacaaaaaca aaatccccta 720
ataacaaata taagaggtac aaatattgaa gaattcttaa cttttggagg tactgattta 780
aacattatta ctagtgctca gtccaatgat atctatacta atcttctagc tgattataaa 840
aaaatagcgt ctaaacttag caaagtacaa gtatctaatc cactacttaa tccttataaa 900
gatgtttttg aagcaaagta tggattagat aaagatgcta gcggaattta ttcggtaaat 960
ataaacaaat ttaatgatat ttttaaaaaa ttatacagct ttacggaatt tgatttacga 1020
actaaatttc aagttaaatg taggcaaact tatattggac agtataaata cttcaaactt 1080
tcaaacttgt taaatgattc tatttataat atatcagaag gctataatat aaataattta 1140
aaggtaaatt ttagaggaca gaatgcaaat ttaaatccta gaattattac accaattaca 1200
ggtagaggac tagtaaaaaa aatcattaga ttttgtaaaa atattgtttc tgtaaaaggc 1260
ataaggaaat caatatgtat cgaaataaat aatggtgagt tattttttgt ggcttccgag 1320
aatagttata atgatgataa tataaatact cctaaagaaa ttgacgatac agtaacttca 1380
aataataatt atgaaaatga tttagatcag gttattttaa attttaatag tgaatcagca 1440
cctggacttt cagatgaaaa attaaattta actatccaaa atgatgctta tataccaaaa 1500
tatgattcta atggaacaag tgatatagaa caacatgatg ttaatgaact taatgtattt 1560
ttctatttag atgcacagaa agtgcccgaa ggtgaaaata atgtcaatct cacctcttca 1620
attgatacag cattattaga acaacctaaa atatatacat ttttttcatc agaatttatt 1680
aataatgtca ataaacctgt gcaagcagca ttatttgtaa gctggataca acaagtgtta 1740
gtagatttta ctactgaagc taaccaaaaa agtactgttg ataaaattgc agatatttct 1800
atagttgttc catatatagg tcttgcttta aatataggaa atgaagcaca aaaaggaaat 1860
tttaaagatg cacttgaatt attaggagca ggtattttat tagaatttga acccgagctt 1920
ttaattccta caattttagt attcacgata aaatcttttt taggttcatc tgataataaa 1980
aataaagtta ttaaagcaat aaataatgca ttgaaagaaa gagatgaaaa atggaaagaa 2040
gtatatagtt ttatagtatc gaattggatg actaaaatta atacacaatt taataaaaga 2100
aaagaacaaa tgtatcaagc tttacaaaat caagtaaatg caattaaaac aataatagaa 2160
tctaagtata atagttatac tttagaggaa aaaaatgagc ttacaaataa atatgatatt 2220
aagcaaatag aaaatgaact taatcaaaag gtttctatag caatgaataa tatagacagg 2280
ttcttaactg aaagttctat atcctattta atgaaaataa taaatgaagt aaaaattaat 2340
aaattaagag aatatgatga gaatgtcaaa acgtatttat tgaattatat tatacaacat 2400
ggatcaatct tgggagagag tcagcaagaa ctaaattcta tggtaactga taccctaaat 2460
aatagtattc cttttaagct ttcttcttat acagatgata aaattttaat ttcatatttt 2520
aataaattct ttaagagaat taaaagtagt tcagttttaa atatgagata taaaaatgat 2580
aaatacgtag atacttcagg atatgattca aatataaata ttaatggaga tgtatataaa 2640
tatccaacta ataaaaatca atttggaata tataatgata aacttagtga agttaatata 2700
tctcaaaatg attacattat atatgataat aaatataaaa attttagtat tagtttttgg 2760
gtaagaattc ctaactatga taataagata gtaaatgtta ataatgaata cactataata 2820
aattgtatga gagataataa ttcaggatgg aaagtatctc ttaatcataa tgaaataatt 2880
tggacattcg aagataatcg aggaattaat caaaaattag catttaacta tggtaacgca 2940
aatggtattt ctgattatat aaataagtgg atttttgtaa ctataactaa tgatagatta 3000
ggagattcta aactttatat taatggaaat ttaatagatc aaaaatcaat tttaaattta 3060
ggtaatattc atgttagtga caatatatta tttaaaatag ttaattgtag ttatacaaga 3120
tatattggta ttagatattt taatattttt gataaagaat tagatgaaac agaaattcaa 3180
actttatata gcaatgaacc taatacaaat attttgaagg atttttgggg aaattatttg 3240
ctttatgaca aagaatacta tttattaaat gtgttaaaac caaataactt tattgatagg 3300
agaaaagatt ctactttaag cattaataat ataagaagca ctattctttt agctaataga 3360
ttatatagtg gaataaaagt taaaatacaa agagttaata atagtagtac taacgataat 3420
cttgttagaa agaatgatca ggtatatatt aattttgtag ccagcaaaac tcacttattt 3480
ccattatatg ctgatacagc taccacaaat aaagagaaaa caataaaaat atcatcatct 3540
ggcaatagat ttaatcaagt agtagttatg aattcagtag gaaattgtac aatgaatttt 3600
aaaaataata atggaaataa tattgggttg ttaggtttca aggcagatac tgtcgttgct 3660
agtacttggt attatacaca tatgagagat catacaaaca gcaatggatg tttttggaac 3720
tttatttctg aagaacatgg atggcaagaa aaataa 3756
<210> 10
<211> 1251
<212> PRT
<213> Clostridium botulinum
<400> 10
Met Pro Lys Ile Asn Ser Phe Asn Tyr Asn Asp Pro Val Asn Asp Arg
1 5 10 15
Thr Ile Leu Tyr Ile Lys Pro Gly Gly Cys Gln Glu Phe Tyr Lys Ser
20 25 30
Phe Asn Ile Met Lys Asn Ile Trp Ile Ile Pro Glu Arg Asn Val Ile
35 40 45
Gly Thr Thr Pro Gln Asp Phe His Pro Pro Thr Ser Leu Lys Asn Gly
50 55 60
Asp Ser Ser Tyr Tyr Asp Pro Asn Tyr Leu Gln Ser Asp Glu Glu Lys
65 70 75 80
Asp Arg Phe Leu Lys Ile Val Thr Lys Ile Phe Asn Arg Ile Asn Asn
85 90 95
Asn Leu Ser Gly Gly Ile Leu Leu Glu Glu Leu Ser Lys Ala Asn Pro
100 105 110
Tyr Leu Gly Asn Asp Asn Thr Pro Asp Asn Gln Phe His Ile Gly Asp
115 120 125
Ala Ser Ala Val Glu Ile Lys Phe Ser Asn Gly Ser Gln Asp Ile Leu
130 135 140
Leu Pro Asn Val Ile Ile Met Gly Ala Glu Pro Asp Leu Phe Glu Thr
145 150 155 160
Asn Ser Ser Asn Ile Ser Leu Arg Asn Asn Tyr Met Pro Ser Asn His
165 170 175
Arg Phe Gly Ser Ile Ala Ile Val Thr Phe Ser Pro Glu Tyr Ser Phe
180 185 190
Arg Phe Asn Asp Asn Cys Met Asn Glu Phe Ile Gln Asp Pro Ala Leu
195 200 205
Thr Leu Met His Glu Leu Ile His Ser Leu His Gly Leu Tyr Gly Ala
210 215 220
Lys Gly Ile Thr Thr Lys Tyr Thr Ile Thr Gln Lys Gln Asn Pro Leu
225 230 235 240
Ile Thr Asn Ile Arg Gly Thr Asn Ile Glu Glu Phe Leu Thr Phe Gly
245 250 255
Gly Thr Asp Leu Asn Ile Ile Thr Ser Ala Gln Ser Asn Asp Ile Tyr
260 265 270
Thr Asn Leu Leu Ala Asp Tyr Lys Lys Ile Ala Ser Lys Leu Ser Lys
275 280 285
Val Gln Val Ser Asn Pro Leu Leu Asn Pro Tyr Lys Asp Val Phe Glu
290 295 300
Ala Lys Tyr Gly Leu Asp Lys Asp Ala Ser Gly Ile Tyr Ser Val Asn
305 310 315 320
Ile Asn Lys Phe Asn Asp Ile Phe Lys Lys Leu Tyr Ser Phe Thr Glu
325 330 335
Phe Asp Leu Arg Thr Lys Phe Gln Val Lys Cys Arg Gln Thr Tyr Ile
340 345 350
Gly Gln Tyr Lys Tyr Phe Lys Leu Ser Asn Leu Leu Asn Asp Ser Ile
355 360 365
Tyr Asn Ile Ser Glu Gly Tyr Asn Ile Asn Asn Leu Lys Val Asn Phe
370 375 380
Arg Gly Gln Asn Ala Asn Leu Asn Pro Arg Ile Ile Thr Pro Ile Thr
385 390 395 400
Gly Arg Gly Leu Val Lys Lys Ile Ile Arg Phe Cys Lys Asn Ile Val
405 410 415
Ser Val Lys Gly Ile Arg Lys Ser Ile Cys Ile Glu Ile Asn Asn Gly
420 425 430
Glu Leu Phe Phe Val Ala Ser Glu Asn Ser Tyr Asn Asp Asp Asn Ile
435 440 445
Asn Thr Pro Lys Glu Ile Asp Asp Thr Val Thr Ser Asn Asn Asn Tyr
450 455 460
Glu Asn Asp Leu Asp Gln Val Ile Leu Asn Phe Asn Ser Glu Ser Ala
465 470 475 480
Pro Gly Leu Ser Asp Glu Lys Leu Asn Leu Thr Ile Gln Asn Asp Ala
485 490 495
Tyr Ile Pro Lys Tyr Asp Ser Asn Gly Thr Ser Asp Ile Glu Gln His
500 505 510
Asp Val Asn Glu Leu Asn Val Phe Phe Tyr Leu Asp Ala Gln Lys Val
515 520 525
Pro Glu Gly Glu Asn Asn Val Asn Leu Thr Ser Ser Ile Asp Thr Ala
530 535 540
Leu Leu Glu Gln Pro Lys Ile Tyr Thr Phe Phe Ser Ser Glu Phe Ile
545 550 555 560
Asn Asn Val Asn Lys Pro Val Gln Ala Ala Leu Phe Val Ser Trp Ile
565 570 575
Gln Gln Val Leu Val Asp Phe Thr Thr Glu Ala Asn Gln Lys Ser Thr
580 585 590
Val Asp Lys Ile Ala Asp Ile Ser Ile Val Val Pro Tyr Ile Gly Leu
595 600 605
Ala Leu Asn Ile Gly Asn Glu Ala Gln Lys Gly Asn Phe Lys Asp Ala
610 615 620
Leu Glu Leu Leu Gly Ala Gly Ile Leu Leu Glu Phe Glu Pro Glu Leu
625 630 635 640
Leu Ile Pro Thr Ile Leu Val Phe Thr Ile Lys Ser Phe Leu Gly Ser
645 650 655
Ser Asp Asn Lys Asn Lys Val Ile Lys Ala Ile Asn Asn Ala Leu Lys
660 665 670
Glu Arg Asp Glu Lys Trp Lys Glu Val Tyr Ser Phe Ile Val Ser Asn
675 680 685
Trp Met Thr Lys Ile Asn Thr Gln Phe Asn Lys Arg Lys Glu Gln Met
690 695 700
Tyr Gln Ala Leu Gln Asn Gln Val Asn Ala Ile Lys Thr Ile Ile Glu
705 710 715 720
Ser Lys Tyr Asn Ser Tyr Thr Leu Glu Glu Lys Asn Glu Leu Thr Asn
725 730 735
Lys Tyr Asp Ile Lys Gln Ile Glu Asn Glu Leu Asn Gln Lys Val Ser
740 745 750
Ile Ala Met Asn Asn Ile Asp Arg Phe Leu Thr Glu Ser Ser Ile Ser
755 760 765
Tyr Leu Met Lys Ile Ile Asn Glu Val Lys Ile Asn Lys Leu Arg Glu
770 775 780
Tyr Asp Glu Asn Val Lys Thr Tyr Leu Leu Asn Tyr Ile Ile Gln His
785 790 795 800
Gly Ser Ile Leu Gly Glu Ser Gln Gln Glu Leu Asn Ser Met Val Thr
805 810 815
Asp Thr Leu Asn Asn Ser Ile Pro Phe Lys Leu Ser Ser Tyr Thr Asp
820 825 830
Asp Lys Ile Leu Ile Ser Tyr Phe Asn Lys Phe Phe Lys Arg Ile Lys
835 840 845
Ser Ser Ser Val Leu Asn Met Arg Tyr Lys Asn Asp Lys Tyr Val Asp
850 855 860
Thr Ser Gly Tyr Asp Ser Asn Ile Asn Ile Asn Gly Asp Val Tyr Lys
865 870 875 880
Tyr Pro Thr Asn Lys Asn Gln Phe Gly Ile Tyr Asn Asp Lys Leu Ser
885 890 895
Glu Val Asn Ile Ser Gln Asn Asp Tyr Ile Ile Tyr Asp Asn Lys Tyr
900 905 910
Lys Asn Phe Ser Ile Ser Phe Trp Val Arg Ile Pro Asn Tyr Asp Asn
915 920 925
Lys Ile Val Asn Val Asn Asn Glu Tyr Thr Ile Ile Asn Cys Met Arg
930 935 940
Asp Asn Asn Ser Gly Trp Lys Val Ser Leu Asn His Asn Glu Ile Ile
945 950 955 960
Trp Thr Phe Glu Asp Asn Arg Gly Ile Asn Gln Lys Leu Ala Phe Asn
965 970 975
Tyr Gly Asn Ala Asn Gly Ile Ser Asp Tyr Ile Asn Lys Trp Ile Phe
980 985 990
Val Thr Ile Thr Asn Asp Arg Leu Gly Asp Ser Lys Leu Tyr Ile Asn
995 1000 1005
Gly Asn Leu Ile Asp Gln Lys Ser Ile Leu Asn Leu Gly Asn Ile
1010 1015 1020
His Val Ser Asp Asn Ile Leu Phe Lys Ile Val Asn Cys Ser Tyr
1025 1030 1035
Thr Arg Tyr Ile Gly Ile Arg Tyr Phe Asn Ile Phe Asp Lys Glu
1040 1045 1050
Leu Asp Glu Thr Glu Ile Gln Thr Leu Tyr Ser Asn Glu Pro Asn
1055 1060 1065
Thr Asn Ile Leu Lys Asp Phe Trp Gly Asn Tyr Leu Leu Tyr Asp
1070 1075 1080
Lys Glu Tyr Tyr Leu Leu Asn Val Leu Lys Pro Asn Asn Phe Ile
1085 1090 1095
Asp Arg Arg Lys Asp Ser Thr Leu Ser Ile Asn Asn Ile Arg Ser
1100 1105 1110
Thr Ile Leu Leu Ala Asn Arg Leu Tyr Ser Gly Ile Lys Val Lys
1115 1120 1125
Ile Gln Arg Val Asn Asn Ser Ser Thr Asn Asp Asn Leu Val Arg
1130 1135 1140
Lys Asn Asp Gln Val Tyr Ile Asn Phe Val Ala Ser Lys Thr His
1145 1150 1155
Leu Phe Pro Leu Tyr Ala Asp Thr Ala Thr Thr Asn Lys Glu Lys
1160 1165 1170
Thr Ile Lys Ile Ser Ser Ser Gly Asn Arg Phe Asn Gln Val Val
1175 1180 1185
Val Met Asn Ser Val Gly Asn Cys Thr Met Asn Phe Lys Asn Asn
1190 1195 1200
Asn Gly Asn Asn Ile Gly Leu Leu Gly Phe Lys Ala Asp Thr Val
1205 1210 1215
Val Ala Ser Thr Trp Tyr Tyr Thr His Met Arg Asp His Thr Asn
1220 1225 1230
Ser Asn Gly Cys Phe Trp Asn Phe Ile Ser Glu Glu His Gly Trp
1235 1240 1245
Gln Glu Lys
1250
<210> 11
<211> 3843
<212> DNA
<213> Clostridium botulinum
<400> 11
atgccagttg taataaatag ttttaattat aatgaccctg ttaatgatga gacaatttta 60
tacatgcaga aaccatatga agaaagaagt agaaaatatt ataaagcttt tgagattatg 120
cctaatgttt ggataatgcc tgagagagat acaataggaa ctaagcctga tgagtttcag 180
gtgccggatt cattaaagaa cggaagtagt gcttattatg atcctaatta tttaaccact 240
gatgctgaaa aagatagata tttaaaaaca atgataaaat tatttaatag aattaatagt 300
aatcctacag ggaaagtttt gttagaagaa gtatcaaatg ctagaccata tttaggagat 360
gatgacacgc taattaatga attccttcca gttaatgtaa ctacaagtgt taatataaaa 420
ttttcaactg atgttgaaag ttcaataata tcgaatcttc ttgtattggg agcaggacct 480
gatatattta aagcttactg tacccccctt gtaaggttta ataagtcaga taaattaatt 540
gaaccaagta atcatggttt tggatcaatt aatatcttga cattttcacc tgagtatgaa 600
catattttta atgatattag tggagggaat cataatagta cagaatcatt tattgcagat 660
cctgcaattt cactagctca tgaattgata catgcactac atggattata cggggctaag 720
gcagttactc ataaagagtc tctagtagca gagcgaggac ctcttatgat agccgaaaag 780
cccataaggc tagaagaatt tttaactttt ggaggtgagg atttaaatat cattcctagt 840
gctatgaagg aaaaaatata taacgatctt ttagctaact atgaaaaaat agctactaga 900
cttagagaag ttaatacggc tcctcctgga tatgatatta atgaatataa agattatttt 960
caatggaagt atggactaga tagaaatgca gatggaagtt atactgtgaa tagaaataaa 1020
tttaatgaaa tttataaaaa attatatagc tttacagaga ttgacttagc aaataaattt 1080
aaagtaaaat gtagaaatac ttattttatt aaatatggat ttgtaaaagt tccaaatttg 1140
ttagatgatg atatttatac tgtatcagag gggtttaata taggtaattt agcagtaaac 1200
aatcgcggac aaaatataaa tttaaatcct aaaattattg attccattcc agataaaggt 1260
ttagtggaaa agattattaa attttgtaag agcattattc ctagaaaagg tacgaagcag 1320
tcaccgtcac tatgcattag agtaaataat agggagttat tttttgtagc ttcagaaagt 1380
agctataatg aaagtgatat taatacacct aaagaaattg acgatacaac aaatctaaat 1440
aataattata gaaataattt agatgaagtt attttagatt ataatagtga gacaatacct 1500
caaatatcaa atcgaacatt aaatacactt gtacaagaca atagttatgt gccaagatat 1560
gattctaatg gaacaagtga aatagaggaa tatgatgttg ttgactttaa tgtatttttc 1620
tatttacatg cacaaaaagt accagaaggt gaaaccaata taagtttaac ttcttcaatt 1680
gatacagcat tattagaaga atccaaagta tatacatttt tttcttcaga gtttatcgat 1740
actatcaata aacctgtaaa tgcagcacta tttatagatt ggataagcaa agtaataaga 1800
gattttacca ctgaagctac acaaaaaagt actgttgata agattgcaga catatcttta 1860
attgtaccct atgtaggtct tgctttgaat atagttattg aggcagaaaa aggaaatttt 1920
gaggaggcat ttgaattatt aggagcgggt attttattag aatttgtgcc agagcttaca 1980
attcctgtaa ttttagtgtt tacgataaaa tcctatatag attcatatga gaataaaaat 2040
aaagcaatta aagcaataaa taattcatta atcgaaagag aagcaaagtg gaaagaaata 2100
tatagttgga tagtatcaaa ttggcttact agaattaata cgcaatttaa taaaagaaaa 2160
gagcaaatgt atcaggcttt acaaaatcaa gtagatgcaa taaaaacagc aatagaatat 2220
aaatataata attatacttc agatgagaaa aatagacttg aatctaaata taatatcaat 2280
aatatagaag aagaattgaa taaaaaagtt tctttagcaa tgaaaaatat agaaagattt 2340
atgacagaaa gttctatatc ttatttaatg aaattaataa atgaagccga agttggtaaa 2400
ttaaaagaat atgataaaca tgttaagagc gatttattag actatattct ctaccataaa 2460
ttaatcttag gagagcagac aaaggaatta attgatttgg tgactagtac tttgaatagt 2520
agtattccat ttgaactttc ttcatatact aatgataaaa ttctaattat atattttaat 2580
agattatata aaaaaattaa agatagttct attttagata tgcgatatga aaataataaa 2640
tttatagata tctctggata tggttcaaat ataagcatta atggaaacgt atatatttat 2700
tcaacaaata gaaatcaatt tggaatatat agtggtaggc ttagtgaagt taatatagct 2760
caaaataatg atattatata caatagtaga tatcaaaatt ttagtattag tttctgggta 2820
accattccta aacactacag acctatgaat cgtaatcggg aatacactat aataaattgt 2880
atggggaata ataattcggg atggaaaata tcacttagaa ctattagaga ttgtgaaata 2940
atttggactt tacaagatac ttccggaaat aaggaaaaat taatttttag gtatgaagaa 3000
cttgctagta tatctgatta tataaataaa tggatttttg taactattac taataataga 3060
ttaggcaatt ctagaattta catcaatgga aatttaatag ttgaaaaatc aatttcgaat 3120
ttaggtgata ttcatgttag tgataatata ttatttaaaa ttgttggttg tgatgatgaa 3180
acgtatgttg gtataagata ttttaaagtt tttaatacgg aattagataa aacagaaatt 3240
gagactttat atagtaatga gccagatcca agtatcttaa aagactattg gggaaattat 3300
ttgctatata ataaaaaata ttatttattc aatttactaa gaaaagataa gtatattact 3360
cggaattcag gcattttaaa tattaatcaa caaagaggtg ttactggagg catatctgtt 3420
tttttgaact ataaattata tgaaggagta gaagttatta taagaaaaaa tgctcctata 3480
gatatatcta atacagataa ttttgttaga aaaaacgatc tagcatacat taatgtagta 3540
gatcatggtg tagaatatcg gttatatgct gatatatcaa ttacaaaatc agagaaaata 3600
ataaaattaa taagaacatc taatccaaac gatagcttag gtcaaattat agttatggat 3660
tcaataggaa ataattgcac aatgaatttt caaaacaatg atgggagcaa tataggatta 3720
ctaggttttc attcagatga tttggttgct agtagttggt attataacca tatacgaaga 3780
aacactagca gtaatggatg cttttggagt tttatttcta aagagcatgg ttggaaagaa 3840
taa 3843
<210> 12
<211> 1280
<212> PRT
<213> Clostridium botulinum
<400> 12
Met Pro Val Val Ile Asn Ser Phe Asn Tyr Asn Asp Pro Val Asn Asp
1 5 10 15
Glu Thr Ile Leu Tyr Met Gln Lys Pro Tyr Glu Glu Arg Ser Arg Lys
20 25 30
Tyr Tyr Lys Ala Phe Glu Ile Met Pro Asn Val Trp Ile Met Pro Glu
35 40 45
Arg Asp Thr Ile Gly Thr Lys Pro Asp Glu Phe Gln Val Pro Asp Ser
50 55 60
Leu Lys Asn Gly Ser Ser Ala Tyr Tyr Asp Pro Asn Tyr Leu Thr Thr
65 70 75 80
Asp Ala Glu Lys Asp Arg Tyr Leu Lys Thr Met Ile Lys Leu Phe Asn
85 90 95
Arg Ile Asn Ser Asn Pro Thr Gly Lys Val Leu Leu Glu Glu Val Ser
100 105 110
Asn Ala Arg Pro Tyr Leu Gly Asp Asp Asp Thr Leu Ile Asn Glu Phe
115 120 125
Leu Pro Val Asn Val Thr Thr Ser Val Asn Ile Lys Phe Ser Thr Asp
130 135 140
Val Glu Ser Ser Ile Ile Ser Asn Leu Leu Val Leu Gly Ala Gly Pro
145 150 155 160
Asp Ile Phe Lys Ala Tyr Cys Thr Pro Leu Val Arg Phe Asn Lys Ser
165 170 175
Asp Lys Leu Ile Glu Pro Ser Asn His Gly Phe Gly Ser Ile Asn Ile
180 185 190
Leu Thr Phe Ser Pro Glu Tyr Glu His Ile Phe Asn Asp Ile Ser Gly
195 200 205
Gly Asn His Asn Ser Thr Glu Ser Phe Ile Ala Asp Pro Ala Ile Ser
210 215 220
Leu Ala His Glu Leu Ile His Ala Leu His Gly Leu Tyr Gly Ala Lys
225 230 235 240
Ala Val Thr His Lys Glu Ser Leu Val Ala Glu Arg Gly Pro Leu Met
245 250 255
Ile Ala Glu Lys Pro Ile Arg Leu Glu Glu Phe Leu Thr Phe Gly Gly
260 265 270
Glu Asp Leu Asn Ile Ile Pro Ser Ala Met Lys Glu Lys Ile Tyr Asn
275 280 285
Asp Leu Leu Ala Asn Tyr Glu Lys Ile Ala Thr Arg Leu Arg Glu Val
290 295 300
Asn Thr Ala Pro Pro Gly Tyr Asp Ile Asn Glu Tyr Lys Asp Tyr Phe
305 310 315 320
Gln Trp Lys Tyr Gly Leu Asp Arg Asn Ala Asp Gly Ser Tyr Thr Val
325 330 335
Asn Arg Asn Lys Phe Asn Glu Ile Tyr Lys Lys Leu Tyr Ser Phe Thr
340 345 350
Glu Ile Asp Leu Ala Asn Lys Phe Lys Val Lys Cys Arg Asn Thr Tyr
355 360 365
Phe Ile Lys Tyr Gly Phe Val Lys Val Pro Asn Leu Leu Asp Asp Asp
370 375 380
Ile Tyr Thr Val Ser Glu Gly Phe Asn Ile Gly Asn Leu Ala Val Asn
385 390 395 400
Asn Arg Gly Gln Asn Ile Asn Leu Asn Pro Lys Ile Ile Asp Ser Ile
405 410 415
Pro Asp Lys Gly Leu Val Glu Lys Ile Ile Lys Phe Cys Lys Ser Ile
420 425 430
Ile Pro Arg Lys Gly Thr Lys Gln Ser Pro Ser Leu Cys Ile Arg Val
435 440 445
Asn Asn Arg Glu Leu Phe Phe Val Ala Ser Glu Ser Ser Tyr Asn Glu
450 455 460
Ser Asp Ile Asn Thr Pro Lys Glu Ile Asp Asp Thr Thr Asn Leu Asn
465 470 475 480
Asn Asn Tyr Arg Asn Asn Leu Asp Glu Val Ile Leu Asp Tyr Asn Ser
485 490 495
Glu Thr Ile Pro Gln Ile Ser Asn Arg Thr Leu Asn Thr Leu Val Gln
500 505 510
Asp Asn Ser Tyr Val Pro Arg Tyr Asp Ser Asn Gly Thr Ser Glu Ile
515 520 525
Glu Glu Tyr Asp Val Val Asp Phe Asn Val Phe Phe Tyr Leu His Ala
530 535 540
Gln Lys Val Pro Glu Gly Glu Thr Asn Ile Ser Leu Thr Ser Ser Ile
545 550 555 560
Asp Thr Ala Leu Leu Glu Glu Ser Lys Val Tyr Thr Phe Phe Ser Ser
565 570 575
Glu Phe Ile Asp Thr Ile Asn Lys Pro Val Asn Ala Ala Leu Phe Ile
580 585 590
Asp Trp Ile Ser Lys Val Ile Arg Asp Phe Thr Thr Glu Ala Thr Gln
595 600 605
Lys Ser Thr Val Asp Lys Ile Ala Asp Ile Ser Leu Ile Val Pro Tyr
610 615 620
Val Gly Leu Ala Leu Asn Ile Val Ile Glu Ala Glu Lys Gly Asn Phe
625 630 635 640
Glu Glu Ala Phe Glu Leu Leu Gly Ala Gly Ile Leu Leu Glu Phe Val
645 650 655
Pro Glu Leu Thr Ile Pro Val Ile Leu Val Phe Thr Ile Lys Ser Tyr
660 665 670
Ile Asp Ser Tyr Glu Asn Lys Asn Lys Ala Ile Lys Ala Ile Asn Asn
675 680 685
Ser Leu Ile Glu Arg Glu Ala Lys Trp Lys Glu Ile Tyr Ser Trp Ile
690 695 700
Val Ser Asn Trp Leu Thr Arg Ile Asn Thr Gln Phe Asn Lys Arg Lys
705 710 715 720
Glu Gln Met Tyr Gln Ala Leu Gln Asn Gln Val Asp Ala Ile Lys Thr
725 730 735
Ala Ile Glu Tyr Lys Tyr Asn Asn Tyr Thr Ser Asp Glu Lys Asn Arg
740 745 750
Leu Glu Ser Lys Tyr Asn Ile Asn Asn Ile Glu Glu Glu Leu Asn Lys
755 760 765
Lys Val Ser Leu Ala Met Lys Asn Ile Glu Arg Phe Met Thr Glu Ser
770 775 780
Ser Ile Ser Tyr Leu Met Lys Leu Ile Asn Glu Ala Glu Val Gly Lys
785 790 795 800
Leu Lys Glu Tyr Asp Lys His Val Lys Ser Asp Leu Leu Asp Tyr Ile
805 810 815
Leu Tyr His Lys Leu Ile Leu Gly Glu Gln Thr Lys Glu Leu Ile Asp
820 825 830
Leu Val Thr Ser Thr Leu Asn Ser Ser Ile Pro Phe Glu Leu Ser Ser
835 840 845
Tyr Thr Asn Asp Lys Ile Leu Ile Ile Tyr Phe Asn Arg Leu Tyr Lys
850 855 860
Lys Ile Lys Asp Ser Ser Ile Leu Asp Met Arg Tyr Glu Asn Asn Lys
865 870 875 880
Phe Ile Asp Ile Ser Gly Tyr Gly Ser Asn Ile Ser Ile Asn Gly Asn
885 890 895
Val Tyr Ile Tyr Ser Thr Asn Arg Asn Gln Phe Gly Ile Tyr Ser Gly
900 905 910
Arg Leu Ser Glu Val Asn Ile Ala Gln Asn Asn Asp Ile Ile Tyr Asn
915 920 925
Ser Arg Tyr Gln Asn Phe Ser Ile Ser Phe Trp Val Thr Ile Pro Lys
930 935 940
His Tyr Arg Pro Met Asn Arg Asn Arg Glu Tyr Thr Ile Ile Asn Cys
945 950 955 960
Met Gly Asn Asn Asn Ser Gly Trp Lys Ile Ser Leu Arg Thr Ile Arg
965 970 975
Asp Cys Glu Ile Ile Trp Thr Leu Gln Asp Thr Ser Gly Asn Lys Glu
980 985 990
Lys Leu Ile Phe Arg Tyr Glu Glu Leu Ala Ser Ile Ser Asp Tyr Ile
995 1000 1005
Asn Lys Trp Ile Phe Val Thr Ile Thr Asn Asn Arg Leu Gly Asn
1010 1015 1020
Ser Arg Ile Tyr Ile Asn Gly Asn Leu Ile Val Glu Lys Ser Ile
1025 1030 1035
Ser Asn Leu Gly Asp Ile His Val Ser Asp Asn Ile Leu Phe Lys
1040 1045 1050
Ile Val Gly Cys Asp Asp Glu Thr Tyr Val Gly Ile Arg Tyr Phe
1055 1060 1065
Lys Val Phe Asn Thr Glu Leu Asp Lys Thr Glu Ile Glu Thr Leu
1070 1075 1080
Tyr Ser Asn Glu Pro Asp Pro Ser Ile Leu Lys Asp Tyr Trp Gly
1085 1090 1095
Asn Tyr Leu Leu Tyr Asn Lys Lys Tyr Tyr Leu Phe Asn Leu Leu
1100 1105 1110
Arg Lys Asp Lys Tyr Ile Thr Arg Asn Ser Gly Ile Leu Asn Ile
1115 1120 1125
Asn Gln Gln Arg Gly Val Thr Gly Gly Ile Ser Val Phe Leu Asn
1130 1135 1140
Tyr Lys Leu Tyr Glu Gly Val Glu Val Ile Ile Arg Lys Asn Ala
1145 1150 1155
Pro Ile Asp Ile Ser Asn Thr Asp Asn Phe Val Arg Lys Asn Asp
1160 1165 1170
Leu Ala Tyr Ile Asn Val Val Asp His Gly Val Glu Tyr Arg Leu
1175 1180 1185
Tyr Ala Asp Ile Ser Ile Thr Lys Ser Glu Lys Ile Ile Lys Leu
1190 1195 1200
Ile Arg Thr Ser Asn Pro Asn Asp Ser Leu Gly Gln Ile Ile Val
1205 1210 1215
Met Asp Ser Ile Gly Asn Asn Cys Thr Met Asn Phe Gln Asn Asn
1220 1225 1230
Asp Gly Ser Asn Ile Gly Leu Leu Gly Phe His Ser Asp Asp Leu
1235 1240 1245
Val Ala Ser Ser Trp Tyr Tyr Asn His Ile Arg Arg Asn Thr Ser
1250 1255 1260
Ser Asn Gly Cys Phe Trp Ser Phe Ile Ser Lys Glu His Gly Trp
1265 1270 1275
Lys Glu
1280
<210> 13
<211> 3894
<212> DNA
<213> Clostridium botulinum
<220>
<221> misc_feature
<222> (20)..(20)
<223> n is a, c, g, or t
<400> 13
atgccagtta atataaaaan ctttaattat aatgacccta ttaataatga tgacattatt 60
atgatggaac cattcaatga cccagggcca ggaacatatt ataaagcttt taggattata 120
gatcgtattt ggatagtacc agaaaggttt acttatggat ttcaacctga ccaatttaat 180
gccagtacag gagtttttag taaagatgtc tacgaatatt acgatccaac ttatttaaaa 240
accgatgctg aaaaagataa atttttaaaa acaatgatta aattatttaa tagaattaat 300
tcaaaaccat caggacagag attactggat atgatagtag atgctatacc ttatcttgga 360
aatgcatcta caccgcccga caaatttgca gcaaatgttg caaatgtatc tattaataaa 420
aaaattatcc aacctggagc tgaagatcaa ataaaaggtt taatgacaaa tttaataata 480
tttggaccag gaccagttct aagtgataat tttactgata gtatgattat gaatggccat 540
tccccaatat cagaaggatt tggtgcaaga atgatgataa gattttgtcc tagttgttta 600
aatgtattta ataatgttca ggaaaataaa gatacatcta tatttagtag acgcgcgtat 660
tttgcagatc cagctctaac gttaatgcat gaacttatac atgtgttaca tggattatat 720
ggaattaaga taagtaattt accaattact ccaaatacaa aagaattttt catgcaacat 780
agcgatcctg tacaagcaga agaactatat acattcggag gacatgatcc tagtgttata 840
agtccttcta cggatatgaa tatttataat aaagcgttac aaaattttca agatatagct 900
aataggctta atattgtttc aagtgcccaa gggagtggaa ttgatatttc cttatataaa 960
caaatatata aaaataaata tgattttgtt gaagatccta atggaaaata tagtgtagat 1020
aaggataagt ttgataaatt atataaggcc ttaatgtttg gctttactga aactaatcta 1080
gctggtgaat atggaataaa aactaggtat tcttatttta gtgaatattt gccaccgata 1140
aaaactgaaa aattgttaga caatacaatt tatactcaaa atgaaggctt taacatagct 1200
agtaaaaatc tcaaaacgga atttaatggt cagaataagg cggtaaataa agaggcttat 1260
gaagaaatca gcctagaaca tctcgttata tatagaatag caatgtgcaa gcctgtaatg 1320
tacaaaaata ccggtaaatc tgaacagtgt attattgtta ataatgagga tttatttttc 1380
atagctaata aagatagttt ttcaaaagat ttagctaaag cagaaactat agcatataat 1440
acacaaaata atactataga aaataatttt tctatagatc agttgatttt agataatgat 1500
ttaagcagtg gcatagactt accaaatgaa aacacagaac catttacaaa ttttgacgac 1560
atagatatcc ctgtgtatat taaacaatct gctttaaaaa aaatttttgt ggatggagat 1620
agcctttttg aatatttaca tgctcaaaca tttccttcta atatagaaaa tctacaacta 1680
acgaattcat taaatgatgc tttaagaaat aataataaag tctatacttt tttttctaca 1740
aaccttgttg aaaaagctaa tacagttgta ggtgcttcac tttttgtaaa ctgggtaaaa 1800
ggagtaatag atgattttac atctgaatcc acacaaaaaa gtactataga taaagtttca 1860
gatgtatcca taattattcc ctatatagga cctgctttga atgtaggaaa tgaaacagct 1920
aaagaaaatt ttaaaaatgc ttttgaaata ggtggagccg ctatcttaat ggagtttatt 1980
ccagaactta ttgtacctat agttggattt tttacattag aatcatatgt aggaaataaa 2040
gggcatatta ttatgacgat atccaatgct ttaaagaaaa gggatcaaaa atggacagat 2100
atgtatggtt tgatagtatc gcagtggctc tcaacggtta atactcaatt ttatacaata 2160
aaagaaagaa tgtacaatgc tttaaataat caatcacaag caatagaaaa aataatagaa 2220
gatcaatata atagatatag tgaagaagat aaaatgaata ttaacattga ttttaatgat 2280
atagatttta aacttaatca aagtataaat ttagcaataa acaatataga tgattttata 2340
aaccaatgtt ctatatcata tctaatgaat agaatgattc cattagctgt aaaaaagtta 2400
aaagactttg atgataatct taagagagat ttattggagt atatagatac aaatgaacta 2460
tatttacttg atgaagtaaa tattctaaaa tcaaaagtaa atagacacct aaaagacagt 2520
ataccatttg atctttcact atataccaag gacacaattt taatacaagt ttttaataat 2580
tatattagta atattagtag taatgctatt ttaagtttaa gttatagagg tgggcgttta 2640
atagattcat ctggatatgg tgcaactatg aatgtaggtt cagatgttat ctttaatgat 2700
ataggaaatg gtcaatttaa attaaataat tctgaaaata gtaatattac ggcacatcaa 2760
agtaaattcg ttgtatatga tagtatgttt gataatttta gcattaactt ttgggtaagg 2820
actcctaaat ataataataa tgatatacaa acttatcttc aaaatgagta tacaataatt 2880
agttgtataa aaaatgactc aggatggaaa gtatctatta agggaaatag aataatatgg 2940
acattaatag atgttaatgc aaaatctaaa tcaatatttt tcgaatatag tataaaagat 3000
aatatatcag attatataaa taaatggttt tccataacta ttactaatga tagattaggt 3060
aacgcaaata tttatataaa tggaagtttg aaaaaaagtg aaaaaatttt aaacttagat 3120
agaattaatt ctagtaatga tatagacttc aaattaatta attgtacaga tactactaaa 3180
tttgtttgga ttaaggattt taatattttt ggtagagaat taaatgctac agaagtatct 3240
tcactatatt ggattcaatc atctacaaat actttaaaag atttttgggg gaatccttta 3300
agatacgata cacaatacta tctgtttaat caaggtatgc aaaatatcta tataaagtat 3360
tttagtaaag cttctatggg ggaaactgca ccacgtacaa actttaataa tgcagcaata 3420
aattatcaaa atttatatct tggtttacga tttattataa aaaaagcatc aaattctcgg 3480
aatataaata atgataatat agtcagagaa ggagattata tatatcttaa tattgataat 3540
atttctgatg aatcttacag agtatatgtt ttggtgaatt ctaaagaaat tcaaactcaa 3600
ttatttttag cacccataaa tgatgatcct acgttctatg atgtactaca aataaaaaaa 3660
tattatgaaa aaacaacata taattgtcag atactttgcg aaaaagatac taaaacattt 3720
gggctgtttg gaattggtaa atttgttaaa gattatggat atgtttggga tacctatgat 3780
aattattttt gcataagtca gtggtatctc agaagaatat ctgaaaatat aaataaatta 3840
aggttgggat gtaattggca attcattccc gtggatgaag gatggacaga ataa 3894
<210> 14
<211> 1297
<212> PRT
<213> Clostridium botulinum
<220>
<221> misc_feature
<222> (7)..(7)
<223> Xaa can be any naturally occurring amino acid
<400> 14
Met Pro Val Asn Ile Lys Xaa Phe Asn Tyr Asn Asp Pro Ile Asn Asn
1 5 10 15
Asp Asp Ile Ile Met Met Glu Pro Phe Asn Asp Pro Gly Pro Gly Thr
20 25 30
Tyr Tyr Lys Ala Phe Arg Ile Ile Asp Arg Ile Trp Ile Val Pro Glu
35 40 45
Arg Phe Thr Tyr Gly Phe Gln Pro Asp Gln Phe Asn Ala Ser Thr Gly
50 55 60
Val Phe Ser Lys Asp Val Tyr Glu Tyr Tyr Asp Pro Thr Tyr Leu Lys
65 70 75 80
Thr Asp Ala Glu Lys Asp Lys Phe Leu Lys Thr Met Ile Lys Leu Phe
85 90 95
Asn Arg Ile Asn Ser Lys Pro Ser Gly Gln Arg Leu Leu Asp Met Ile
100 105 110
Val Asp Ala Ile Pro Tyr Leu Gly Asn Ala Ser Thr Pro Pro Asp Lys
115 120 125
Phe Ala Ala Asn Val Ala Asn Val Ser Ile Asn Lys Lys Ile Ile Gln
130 135 140
Pro Gly Ala Glu Asp Gln Ile Lys Gly Leu Met Thr Asn Leu Ile Ile
145 150 155 160
Phe Gly Pro Gly Pro Val Leu Ser Asp Asn Phe Thr Asp Ser Met Ile
165 170 175
Met Asn Gly His Ser Pro Ile Ser Glu Gly Phe Gly Ala Arg Met Met
180 185 190
Ile Arg Phe Cys Pro Ser Cys Leu Asn Val Phe Asn Asn Val Gln Glu
195 200 205
Asn Lys Asp Thr Ser Ile Phe Ser Arg Arg Ala Tyr Phe Ala Asp Pro
210 215 220
Ala Leu Thr Leu Met His Glu Leu Ile His Val Leu His Gly Leu Tyr
225 230 235 240
Gly Ile Lys Ile Ser Asn Leu Pro Ile Thr Pro Asn Thr Lys Glu Phe
245 250 255
Phe Met Gln His Ser Asp Pro Val Gln Ala Glu Glu Leu Tyr Thr Phe
260 265 270
Gly Gly His Asp Pro Ser Val Ile Ser Pro Ser Thr Asp Met Asn Ile
275 280 285
Tyr Asn Lys Ala Leu Gln Asn Phe Gln Asp Ile Ala Asn Arg Leu Asn
290 295 300
Ile Val Ser Ser Ala Gln Gly Ser Gly Ile Asp Ile Ser Leu Tyr Lys
305 310 315 320
Gln Ile Tyr Lys Asn Lys Tyr Asp Phe Val Glu Asp Pro Asn Gly Lys
325 330 335
Tyr Ser Val Asp Lys Asp Lys Phe Asp Lys Leu Tyr Lys Ala Leu Met
340 345 350
Phe Gly Phe Thr Glu Thr Asn Leu Ala Gly Glu Tyr Gly Ile Lys Thr
355 360 365
Arg Tyr Ser Tyr Phe Ser Glu Tyr Leu Pro Pro Ile Lys Thr Glu Lys
370 375 380
Leu Leu Asp Asn Thr Ile Tyr Thr Gln Asn Glu Gly Phe Asn Ile Ala
385 390 395 400
Ser Lys Asn Leu Lys Thr Glu Phe Asn Gly Gln Asn Lys Ala Val Asn
405 410 415
Lys Glu Ala Tyr Glu Glu Ile Ser Leu Glu His Leu Val Ile Tyr Arg
420 425 430
Ile Ala Met Cys Lys Pro Val Met Tyr Lys Asn Thr Gly Lys Ser Glu
435 440 445
Gln Cys Ile Ile Val Asn Asn Glu Asp Leu Phe Phe Ile Ala Asn Lys
450 455 460
Asp Ser Phe Ser Lys Asp Leu Ala Lys Ala Glu Thr Ile Ala Tyr Asn
465 470 475 480
Thr Gln Asn Asn Thr Ile Glu Asn Asn Phe Ser Ile Asp Gln Leu Ile
485 490 495
Leu Asp Asn Asp Leu Ser Ser Gly Ile Asp Leu Pro Asn Glu Asn Thr
500 505 510
Glu Pro Phe Thr Asn Phe Asp Asp Ile Asp Ile Pro Val Tyr Ile Lys
515 520 525
Gln Ser Ala Leu Lys Lys Ile Phe Val Asp Gly Asp Ser Leu Phe Glu
530 535 540
Tyr Leu His Ala Gln Thr Phe Pro Ser Asn Ile Glu Asn Leu Gln Leu
545 550 555 560
Thr Asn Ser Leu Asn Asp Ala Leu Arg Asn Asn Asn Lys Val Tyr Thr
565 570 575
Phe Phe Ser Thr Asn Leu Val Glu Lys Ala Asn Thr Val Val Gly Ala
580 585 590
Ser Leu Phe Val Asn Trp Val Lys Gly Val Ile Asp Asp Phe Thr Ser
595 600 605
Glu Ser Thr Gln Lys Ser Thr Ile Asp Lys Val Ser Asp Val Ser Ile
610 615 620
Ile Ile Pro Tyr Ile Gly Pro Ala Leu Asn Val Gly Asn Glu Thr Ala
625 630 635 640
Lys Glu Asn Phe Lys Asn Ala Phe Glu Ile Gly Gly Ala Ala Ile Leu
645 650 655
Met Glu Phe Ile Pro Glu Leu Ile Val Pro Ile Val Gly Phe Phe Thr
660 665 670
Leu Glu Ser Tyr Val Gly Asn Lys Gly His Ile Ile Met Thr Ile Ser
675 680 685
Asn Ala Leu Lys Lys Arg Asp Gln Lys Trp Thr Asp Met Tyr Gly Leu
690 695 700
Ile Val Ser Gln Trp Leu Ser Thr Val Asn Thr Gln Phe Tyr Thr Ile
705 710 715 720
Lys Glu Arg Met Tyr Asn Ala Leu Asn Asn Gln Ser Gln Ala Ile Glu
725 730 735
Lys Ile Ile Glu Asp Gln Tyr Asn Arg Tyr Ser Glu Glu Asp Lys Met
740 745 750
Asn Ile Asn Ile Asp Phe Asn Asp Ile Asp Phe Lys Leu Asn Gln Ser
755 760 765
Ile Asn Leu Ala Ile Asn Asn Ile Asp Asp Phe Ile Asn Gln Cys Ser
770 775 780
Ile Ser Tyr Leu Met Asn Arg Met Ile Pro Leu Ala Val Lys Lys Leu
785 790 795 800
Lys Asp Phe Asp Asp Asn Leu Lys Arg Asp Leu Leu Glu Tyr Ile Asp
805 810 815
Thr Asn Glu Leu Tyr Leu Leu Asp Glu Val Asn Ile Leu Lys Ser Lys
820 825 830
Val Asn Arg His Leu Lys Asp Ser Ile Pro Phe Asp Leu Ser Leu Tyr
835 840 845
Thr Lys Asp Thr Ile Leu Ile Gln Val Phe Asn Asn Tyr Ile Ser Asn
850 855 860
Ile Ser Ser Asn Ala Ile Leu Ser Leu Ser Tyr Arg Gly Gly Arg Leu
865 870 875 880
Ile Asp Ser Ser Gly Tyr Gly Ala Thr Met Asn Val Gly Ser Asp Val
885 890 895
Ile Phe Asn Asp Ile Gly Asn Gly Gln Phe Lys Leu Asn Asn Ser Glu
900 905 910
Asn Ser Asn Ile Thr Ala His Gln Ser Lys Phe Val Val Tyr Asp Ser
915 920 925
Met Phe Asp Asn Phe Ser Ile Asn Phe Trp Val Arg Thr Pro Lys Tyr
930 935 940
Asn Asn Asn Asp Ile Gln Thr Tyr Leu Gln Asn Glu Tyr Thr Ile Ile
945 950 955 960
Ser Cys Ile Lys Asn Asp Ser Gly Trp Lys Val Ser Ile Lys Gly Asn
965 970 975
Arg Ile Ile Trp Thr Leu Ile Asp Val Asn Ala Lys Ser Lys Ser Ile
980 985 990
Phe Phe Glu Tyr Ser Ile Lys Asp Asn Ile Ser Asp Tyr Ile Asn Lys
995 1000 1005
Trp Phe Ser Ile Thr Ile Thr Asn Asp Arg Leu Gly Asn Ala Asn
1010 1015 1020
Ile Tyr Ile Asn Gly Ser Leu Lys Lys Ser Glu Lys Ile Leu Asn
1025 1030 1035
Leu Asp Arg Ile Asn Ser Ser Asn Asp Ile Asp Phe Lys Leu Ile
1040 1045 1050
Asn Cys Thr Asp Thr Thr Lys Phe Val Trp Ile Lys Asp Phe Asn
1055 1060 1065
Ile Phe Gly Arg Glu Leu Asn Ala Thr Glu Val Ser Ser Leu Tyr
1070 1075 1080
Trp Ile Gln Ser Ser Thr Asn Thr Leu Lys Asp Phe Trp Gly Asn
1085 1090 1095
Pro Leu Arg Tyr Asp Thr Gln Tyr Tyr Leu Phe Asn Gln Gly Met
1100 1105 1110
Gln Asn Ile Tyr Ile Lys Tyr Phe Ser Lys Ala Ser Met Gly Glu
1115 1120 1125
Thr Ala Pro Arg Thr Asn Phe Asn Asn Ala Ala Ile Asn Tyr Gln
1130 1135 1140
Asn Leu Tyr Leu Gly Leu Arg Phe Ile Ile Lys Lys Ala Ser Asn
1145 1150 1155
Ser Arg Asn Ile Asn Asn Asp Asn Ile Val Arg Glu Gly Asp Tyr
1160 1165 1170
Ile Tyr Leu Asn Ile Asp Asn Ile Ser Asp Glu Ser Tyr Arg Val
1175 1180 1185
Tyr Val Leu Val Asn Ser Lys Glu Ile Gln Thr Gln Leu Phe Leu
1190 1195 1200
Ala Pro Ile Asn Asp Asp Pro Thr Phe Tyr Asp Val Leu Gln Ile
1205 1210 1215
Lys Lys Tyr Tyr Glu Lys Thr Thr Tyr Asn Cys Gln Ile Leu Cys
1220 1225 1230
Glu Lys Asp Thr Lys Thr Phe Gly Leu Phe Gly Ile Gly Lys Phe
1235 1240 1245
Val Lys Asp Tyr Gly Tyr Val Trp Asp Thr Tyr Asp Asn Tyr Phe
1250 1255 1260
Cys Ile Ser Gln Trp Tyr Leu Arg Arg Ile Ser Glu Asn Ile Asn
1265 1270 1275
Lys Leu Arg Leu Gly Cys Asn Trp Gln Phe Ile Pro Val Asp Glu
1280 1285 1290
Gly Trp Thr Glu
1295
<210> 15
<211> 4400
<212> DNA
<213> Clostridium tetani
<400> 15
tagcattaaa aaaattagaa cctatagtaa ataaattaat taatatatag tttttataat 60
ttaattatga ataatattct taagataaaa agtaaatttt taaaaattta aattttcagt 120
ttacaaaaaa taacctgatt atgttatatg taattgtaaa aaacatataa aaaatcagaa 180
aaatttagga ggtatattat taatggatta aataataatt ttttaattta cttttgatta 240
ataaatatta aatgtttatt ttaattagga gatgatacgt atgccaataa ccataaataa 300
ttttagatat agtgatcctg ttaataatga tacaattatt atgatggagc caccatactg 360
taagggtcta gatatctatt ataaggcttt caaaataaca gatcgtattt ggatagtgcc 420
ggaaaggtat gaatttggga caaaacctga agattttaac ccaccatctt cattaataga 480
aggtgcatct gagtattacg atccaaatta tttaaggact gattctgata aagatagatt 540
tttacaaacc atggtaaaac tgtttaacag aattaaaaac aatgtagcag gtgaagcctt 600
attagataag ataataaatg ccatacctta ccttggaaat tcatattcct tactagacaa 660
gtttgataca aactctaatt cagtatcttt taatttatta gaacaagacc ccagtggagc 720
aactacaaaa tcagcaatgc tgacaaattt aataatattt ggacctgggc ctgttttaaa 780
taaaaatgag gttagaggta ttgtattgag ggtagataat aaaaattact tcccatgtag 840
agatggtttt ggctcaataa tgcaaatggc attttgccca gaatatgtac ctacctttga 900
taatgtaata gaaaatatta cgtcactcac tattggcaaa agcaaatatt ttcaagatcc 960
agcattacta ttaatgcacg aacttataca tgtactacat ggtttatacg gaatgcaggt 1020
atcaagccat gaaattattc catccaaaca agaaatttat atgcagcata catatccaat 1080
aagtgctgaa gaactattca cttttggcgg acaggatgct aatcttataa gtattgatat 1140
aaaaaacgat ttatatgaaa aaactttaaa tgattataaa gctatagcta acaaacttag 1200
tcaagtcact agctgcaatg atcccaacat tgatattgat agctacaaac aaatatatca 1260
acaaaaatat caattcgata aagatagcaa tggacaatat attgtaaatg aggataaatt 1320
tcagatacta tataatagca taatgtatgg ttttacagag attgaattgg gaaaaaaatt 1380
taatataaaa actagacttt cttattttag tatgaatcat gaccctgtaa aaattccaaa 1440
tttattagat gatacaattt acaatgatac agaaggattt aatatagaaa gcaaagatct 1500
gaaatctgaa tataaaggac aaaatatgag ggtaaataca aatgctttta gaaatgttga 1560
tggatcaggc ctagtttcaa aacttattgg cttatgtaaa aaaattatac caccaacaaa 1620
tataagagaa aatttatata atagaactgc atcattaaca gatttaggag gagaattatg 1680
tataaaaatt aaaaatgaag atttaacttt tatagctgaa aaaaatagct tttcagaaga 1740
accatttcaa gatgaaatag ttagttataa tacaaaaaat aaaccattaa attttaatta 1800
ttcgctagat aaaattattg tagattataa tctacaaagt aaaattacat tacctaatga 1860
taggacaacc ccagttacaa aaggaattcc atatgctcca gaatataaaa gtaatgctgc 1920
aagtacaata gaaatacata atattgatga caatacaata tatcaatatt tgtatgctca 1980
aaaatctcct acaactctac aaagaataac tatgactaat tctgttgatg acgcattaat 2040
aaattccacc aaaatatatt catattttcc atctgtaatc agtaaagtta accaaggtgc 2100
acaaggaatt ttattcttac agtgggtgag agatataatt gatgatttta ccaatgaatc 2160
ttcacaaaaa actactattg ataaaatttc agatgtatcc actattgttc cttatatagg 2220
acccgcatta aacattgtaa aacaaggcta tgagggaaac tttataggcg ctttagaaac 2280
taccggagtg gttttattat tagaatatat tccagaaatt actttaccag taattgcagc 2340
tttatctata gcagaaagta gcacacaaaa agaaaagata ataaaaacaa tagataactt 2400
tttagaaaaa agatatgaaa aatggattga agtatataaa ctagtaaaag caaaatggtt 2460
aggcacagtt aatacgcaat tccaaaaaag aagttatcaa atgtatagat ctttagaata 2520
tcaagtagat gcaataaaaa aaataataga ctatgaatat aaaatatatt caggacctga 2580
taaggaacaa attgccgacg aaattaataa tctgaaaaac aaacttgaag aaaaggctaa 2640
taaagcaatg ataaacataa atatatttat gagggaaagt tctagatcat ttttagttaa 2700
tcaaatgatt aacgaagcta aaaagcagtt attagagttt gatactcaaa gcaaaaatat 2760
tttaatgcag tatataaaag caaattctaa atttataggt ataactgaac taaaaaaatt 2820
agaatcaaaa ataaacaaag ttttttcaac accaattcca ttttcttatt ctaaaaatct 2880
ggattgttgg gttgataatg aagaagatat agatgttata ttaaaaaaga gtacaatttt 2940
aaatttagat attaataatg atattatatc agatatatct gggtttaatt catctgtaat 3000
aacatatcca gatgctcaat tggtgcccgg aataaatggc aaagcaatac atttagtaaa 3060
caatgaatct tctgaagtta tagtgcataa agctatggat attgaatata atgatatgtt 3120
taataatttt accgttagct tttggttgag ggttcctaaa gtatctgcta gtcatttaga 3180
acaatatggc acaaatgagt attcaataat tagctctatg aaaaaacata gtctatcaat 3240
aggatctggt tggagtgtat cacttaaagg taataactta atatggactt taaaagattc 3300
cgcgggagaa gttagacaaa taacttttag ggatttacct gataaattta atgcttattt 3360
agcaaataaa tgggttttta taactattac taatgataga ttatcttctg ctaatttgta 3420
tataaatgga gtacttatgg gaagtgcaga aattactggt ttaggagcta ttagagagga 3480
taataatata acattaaaac tagatagatg taataataat aatcaatacg tttctattga 3540
taaatttagg atattttgca aagcattaaa tccaaaagag attgaaaaat tatacacaag 3600
ttatttatct ataacctttt taagagactt ctggggaaac cctttacgat atgatacaga 3660
atattattta ataccagtag cttctagttc taaagatgtt caattgaaaa atataacaga 3720
ttatatgtat ttgacaaatg cgccatcgta tactaacgga aaattgaata tatattatag 3780
aaggttatat aatggactaa aatttattat aaaaagatat acacctaata atgaaataga 3840
ttcttttgtt aaatcaggtg attttattaa attatatgta tcatataaca ataatgagca 3900
cattgtaggt tatccgaaag atggaaatgc ctttaataat cttgatagaa ttctaagagt 3960
aggttataat gccccaggta tccctcttta taaaaaaatg gaagcagtaa aattgcgtga 4020
tttaaaaacc tattctgtac aacttaaatt atatgatgat aaaaatgcat ctttaggact 4080
agtaggtacc cataatggtc aaataggcaa cgatccaaat agggatatat taattgcaag 4140
caactggtac tttaatcatt taaaagataa aattttagga tgtgattggt actttgtacc 4200
tacagatgaa ggatggacaa atgattaaac agattgatat gttcatgatt actctatata 4260
aaaaattaaa taatataaca atctagctat attatttttg attattttct taatatatac 4320
taataaaata atcaaaatag agcctatctt aaattactga agggctgtgt caaaataaga 4380
ttttgacaca gcctctactt 4400
<210> 16
<211> 1315
<212> PRT
<213> Clostridium tetani
<400> 16
Met Pro Ile Thr Ile Asn Asn Phe Arg Tyr Ser Asp Pro Val Asn Asn
1 5 10 15
Asp Thr Ile Ile Met Met Glu Pro Pro Tyr Cys Lys Gly Leu Asp Ile
20 25 30
Tyr Tyr Lys Ala Phe Lys Ile Thr Asp Arg Ile Trp Ile Val Pro Glu
35 40 45
Arg Tyr Glu Phe Gly Thr Lys Pro Glu Asp Phe Asn Pro Pro Ser Ser
50 55 60
Leu Ile Glu Gly Ala Ser Glu Tyr Tyr Asp Pro Asn Tyr Leu Arg Thr
65 70 75 80
Asp Ser Asp Lys Asp Arg Phe Leu Gln Thr Met Val Lys Leu Phe Asn
85 90 95
Arg Ile Lys Asn Asn Val Ala Gly Glu Ala Leu Leu Asp Lys Ile Ile
100 105 110
Asn Ala Ile Pro Tyr Leu Gly Asn Ser Tyr Ser Leu Leu Asp Lys Phe
115 120 125
Asp Thr Asn Ser Asn Ser Val Ser Phe Asn Leu Leu Glu Gln Asp Pro
130 135 140
Ser Gly Ala Thr Thr Lys Ser Ala Met Leu Thr Asn Leu Ile Ile Phe
145 150 155 160
Gly Pro Gly Pro Val Leu Asn Lys Asn Glu Val Arg Gly Ile Val Leu
165 170 175
Arg Val Asp Asn Lys Asn Tyr Phe Pro Cys Arg Asp Gly Phe Gly Ser
180 185 190
Ile Met Gln Met Ala Phe Cys Pro Glu Tyr Val Pro Thr Phe Asp Asn
195 200 205
Val Ile Glu Asn Ile Thr Ser Leu Thr Ile Gly Lys Ser Lys Tyr Phe
210 215 220
Gln Asp Pro Ala Leu Leu Leu Met His Glu Leu Ile His Val Leu His
225 230 235 240
Gly Leu Tyr Gly Met Gln Val Ser Ser His Glu Ile Ile Pro Ser Lys
245 250 255
Gln Glu Ile Tyr Met Gln His Thr Tyr Pro Ile Ser Ala Glu Glu Leu
260 265 270
Phe Thr Phe Gly Gly Gln Asp Ala Asn Leu Ile Ser Ile Asp Ile Lys
275 280 285
Asn Asp Leu Tyr Glu Lys Thr Leu Asn Asp Tyr Lys Ala Ile Ala Asn
290 295 300
Lys Leu Ser Gln Val Thr Ser Cys Asn Asp Pro Asn Ile Asp Ile Asp
305 310 315 320
Ser Tyr Lys Gln Ile Tyr Gln Gln Lys Tyr Gln Phe Asp Lys Asp Ser
325 330 335
Asn Gly Gln Tyr Ile Val Asn Glu Asp Lys Phe Gln Ile Leu Tyr Asn
340 345 350
Ser Ile Met Tyr Gly Phe Thr Glu Ile Glu Leu Gly Lys Lys Phe Asn
355 360 365
Ile Lys Thr Arg Leu Ser Tyr Phe Ser Met Asn His Asp Pro Val Lys
370 375 380
Ile Pro Asn Leu Leu Asp Asp Thr Ile Tyr Asn Asp Thr Glu Gly Phe
385 390 395 400
Asn Ile Glu Ser Lys Asp Leu Lys Ser Glu Tyr Lys Gly Gln Asn Met
405 410 415
Arg Val Asn Thr Asn Ala Phe Arg Asn Val Asp Gly Ser Gly Leu Val
420 425 430
Ser Lys Leu Ile Gly Leu Cys Lys Lys Ile Ile Pro Pro Thr Asn Ile
435 440 445
Arg Glu Asn Leu Tyr Asn Arg Thr Ala Ser Leu Thr Asp Leu Gly Gly
450 455 460
Glu Leu Cys Ile Lys Ile Lys Asn Glu Asp Leu Thr Phe Ile Ala Glu
465 470 475 480
Lys Asn Ser Phe Ser Glu Glu Pro Phe Gln Asp Glu Ile Val Ser Tyr
485 490 495
Asn Thr Lys Asn Lys Pro Leu Asn Phe Asn Tyr Ser Leu Asp Lys Ile
500 505 510
Ile Val Asp Tyr Asn Leu Gln Ser Lys Ile Thr Leu Pro Asn Asp Arg
515 520 525
Thr Thr Pro Val Thr Lys Gly Ile Pro Tyr Ala Pro Glu Tyr Lys Ser
530 535 540
Asn Ala Ala Ser Thr Ile Glu Ile His Asn Ile Asp Asp Asn Thr Ile
545 550 555 560
Tyr Gln Tyr Leu Tyr Ala Gln Lys Ser Pro Thr Thr Leu Gln Arg Ile
565 570 575
Thr Met Thr Asn Ser Val Asp Asp Ala Leu Ile Asn Ser Thr Lys Ile
580 585 590
Tyr Ser Tyr Phe Pro Ser Val Ile Ser Lys Val Asn Gln Gly Ala Gln
595 600 605
Gly Ile Leu Phe Leu Gln Trp Val Arg Asp Ile Ile Asp Asp Phe Thr
610 615 620
Asn Glu Ser Ser Gln Lys Thr Thr Ile Asp Lys Ile Ser Asp Val Ser
625 630 635 640
Thr Ile Val Pro Tyr Ile Gly Pro Ala Leu Asn Ile Val Lys Gln Gly
645 650 655
Tyr Glu Gly Asn Phe Ile Gly Ala Leu Glu Thr Thr Gly Val Val Leu
660 665 670
Leu Leu Glu Tyr Ile Pro Glu Ile Thr Leu Pro Val Ile Ala Ala Leu
675 680 685
Ser Ile Ala Glu Ser Ser Thr Gln Lys Glu Lys Ile Ile Lys Thr Ile
690 695 700
Asp Asn Phe Leu Glu Lys Arg Tyr Glu Lys Trp Ile Glu Val Tyr Lys
705 710 715 720
Leu Val Lys Ala Lys Trp Leu Gly Thr Val Asn Thr Gln Phe Gln Lys
725 730 735
Arg Ser Tyr Gln Met Tyr Arg Ser Leu Glu Tyr Gln Val Asp Ala Ile
740 745 750
Lys Lys Ile Ile Asp Tyr Glu Tyr Lys Ile Tyr Ser Gly Pro Asp Lys
755 760 765
Glu Gln Ile Ala Asp Glu Ile Asn Asn Leu Lys Asn Lys Leu Glu Glu
770 775 780
Lys Ala Asn Lys Ala Met Ile Asn Ile Asn Ile Phe Met Arg Glu Ser
785 790 795 800
Ser Arg Ser Phe Leu Val Asn Gln Met Ile Asn Glu Ala Lys Lys Gln
805 810 815
Leu Leu Glu Phe Asp Thr Gln Ser Lys Asn Ile Leu Met Gln Tyr Ile
820 825 830
Lys Ala Asn Ser Lys Phe Ile Gly Ile Thr Glu Leu Lys Lys Leu Glu
835 840 845
Ser Lys Ile Asn Lys Val Phe Ser Thr Pro Ile Pro Phe Ser Tyr Ser
850 855 860
Lys Asn Leu Asp Cys Trp Val Asp Asn Glu Glu Asp Ile Asp Val Ile
865 870 875 880
Leu Lys Lys Ser Thr Ile Leu Asn Leu Asp Ile Asn Asn Asp Ile Ile
885 890 895
Ser Asp Ile Ser Gly Phe Asn Ser Ser Val Ile Thr Tyr Pro Asp Ala
900 905 910
Gln Leu Val Pro Gly Ile Asn Gly Lys Ala Ile His Leu Val Asn Asn
915 920 925
Glu Ser Ser Glu Val Ile Val His Lys Ala Met Asp Ile Glu Tyr Asn
930 935 940
Asp Met Phe Asn Asn Phe Thr Val Ser Phe Trp Leu Arg Val Pro Lys
945 950 955 960
Val Ser Ala Ser His Leu Glu Gln Tyr Gly Thr Asn Glu Tyr Ser Ile
965 970 975
Ile Ser Ser Met Lys Lys His Ser Leu Ser Ile Gly Ser Gly Trp Ser
980 985 990
Val Ser Leu Lys Gly Asn Asn Leu Ile Trp Thr Leu Lys Asp Ser Ala
995 1000 1005
Gly Glu Val Arg Gln Ile Thr Phe Arg Asp Leu Pro Asp Lys Phe
1010 1015 1020
Asn Ala Tyr Leu Ala Asn Lys Trp Val Phe Ile Thr Ile Thr Asn
1025 1030 1035
Asp Arg Leu Ser Ser Ala Asn Leu Tyr Ile Asn Gly Val Leu Met
1040 1045 1050
Gly Ser Ala Glu Ile Thr Gly Leu Gly Ala Ile Arg Glu Asp Asn
1055 1060 1065
Asn Ile Thr Leu Lys Leu Asp Arg Cys Asn Asn Asn Asn Gln Tyr
1070 1075 1080
Val Ser Ile Asp Lys Phe Arg Ile Phe Cys Lys Ala Leu Asn Pro
1085 1090 1095
Lys Glu Ile Glu Lys Leu Tyr Thr Ser Tyr Leu Ser Ile Thr Phe
1100 1105 1110
Leu Arg Asp Phe Trp Gly Asn Pro Leu Arg Tyr Asp Thr Glu Tyr
1115 1120 1125
Tyr Leu Ile Pro Val Ala Ser Ser Ser Lys Asp Val Gln Leu Lys
1130 1135 1140
Asn Ile Thr Asp Tyr Met Tyr Leu Thr Asn Ala Pro Ser Tyr Thr
1145 1150 1155
Asn Gly Lys Leu Asn Ile Tyr Tyr Arg Arg Leu Tyr Asn Gly Leu
1160 1165 1170
Lys Phe Ile Ile Lys Arg Tyr Thr Pro Asn Asn Glu Ile Asp Ser
1175 1180 1185
Phe Val Lys Ser Gly Asp Phe Ile Lys Leu Tyr Val Ser Tyr Asn
1190 1195 1200
Asn Asn Glu His Ile Val Gly Tyr Pro Lys Asp Gly Asn Ala Phe
1205 1210 1215
Asn Asn Leu Asp Arg Ile Leu Arg Val Gly Tyr Asn Ala Pro Gly
1220 1225 1230
Ile Pro Leu Tyr Lys Lys Met Glu Ala Val Lys Leu Arg Asp Leu
1235 1240 1245
Lys Thr Tyr Ser Val Gln Leu Lys Leu Tyr Asp Asp Lys Asn Ala
1250 1255 1260
Ser Leu Gly Leu Val Gly Thr His Asn Gly Gln Ile Gly Asn Asp
1265 1270 1275
Pro Asn Arg Asp Ile Leu Ile Ala Ser Asn Trp Tyr Phe Asn His
1280 1285 1290
Leu Lys Asp Lys Ile Leu Gly Cys Asp Trp Tyr Phe Val Pro Thr
1295 1300 1305
Asp Glu Gly Trp Thr Asn Asp
1310 1315
Claims (15)
- 세포 내로의 신경독소 폴리펩티드의 특이적 흡수를 향상시키는 방법으로서,
신경독소 중독에 민감한 세포를 신경독소 폴리펩티드와 함께, 상기 신경독소 폴리펩티드가 그의 생물학적 활성을 발휘할 수 있게 하는 시간 동안 그리고 그렇게 하는 조건 하에서 인큐베이션하여, 상기 세포 내로의 상기 신경독소 폴리펩티드의 특이적 흡수를 향상시키는 단계를 포함하며,
상기 인큐베이션은 하기 단계 중 적어도 둘을 포함하는, 방법: (i) 상기 세포의 K+ 매개 탈분극, (ii) 감소된 신경독소 폴리펩티드 제시(exposition) 시간 및/또는 (iii) 신경독소 폴리펩티드 제시 동안 상기 세포의 교반. - 제1항에 있어서, 상기 세포에서 상기 신경독소 폴리펩티드의 생물학적 활성을 결정하는 단계가 후속하는, 방법.
- 세포에서 신경독소 폴리펩티드의 생물학적 활성을 직접 결정하는 방법으로서,
a) 신경독소 중독에 민감한 세포를 신경독소 폴리펩티드와 함께, 상기 신경독소 폴리펩티드가 그의 생물학적 활성을 발휘할 수 있게 하는 시간 동안 그리고 그렇게 하는 조건 하에서 인큐베이션하는 단계 - 상기 인큐베이션은 하기 단계 중 적어도 둘을 포함함: (i) 상기 세포의 K+ 매개 탈분극, (ii) 감소된 신경독소 폴리펩티드 제시 시간 및/또는 (iii) 신경독소 폴리펩티드 제시 동안 상기 세포의 교반 -;
b) 상기 세포를 고정시키고, 선택적으로 표면활성제(detergent)를 사용하여 상기 세포를 투과화(permeabilize)하는 단계;
c) 상기 세포를, 비-절단(non-cleaved) 기질과 신경독소 절단 기질에 특이적으로 결합하는 적어도 제1 포획 항체 및 상기 신경독소 절단 기질의 절단 부위에 특이적으로 결합하는 적어도 제2 포획 항체와, 상기 기질에 대한 상기 포획 항체의 결합을 가능하게 하는 조건 하에서 접촉시키는 단계;
d) 상기 세포를, 상기 제1 포획 항체에 특이적으로 결합하는 적어도 제1 검출 항체와, 상기 제1 포획 항체에 대한 상기 제1 검출 항체의 결합을 가능하게 하는 조건 하에서 접촉시켜 제1 검출 복합체를, 그리고 상기 제2 포획 항체에 특이적으로 결합하는 적어도 제2 검출 항체와, 상기 제2 포획 항체에 대한 상기 제2 검출 항체의 결합을 가능하게 하는 조건 하에서 접촉시켜 제2 검출 복합체를 형성하는 단계;
e) 단계 d)의 상기 제1 검출 복합체와 상기 제2 검출 복합체의 양을 결정하는 단계; 및
f) 상기 세포에서 상기 신경독소 폴리펩티드에 의해 절단된 기질의 양을 상기 제2 검출 복합체로 계산하여 상기 세포에서 상기 신경독소 폴리펩티드의 생물학적 활성을 결정하는 단계를 포함하는, 방법. - 제1항 내지 제3항 중 어느 한 항에 있어서, 상기 세포의 K+ 매개 탈분극은 약 20 mM 내지 약 55 mM의 추가 K+ 농도에서 적어도 2시간 동안 수행되는, 방법.
- 제1항 내지 제4항 중 어느 한 항에 있어서, 상기 세포의 K+ 매개 탈분극 및/또는 신경독소 폴리펩티드 제시는 GT1b의 존재 하에 수행되는, 방법.
- 제1항 내지 제5항 중 어느 한 항에 있어서, GT1b는 15 내지 50 μM, 바람직하게는 20 μM의 농도로 사용되는, 방법.
- 제1항 내지 제6항 중 어느 한 항에 있어서, 상기 감소된 신경독소 폴리펩티드 제시 시간은 적어도 24시간 내지 96시간 미만 동안, 바람직하게는 적어도 48시간 내지 최대 72시간 동안 상기 신경독소 폴리펩티드에 대한 상기 세포의 제시인, 방법.
- 제1항 내지 제7항 중 어느 한 항에 있어서, 신경독소 폴리펩티드 제시 동안 상기 세포의 교반은, 바람직하게는 약 25 cm/분 내지 약 300 cm/분의 평균 배지 유속(mean medium flow rate)에서, 자석 교반기, 회전 스피너 플라스크(rotating spinner flask) 또는 진탕기에 의한 상기 세포의 진탕으로 수행되는, 방법.
- 제1항 내지 제8항 중 어느 한 항에 있어서, 상기 세포의 K+ 매개 탈분극은 20 μM의 GT1b 및 신경독소 폴리펩티드의 존재 하에 적어도 약 20 mM 내지 약 55 mM의 추가 K+ 농도에서 적어도 2시간 동안 수행되고, 이어서 교반 하에서 추가 70시간 동안 신경독소 폴리펩티드 제시가 수행되는, 방법.
- 제1항 내지 제8항 중 어느 한 항에 있어서, 신경독소 폴리펩티드가 없는 상태의 인큐베이션 시간이 상기 신경독소 폴리펩티드 제시보다 선행되는, 방법.
- 제10항에 있어서, 신경독소 폴리펩티드가 없는 상태의 상기 인큐베이션 시간은 16 내지 48시간인, 방법.
- 제1항 내지 제11항 중 어느 한 항에 있어서, 상기 방법은 형광 방법인, 방법.
- 제1항 내지 제12항 중 어느 한 항에 있어서, 상기 신경독소 폴리펩티드는 BoNT/A, BoNT/B, BoNT/C1, BoNT/D, BoNT/E, BoNT/F, BoNT/G, BoNT/H, TeNT, 또는 이의 서브타입인, 방법.
- 제1항 내지 제13항 중 어느 한 항에 있어서, 상기 기질은 VAMP/시냅토브레빈(Synaptobrevin), SNAP-25 또는 신택신(Syntaxin)인, 방법.
- 제1항 내지 제14항 중 어느 한 항에 있어서, 상기 세포는 1차 신경 세포, 신경 세포로 분화할 수 있는 종양 세포, 예를 들어 신경모세포종 세포, P19 세포 또는 유도 만능성 줄기 세포 (induced pluripotent stem cell, IPS) 유래 뉴런으로 이루어진 군으로부터 선택된 신경 세포 또는 신경 분화 세포인, 방법.
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