CN112708630A - 用于慢性疼痛的多蛋白酶治疗剂 - Google Patents
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Abstract
本发明涉及用于慢性疼痛的多蛋白酶治疗剂。本发明包括含有至少两个轻链内肽酶结构域的梭菌属神经毒素衍生物，以及编码所述梭菌属神经毒素衍生物的核酸。在优选实施方案中，本发明包括用于通过使用所述梭菌属神经毒素衍生物治疗炎性病症(如关节炎)；慢性疼痛如神经性疼痛和炎性疼痛的方法和组合物，所述梭菌属神经毒素衍生物包括源自具有连接至LC/A内肽酶的LC/E来源的内肽酶的完整BoNT/A的那些。
Description
本申请是PCT申请号PCT/EP2014/078732，发明名称为“用于慢性疼痛的多蛋白酶治疗剂”，申请日为2014年12月19日的PCT申请进入中国国家阶段后申请号为201480073447.X的中国国家阶段申请的分案申请。
本发明涉及方法和组合物，所述方法和组合物涉及具有增强的破坏来自疼痛感受器或炎症诱导物的疼痛和/或炎症介质的胞外分泌能力的梭菌属神经毒素。
背景
通过肉毒梭菌产生的肉毒杆菌神经毒素(BoNT)血清型A-G由于通过蛋白水解裂解SNARE(“可溶性NSF附着蛋白受体”)蛋白质来特异性地阻断乙酰胆碱从外周神经的释放而是已知的最强效毒物，所述蛋白质介导突触囊泡与细胞膜的融合，且因此是Ca2+刺激的神经递质、疼痛肽和细胞因子从神经元的胞外分泌来说必需的。
梭菌属毒素例如像肉毒杆菌神经毒素(BoNT)(包括BoNT血清型BoNT/A、BoNT/B、BoNT/C1、BoNT/D、BoNT/E、BoNT/F以及BoNT/G，以及破伤风毒素TeTx)抑制神经元传递的能力已在多种治疗性应用和美容应用中得到应用，参见例如Ward AB和Barnes MP，CLINICALUSERS OF BOTULINUM TOXINS(Cambridge University Press,Cambridge 2007)。作为实例，BoNT/A来源的药剂
已在一个或多个国家用于以下适应症：迟缓不能、成人痉挛状态、肛裂、背痛、眼睑痉挛、磨牙症、颈肌张力障碍、特发性震颤、眉间纹或过动性面部皱纹、头痛、半面痉挛、膀胱过动症、多汗症、青少年大脑性瘫痪、多发性硬化症、肌阵挛性病症、鼻唇纹、痉挛性发音障碍、斜视以及VII神经病症。
存在除了肉毒梭菌和破伤风梭菌来源的毒素以外的梭菌属毒素；这些包括但不限于产气荚膜梭菌、败毒梭菌、艰难梭菌、螺状梭菌、丁酸梭菌以及巴氏梭菌。然而，应理解在本说明书中，除非另外具体地或上下文指示，提及“梭菌属毒素”或类似提及涉及肉毒梭菌亚型和破伤风梭菌亚型。
此外，梭菌属毒素疗法用于或已被提出用于治疗包括但不限于以下的病状，
a)神经肌肉病症，参见例如，Kei Roger Aoki等人,Method for TreatingNeuromuscular Disorders and Conditions with Botulinum Toxin Types A and B,美国专利号6,872,397(2005年3月29日)；Rhett M.Schiffman,Methods for TreatingUterine Disorders,美国专利公布号2004/0175399(2004年9月9日)；Richard L.Barron,Methods for Treating Ulcers and Gastroesophageal Reflux Disease,美国专利公布号2004/0086531(2004年5月7日)；以及Kei Roger Aoki等人,Method for TreatingDystonia with Botulinum Toxin C to G,美国专利号6,319,505(2001年11月20日)；
b)眼病症，参见例如，Eric R.First,Methods and Compositions for TreatingEye Disorders,美国专利公布号2004/0234532(2004年11月25日)；Kei Roger Aoki等人,Botulinum Toxin Treatment for Blepharospasm,美国专利公布号2004/0151740(2004年8月5日)；以及Kei Roger Aoki等人,Botulinum Toxin Treatment for Strabismus,美国专利公布号2004/0126396(2004年7月1日)；
c)疼痛，参见例如，Kei Roger Aoki等人,Pain Treatment by PeripheralAdministration of a Neurotoxin,美国专利号6,869,610(2005年3月22日)；StephenDonovan,Clostridial Toxin Derivatives and Methods to Treat Pain,美国专利号6,641,820(2003年11月4日)；Kei Roger Aoki等人,Method for Treating Pain byPeripheral Administration of a Neurotoxin,美国专利号6,464,986(2002年10月15日)；Kei Roger Aoki和Minglei Cui,Methods for Treating Pain,美国专利号6,113,915(2000年9月5日)；Martin A.Voet,Methods for Treating Fibromyalgia,美国专利6,623,742(2003年9月23日)；Martin A.Voet,Botulinum Toxin Therapy for Fibromyalgia,美国专利公布号2004/0062776(2004年4月1日)；以及Kei Roger Aoki等人,Botulinum ToxinTherapy for Lower Back Pain,美国专利公布号2004/0037852(2004年2月26日)；
d)肌肉损伤，参见例如，Gregory F.Brooks,Methods for Treating MuscleInjuries,美国专利号6,423,319(2002年7月23日)；
e)头痛，参见例如，Martin Voet,Methods for Treating Sinus Headache,美国专利号6,838,434(2005年1月4日)；Kei Roger Aoki等人,Methods for Treating TensionHeadache,美国专利号6,776,992(2004年8月17日)；以及Kei Roger Aoki等人,Method forTreating Headache,美国专利号6,458,365(2002年10月1日)；William J.Binder,Methodfor Reduction of Migraine Headache Pain,美国专利5,714,469(1998年2月3日)；
f)心血管疾病，参见例如，Gregory F.Brooks和Stephen Donovan,Methods forTreating Cardiovascular Diseases with Botulinum Toxin,美国专利号6,767,544(2004年7月27日)；
e)神经病症，参见例如，Stephen Donovan,Parkinson's Disease Treatment,美国专利号6,620,415(2003年9月16日)；以及Stephen Donovan,Method for TreatingParkinson's Disease with a Botulinum Toxin,美国专利号6,306,403(2001年10月23日)；
g)神经精神病症，参见例如，Stephen Donovan,Botulinum Toxin Therapy forNeuropsychiatric Disorders,美国专利公布号2004/0180061(2004年9月16日)；以及Steven Donovan,Therapeutic Treatments for Neuropsychiatric Disorders,美国专利公布号2003/0211121(2003年11月13日)；
f)内分泌病症，参见例如，Stephen Donovan,Method for Treating EndocrineDisorders,美国专利号6,827,931(2004年12月7日)；Stephen Donovan,Method forTreating Thyroid Disorders with a Botulinum Toxin,美国专利号6740321(2004年5月25日)；Kei Roger Aoki等人,Method for Treating a Cholinergic Influenced SweatGland,美国专利号6,683,049(2004年1月27日)；Stephen Donovan,Neurotoxin Therapyfor Diabetes,美国专利号6,416,765(2002年7月9日)；Stephen Donovan,Methods forTreating Diabetes,美国专利号6,337,075(2002年1月8日)；Stephen Donovan,Methodfor Treating a Pancreatic Disorder with a Neurotoxin,美国专利号6,261,572(2001年7月17日)；Stephen Donovan,Methods for Treating Pancreatic Disorders,美国专利号6,143,306(2000年11月7日)；
g)癌症，参见例如，Stephen Donovan,Methods for Treating Bone Tumors,美国专利号6,565,870(2003年5月20日)；Stephen Donovan,Method for Treating Cancerwith a Neurotoxin to Improve Patient Function,美国专利号6,368,605(2002年4月9日)；Stephen Donovan,Method for Treating Cancer with a Neurotoxin,美国专利号6,139,845(2000年10月31日)；以及Mitchell F.Brin和Stephen Donovan,Methods forTreating Diverse Cancers,美国专利公布号2005/0031648(2005年2月10日)；
h)耳病症，参见例如，Stephen Donovan,Neurotoxin Therapy for Inner EarDisorders,美国专利号6358926(2002年3月19日)；以及Stephen Donovan,Method forTreating Otic Disorders,美国专利号6265379(2001年7月24日)；
i)自主神经病症，参见例如，Pankai J.Pasricha和Anthony N.Kalloo,Methodfor Treating Gastrointestinal Muscle Disorders and Other Smooth MuscleDysfunction,美国专利5,437,291(1995年8月1日)；
j)以及其他病症，参见例如，William J.Binder,Method for Treatment of SkinLesions Associated with Cutaneous Cell-proliferative Disorders,美国专利5,670,484(1997年9月23日)；Eric R.First,Application of Botulinum Toxin to theManagement of Neurogenic Inflammatory Disorders,美国专利6,063,768(2000年5月16日)；Marvin Schwartz和Brian J.Freund,Method to Reduce Hair Loss andStimulateHair Growth,美国专利6,299,893(2001年10月9日)；Jean D.A.Carruthers和AlastairCarruthers,Cosmetic Use of Botulinum Toxin for Treatment of Downturned Mouth,美国专利6,358,917(2002年3月19日)；Stephen Donovan,Use of a Clostridial Toxinto Reduce Appetite,美国专利公布号2004/40253274(2004年12月16日)；以及HowardI.Katz和Andrew M.Blumenfeld,Botulinum Toxin Dental Therapies and Procedures,美国专利公布号2004/0115139(2004年6月17日)；Kei Roger Aoki等人,Treatment ofNeuromuscular Disorders and Conditions with Different Botulinum,美国专利公布号2002/0010138(2002年1月24日)；以及Kei Roger Aoki等人,Use of Botulinum Toxinsfor Treating Various Disorders and Conditions and Associated Pain,美国专利公布号2004/0013692(2004年1月22日)。
以下表2提供各种当前已知的肉毒杆菌相关的(BoNT和TeTX)梭菌属毒素的同种型的氨基酸序列。这些毒素彼此具有最少约35％氨基酸同一性且共享相同的功能性结构域组织和总体结构架构。天然存在的梭菌属毒素各自被翻译为约150kDa的单链多肽，所述单链多肽的二硫环随后被天然存在的蛋白酶(例如像内源性梭菌属毒素蛋白酶或环境中产生的天然存在的蛋白酶)通过蛋白水解切割作用而裂解。这种翻译后加工产生成熟双链分子，所述分子包含约50kDa轻链(LC)和约100kDa重链(HC)，二者通过单个链间二硫键和非共价相互作用结合在一起。
各成熟双链梭菌属毒素分子包含三个功能上不同的结构域：1)位于LC中的酶结构域，其包含含有特异性地靶向介导突触囊泡与细胞膜的融合的一种或多种SNARE蛋白的锌依赖性内肽酶活性的金属蛋白酶区；2)含于H链的氨基端半部(称为“HN”)内的易位结构域，其促进毒素的至少LC链从内体释放至靶细胞的细胞质中；以及3)存在于H链的羧基端半部(HC)中的结合结构域，其决定毒素的结合活性和结合特异性。
HC包含HCN和HCC亚结构域(分别HC的N-末端部分和C末端部分)。现在存在大量证据表明大多数或所有BoNT/X毒素使用“双重受体”结合靶细胞，其中毒素的包含HCN和HCC亚结构域两者的HC部分结合某些细胞表面神经节苷脂和蛋白质受体(可能糖基化的)；所述蛋白质受体的结合有助于细胞内的毒素的内化。“X”意指肉毒杆菌毒素的任一血清型。虽然术语“BoNT/X”通常用于指示肉毒杆菌毒素的血清型，但所述术语还可包括其TeTX区。HCC结合在靶细胞的表面处复杂定位的受体。
应理解存在这些毒素的每种血清型的菌株或亚型；这些可在其氨基酸序列中、特别是(但非排他性地)在所指示毒素或毒素结构域的同一性或活性特征中无显著变化的非关键区(所谓的“可变”区)中在某种程度上不同。
在一些表1中，提供标准单字母和三字母氨基酸代码：
表1
表2
本领域的普通技术人员认识到，梭菌属亚型毒素变体可存在于自然中，具有以上所示的氨基酸序列(或编码这些氨基酸序列的核苷酸序列)的变化。如本文所用，术语“天然存在的梭菌属结构域变体”意指由天然存在的过程产生的任何梭菌属结构域(内肽酶、易位和/或结合结构域)，包括但不限于由选择性剪接的转录物产生的梭菌属结构域同工型、由自发突变产生的梭菌属结构域同工型和梭菌属结构域亚型。如本文所用，天然存在的梭菌属结构域变体可与所述天然存在的梭菌属结构域变体所基于的参考梭菌属结构域实质上相同的方式起作用，且在本发明的任何方面中可取代参考梭菌属结构域。
天然存在的梭菌属结构域变体可取代来自所述天然存在的梭菌属结构域变体所基于的参考梭菌属结构域的一个或多个氨基酸、两个或更多个氨基酸、三个或更多个氨基酸、四个或更多个氨基酸、五个或更多个氨基酸、十个或更多个氨基酸、20个或更多个氨基酸、30个或更多个氨基酸、40个或更多个氨基酸、50个或更多个氨基酸或100个或更多个氨基酸。天然存在的梭菌属结构域变体还可取代来自所述天然存在的梭菌属结构域变体所基于的参考梭菌属结构域的至少10个连续氨基酸、至少15个连续氨基酸、至少20个连续氨基酸或至少25个连续氨基酸，所述天然存在的梭菌属结构域变体与所述天然存在的梭菌属结构域变体所基于的参考梭菌属结构域具有至少50％氨基酸同一性、65％氨基酸同一性、75％氨基酸同一性、85％氨基酸同一性或95％氨基酸同一性，只要所述天然存在的梭菌属结构域的生物或生物化学活性被基本上保留。还应了解，还可进行保守性氨基酸插入和缺失，只要所述结构域的特征性功能和同一性未基本上改变。
由于遗传密码的简并性，本领域的普通技术人员将认识到这些氨基酸序列可由一组有限的具有不同但限定的核苷酸序列的不同DNA分子编码。例如，编码给定肽或蛋白质的简并核苷酸序列可具有适于或被选择用于有利于在特定宿主细胞中表达的不同密码子。使用这一信息，能够构建可表达的开放核酸阅读框以用于组装包含这些氨基酸结构域编码区的任何组合的核酸分子，单独地或与另外的核酸序列组合，插入至适合的表达载体中且随后在所选择的宿主细胞中表达。例如，国际专利公布WO01/14570公开制备单链可裂解的重组修饰或未修饰的梭菌属神经毒素衍生物的方法以及使用这类方法制备其嵌合和杂合形式。公开制备可表达的重组神经毒素及其衍生物的方法的另外公布包括美国专利5,989,545；6,203,794；6,395,513；美国公布号U.S.2003/0166238；U.S.2002/169942；U.S.2004/176299；U.S.2004/126397；U.S.2005/035730；U.S.2005/068494；U.S.2006/011966；国际专利公布W095/32738；WO 99/55359；W096/33273；W098/07864；W099/17806；WO98/07864；WO02/44199；WO02/40506以及2012年10月4日提交的美国专利申请序列号13/644,386。在本专利申请中引用的这些和所有其他专利、专利公布以及非专利公布(无论是否如此具体地指示)据此以引用的方式作为本说明书的一部分单独地并入。
使用重组DNA技术允许从天然存在的毒素亚型及其菌株构建具有不同或修饰的功能特性的修饰的梭菌属神经毒素。
例如，改变天然神经毒素轻链的天然存在的氨基酸序列和/或添加不同的治疗性部分允许构建被设计用于在神经元内携带治疗剂的转运蛋白。参见美国专利号6,203,794(据此以引用的方式并入本文)。
改变靶向(细胞结合)结构域允许毒素在胰腺细胞如腺泡细胞内转运，从而防止由这类细胞分泌活化的消化酶，参见美国专利号6,843,998(据此以引用的方式并入本文)；或在感觉传入神经元内转运，从而防止神经递质、细胞因子和特通肽释放且因此提供疼痛缓解；参见美国专利号6,395,513(据此以引用的方式并入本文)。
此外，美国专利号7,422,877(据此以引用的方式并入本文)公开了嵌合神经毒素衍生物的产生，所述嵌合神经毒素衍生物包含例如一种神经毒素亚型(例如BoNT/A)的结合结构域和易位结构域(或其修饰型式)以及另一种神经毒素亚型(例如BoNT/E)的轻链区。由此可见鉴于神经毒素亚型之间的总体结构同源性，三种基本梭菌属神经毒素结构域的任何组合可在单一氨基酸链中(或在裂解的双链分子中)进行。因此例如，来自神经毒素亚型A、B、C1、D、E、F、G或TeTX中的任一种的结合结构域可独立地与来自神经毒素亚型A、B、C1、D、E、F、G或TeTX的易位结构域组合，且进一步独立地与来自神经毒素亚型A、B、C1、D、E、F、G或TeTX中的任一种的内肽酶结构域组合。这可例如通过重组构建且表达随后裂解以产生双链毒素的单一嵌合链或通过单独表达单一H链和L链来进行，所述单一H链和L链然后通过例如产生链间二硫键且随后纯化进行组合。此外，使用这类技术，可改变不同结构域的活性(例如，可在LC结构域中引入突变以破坏LC的蛋白酶活性)，或可用其他部分置换天然存在的结构域，如本文其他地方所描述，其中例如BoNT/A的HC结构域(或其一部分)突变或缺失且附加靶向配体(TL)。
当讨论每种梭菌属神经毒素亚型的三种一般神经毒素结构域(结合、易位和内肽酶)时，应了解梭菌属神经毒素研究是发展良好的领域，并且矫正包含具有其功能的这些结构域中的每种的氨基酸序列是熟知的。提及这些术语中的每种(“易位结构域”、“结合结构域”、以及“蛋白酶”、“内肽酶”、“LC”或“轻链”结构域)应被理解为包括包含于如表2中列举的SEQ ID NO:7-14中列举的梭菌属神经毒素亚型的氨基酸序列中的任一个中的相应结构域以及这些序列或这些序列内的结构域的保守性修饰和优化的变体。
另外，这些一般结构域细分成亚结构域也是已知的。例如，结合结构域HC细分成亚结构域HCN(所述结构域的氨基末端部分，大致对应于BoNT/A的氨基酸871-1091)和HCC(HC结构域的羧基末端部分，大致对应于BoNT/A的氨基酸1092-1296)也是熟知的。参见例如，LacyDB和Stevens RC,Sequence Homology and Structural Analysis of the ClostridialNeurotoxins,1999,J.Mol.Biol.291:1091-1104。亚结构域HCN在肉毒杆菌毒素亚型之中是高度保守的，然而，关于其功能所知甚少。HCC亚结构域是不太保守的。
另外，这些结构域和亚结构域各自的核苷酸序列和氨基酸序列是已知的并且已在本说明书中公开，且因此使用本公开与遗传密码的知识的组合，可制备编码待表达的蛋白质的核苷酸序列。当然，鉴于本说明书对于本领域的普通技术人员来说立即设想编码所指示多肽的其他核苷酸序列将是常规问题。此外，由于遗传密码的冗余，对于每种多肽来说有限数目的核苷酸序列是可能的。此外，清楚的是可合成在同源性区中包含这些核苷酸序列(或它们的独特部分)的含有与参考序列的不超过10％、8％或5％碱基对差异的保守性修饰的变体。
此外，应了解在表2和本说明书中其他地方或相关序列表中提出的氨基酸序列提供编码这些氨基酸序列及其指示区域的任何和所有核苷酸序列的完整公开。编码给定神经毒素亚型的内肽酶结构域、易位结构域或结合结构域(包括任何亚结构域)的核苷酸序列分别可与表2或其他地方中列举的这类参考氨基酸序列区域中的任一者具有60％或更大、或65％或更大、或70％或更大、或75％或更大、或80％或更大、或85％或更大、或90％或更大、或95％或更大或100％同一性。
肉毒杆菌神经毒素由梭菌属细胞表达，所述细胞还产生与神经毒素非共价缔合以形成血凝素复合物(还被称为祖细胞复合物)的一种或多种非毒素“神经毒素相关蛋白”或NAP。这些NAP帮助神经毒素在其于污染的食物中消化时抵抗肠中的蛋白酶降解。
NAP蛋白包括三种血凝素(HA)蛋白(HA1、HA2和HA3)以及非毒性非血凝素蛋白(NTNH)。BoNT A2型、E型和F型不具有HA基因，并且仅产生包含BoNT和NTNH的12S(约300kDa)复合物。“S”代表斯维德伯格单位(离心沉降率的单位)。B型、C型和D型产生12S和16S(约500kDa)复合物；16S复合物包括BoNT、NTNH、HA1、HA2和HA3。A1型具有12S和16S复合物加约900kDA的19S复合物，其可表示16S复合物的二聚体。
当前，BoNT/A1-和/B-血凝素复合物已被批准用于这类临床用途。BoNT/A1复合物的治疗益处比BoNT/B的治疗益处更持久，这是由于其在神经元中具有较长寿命的蛋白酶。
如以上所指示，BoNT由轻链相关蛋白酶结构域(LC)组成，所述结构域通过单个共价二硫键和另外非非共价键连接至重链(HC)。HC的羧基末端(C末端)部分(HC)结合在各种神经类型(包括运动、自主和感觉神经元)上表达的其特异性受体。当结合靶细胞时，BoNT分子通过内吞作用转运至囊泡中；HC的氨基末端(N末端)半部(HN)形成允许LC从‘内体样’膜囊泡易位至细胞溶质中的通道。此后，LC裂解特异性SNARE蛋白质底物，从而破坏SNARE介导囊泡-膜融合且因此神经递质、细胞因子和疼痛肽从细胞释放的能力。
不同BoNT血清型的LC是类似的，但不是相同的，并且两个不同的LC可裂解不同的SNARE蛋白，或不同地裂解同一SNARE蛋白。例如，LC/A、LC/C和LC/E裂解SNAP-25；LC/B、LC/D、LC/F和LC/G裂解小突触泡蛋白-2(VAMP-2)；此外，LC/C裂解突触融合蛋白，其是据报道为细胞分裂所需的另一种SNARE蛋白。TeTx的LC裂解VAMP-2。每种血清型的LC在分子中的独特位置处裂解其底物。
例如，BoNT/A(LC/A)的轻链从SNAP-25的C末端去除9个氨基酸，而LC/E缺失另外17个C末端残基，并且因此通过通过对稳定的SNARE复合物去稳定而得到神经-胞外分泌的更具破坏性的阻断(Meng等人,2009；Wang等人,2011)。例如，通过LC/A抑制神经递质释放通常可通过升高Ca2+流入逆转，但在LC/E的情况下不能，这可能是由于SNAP-25底物的更大破坏。然而，尽管通过LC/E更大的活性“稳健性”，因为LC/E诱导仅较短的瞬时神经肌肉麻痹，所以其临床应用受到限制。
高度希望产生具有新特性的治疗剂。例如，其中两种或更多种源自多于一种血清型的轻链内肽酶可组合在BoNT或TeTx衍生物中(其中每个轻链是活性的且识别其底物SNARE蛋白中的不同氨基酸序列)的治疗剂可被设计成靶向如慢性疼痛、慢性炎性病状(包括关节炎)的病状和/或涉及细胞因子释放的病状。
在一个实例中，设计将LC/E的强效蛋白酶与LC/A的长效作用组合的治疗剂。对于提高用于治疗慢性疼痛(包括紧张性头痛/偏头痛和慢性炎性疾病如关节炎)的BoNT/A的功效来说这是特别重要的，因为BoNT/A复合物本身据发现在一些但并非所有这类患者中是有效的。参见例如，Naumann M.等人(2008)ASSESSMENT:BOTULINUM NEUROTOXIN IN THE TREATMENTOF AUTONOMIC DISORDERS AND PAIN(AN EVIDENCE-BASED REVIEW):REPORT OF THETHERAPEUTICS AND TECHNOLOGY ASSESSMENT SUBCOMMITTEE OF THE AMERICAN ACADEMYOF NEUROLOGY 70:1707-1714(据此以引用的方式并入本文)。阻断疼痛相关因子如疼痛蛋白和细胞因子的胞外分泌可证明适用于治疗慢性疼痛、神经性疼痛和炎性病状。
当通过活化TRPV1(瞬时受体电位香草酸1)(参与大多形式的疼痛的信号转导的阳离子通道)引发时，BoNT/A不能阻断疼痛刺激肽[例如降钙素基因相关肽(CGRP)和底物P]从感觉神经元的胞外分泌(Meng等人,2007；Meng等人,2009)。
BoNT/E也未能抑制来自感觉神经元的辣椒素刺激的、TRPV1介导的CGRP和物质P释放，这是由于其细胞表面受体(糖基化的突触囊泡蛋白2A(SVP2A)和糖基化的SVP2B)稀疏或从感觉神经元缺失。然而，其中BoNT/E的HC(受体结合结构域)被来自BoNT/A的其对应物置换的嵌合蛋白能够阻断这些疼痛介导的肽的释放，从而表明BoNT/A细胞表面受体有助于LC/E内吞和递送至伤害性C纤维中。
一旦在神经元内部，LC/E蛋白酶就去除26个SNAP-25氨基酸残基，由此防止为神经-胞外分泌所需的稳定SNARE复合物的形成(Meng等人,2009)。虽然LC/A也裂解SNAP-25，但它仅裂解9个氨基酸残基，并且胞外分泌活性的阻断不太完全和稳定。
为了使临床上使用LC/E蛋白酶的这种有利特征变得实际，希望极大地延伸其作用持续时间。
附图简述
图1是用于通过产生编码经由接头连接至BoNT/A的N末端LC/A部分的活性LC/E的基因构建体以产生含有两种活性蛋白酶的复合神经毒素LC/E-BoNT/A而产生复合神经毒素的示意图。
图2A是示出使用
Superflow树脂(由Clonetech Laboratories,Inc.制造)(一种对His6标签(SEQ ID NO:15)具有高度灵敏度的Co2+带电荷的琼脂糖树脂)通过固定金属亲和色谱法(IMAC)纯化His6标记的(“His6”公开为SEQ ID NO:15)LC/E-BoNT/A构建体的SDS-PAGE电泳的照片。
图2B示出随后经受阳离子交换色谱法的汇集的含LC/E-BoNT/A IMAC级分的洗脱曲线中吸光度和传导率对时间。
图3是示出用生物素化的凝血酶处理纯化的LC/E-BoNT/A以产生双链毒素且除去His6(SEQ ID NO:15)标签的SDS-PAGE电泳的照片。符号+和–分别指示用或不用试剂二硫苏糖醇(DTT)处理以减少连接LC/E-LC/A和HC/A链的二硫键。
图4是蛋白质印迹的照片，其中将BoNT/A(上部凝胶)和LC/E-BoNT/A(下部凝胶)的连续稀释液针对其裂解培养的大鼠小脑颗粒神经元(CGN)中的SNARE蛋白SNAP-25的能力进行测定。
图5示出注射LC/E-BoNT/A、BoNT/E或BoNT/A的腓肠肌中肌肉麻痹的持续时间，其中将最大耐受剂量(TDmax)对比天数的时间长度进行绘图。
图6A是蛋白质印迹的照片，其中将LC/E-BoNT/A的连续稀释液与大鼠TGN(三叉神经节神经元)孵育过夜，然后使用抗SNAP-25和抗突触融合蛋白抗体针对LC/E-BoNT/A裂解SNAP-25(主要产生由LC/E产生的26个残基截短的SNAP-25裂解产生)而不裂解突触融合蛋白的能力测定溶解产物。
图6B是LC/E-BoNT/A的剂量反应曲线，其示出通过60mM KCl引发的a)SNAP-25的裂解和b)CGRP释放的抑制或c)大鼠TGN中的辣椒素，以及BoNT/A未能显著降低与BoNT/A一起孵育的TGN中由辣椒素引发的CGRP释放。
图7A是从术前4天至术后约21天进行的用盐水、BoNT/A或LC/E-BoNT/A处理动物、接着将爪置于冷(4℃)板中且测量大鼠从所述板缩回其爪所需的时间的大鼠模型保留神经损伤(SNI)测试中抗伤害性活动持续时间的曲线图。
图7B是从术前4天至术后约21天进行的用盐水、BoNT/A或LC/E-BoNT/A处理动物、接着通过对施加校准的von Frey毛发到后爪的趾面上的敏感性测量诱导的异常性疼痛的大鼠模型保留神经损伤(SNI)测试中抗伤害性活动持续时间的曲线图。
图8A是本发明的双蛋白酶多肽的示意图。这种多肽使两种不同的SNARE蛋白失活：通过LC/B使VAMP失活且通过LC/A使SNAP-25失活。将合成LC/B基因经由接头序列(编码“DI”残基)融合至BoNT/A的5端以产生复合神经毒素LC/B-BoNT/A。后者还包含两个凝血酶识别序列。
图8B说明使用
Superflow树脂(由Clonetech Laboratories,Inc.制造)通过IMAC纯化His6标记的LC/B-BoNT/A的通过考马斯蓝染色的SDS-PAGE凝胶。
图8C在用生物素化的凝血酶处理以产生双链(DC)毒素之后IMAC纯化的LC/B-BoNT/A的SDS-PAGE。符号+和–分别指示用或不用还原剂二硫苏糖醇(DTT)处理。
图8D示出SDS-PAGE凝胶的蛋白质印迹，其中将LC/B-BoNT/A的连续稀释液与大鼠CGN在37℃下孵育24小时。然后使用抗SNAP-25抗体和抗VAMP 2抗体测定溶解产物以监测毒素对两种SNARE蛋白SNAP-25和VAMP 2的裂解。通过其特异性抗体探测且通过LC/B或LC/A未识别的突触融合蛋白1充当内部负载对照。
图8E示出LC/B-BoNT/A的剂量/反应曲线，其示出在较高浓度的LC/B-BoNT/A构建体下SNAP-25(矩形)和VAMP 2(倒三角形)的裂解。
图9是本发明的另一个实施例，其中多SNARE裂解治疗性候选物具有是所有三种主要类型的SNARE蛋白质失活的能力：通过LC/C1使SNAP-25和突触融合蛋白1-3失活且通过LC/D使VAMP1-3失活。DI是LC/D与LC/C1之间的接头。
图10A是从术前4天至术后约21天进行的用盐水、PK(GMP符合的LC/E-BoNT/A)或普瑞巴林处理动物、接着用Von Frey细丝刺激爪且测量大鼠缩回其爪的机械阈值的大鼠模型保留神经损伤(SNI)测试中抗伤害性活动持续时间的曲线图。
图10B是从术前4天至术后约21天进行的用盐水、PK(使用适于GMP符合生产的方法制造的LC/E-BoNT/A)或普瑞巴林处理动物、接着将爪置于冷(4℃)板中且测量大鼠从所述板缩回其爪所需的时间的大鼠模型保留神经损伤(SNI)测试中抗伤害性活动持续时间的曲线图。
图11是从术前4天至术后约36天进行的用盐水或PK(使用适于GMP符合生产的方法制造的LC/E-BoNT/A)处理动物、接着用Von Frey细丝刺激爪且测量大鼠缩回其爪的机械阈值的大鼠模型保留神经损伤(SNI)测试中抗伤害性活动持续时间的曲线图。在术后第10天对一组动物进行第二PK注射。
发明详述
本发明涉及与源自肉毒杆菌神经毒素的治疗性多肽分子相关的方法和组合物。具体地说，所述分子包含至少两个源自不同BoNT血清型的轻链的活性内肽酶结构域。非常优选地，所述内肽酶结构域识别且裂解其底物中的不同氨基酸序列。尤其优选地，所述内肽酶结构域源自两种或更多种BoNT血清型，或BoNT血清型和TeTx LC。
组合来自选定BoNT的重链与至少两个不同的活性梭菌属轻链内肽酶结构域的能力提供具有增强的和耐受特性的工程化的治疗分子。这类治疗剂首先通过设计和产生编码两种不同BoNT血清型的复合物的基因构建体以及展示多重和协同生物活性与治疗应用的重组蛋白的原核表达/纯化来举例说明。
通过这类多内肽酶治疗剂阻断胞外分泌可具有累加活性，如阻断痛觉受体运输至感觉神经元的表面。因此，这类治疗剂不仅抑制可溶性突触因子的胞外分泌，而且可抑制为神经膜内部的蛋白质的运输。
在未在实施例部分中说明的某些治疗剂中，天然存在的结合结构域可被改变以使得治疗剂重新靶向不同或另外的细胞类型。例如，在Aoki等人，美国专利6,776,990中，BoNT的结合区被人缩胆囊素或其类似物置换，从而使毒素(具有仅单一内肽酶)靶向胰腺腺泡细胞。类似地，在2012年10月4日提交的美国专利申请序列号13/644,386中，在某些实例中靶向配体置换天然存在的结合结构域。在这样一个实例中，编码人白细胞介素-1受体拮抗剂(IL-1RA)的基因用于置换天然存在的HC区或其部分，从而靶向分泌细胞因子的细胞。
例证本发明的当前优选的分子是基于使用分子生物学方法用于产生表达包含融合至活性重组BoNT/A的LC/A部分的BoNT/E的LC的蛋白质的核酸构建体的新颖概念。这种独特分子包含LC/E-BoNT/A(在图1中示出)，其结合BoNT/A受体(例如，突触囊泡蛋白2和/或神经节苷酯)，经历受体介导的内吞作用且易位至细胞溶质，其中SNARE蛋白SNAP-25有效的裂解，从而产生神经递质、细胞因子和疼痛肽释放的抑制。“有效裂解”意指其中大多数SNAP-25分子具有足够数目的氨基酸裂解以通过提高Ca2+流量防止胞外分泌阻断的逆转；例如像由通过LC/E裂解SNAP-25引起。
上述构建体优选地被设计成包含位于/A的HC与LC之间的编码特异性氨基酸残基的短序列，所述氨基酸残基由凝血酶蛋白酶选择性地识别和裂解，因此所获得的单链(SC)重组蛋白可通过暴露于凝血酶体外转化成双链(DC)形式。
非常优选地，本发明由经由双氨基酸接头(例如，天冬氨酸-异亮氨酸；DI)连接至BoNT/A的LC/A部分的LC/E例证，从而产生新颖的复合毒素。在涉及使感觉神经元暴露于此构建体的实验中，蛋白酶显示被递送在培养的神经元内，并且连接的LC/E被稳定化，其进而产生长效神经性麻痹像LC/A。
重要地，与LC/A不同，这种长效分子主要产生具有LC/E特征的蛋白水解产物并且阻断由来自大鼠培养的感觉神经元的辣椒素引发的疼痛介体的释放，这是由于/E裂解的SNAP-25不能介导神经递质、细胞因子和疼痛肽释放。此外，这种复合蛋白质证明在减弱神经性疼痛(保留神经损伤诱导的)的大鼠模型中的疼痛行为方面比单独LC/A更有效。
示例性嵌合分子因此提供作为用于治疗慢性疼痛的治疗剂的主要优点：(a)凭借存在于连接的LC/A中的神经末端保留/稳定化基序，正常瞬时作用/E蛋白酶的高度合乎需要和极大延长的寿命；(b)通过/E蛋白酶显著裂解SNAP-25使SNARE复合物不稳定，以及(c)抑制来自感觉神经元的疼痛肽的TRPV1介导的胞外分泌。这些新发现突出了展示协同复合作用的这种专有工程化蛋白的抗伤害性潜力。其相对于第一代天然BoNT的优点已决定性地证明且因此应带来更多改进的治疗剂。
因为天然BoNT仅具有一个蛋白酶结构域，递送额外LC的创新概念—其裂解在不同位置处的相同底物(或另一种底物)—不仅显著增强其抑制特性，而且原始LC/A的额外稳定化影响产生出人意料的协同作用，即相较于BoNT/E大大延长的治疗益处持续时间。
在其他实例中，不同的多内肽酶治疗剂通过使用用于构建LC/E-BoNT/A核酸的技术构建LC/B-BoNT/A核酸构建体来举例说明。在表达由LC/E-BoNT/A开放阅读框编码的多肽且产生凝血酶位点的缺口之后，所得蛋白质裂解SNAP-25和VAMP-2两者。裂解参与突触融合三元复合物的两种SNARE蛋白可导致更有效。
根据本发明的一般概念，提供一种包含梭菌属神经毒素衍生物的组合物，所述梭菌属神经毒素衍生物包含多肽，所述多肽包含：结合结构域、易位结构域、第一内肽酶结构域以及第二内肽酶结构域，其中所述第一内肽酶结构域和所述第二内肽酶结构域各自具有针对SNARE蛋白的选择性蛋白水解活性且识别SNARE蛋白中的不同裂解位点。
还考虑使用这种一般概念组合物的核酸和治疗方法。此外，还考虑一种用于治疗慢性疼痛的包含梭菌属神经毒素衍生物的治疗性组合物，所述梭菌属神经毒素衍生物包含多肽，所述多肽包含：结合结构域、易位结构域、第一内肽酶结构域以及第二内肽酶结构域，其中所述第一内肽酶结构域和所述第二内肽酶结构域各自具有针对SNARE蛋白的选择性蛋白水解活性且识别SNARE蛋白中的不同裂解位点。此外，还考虑包含梭菌属神经毒素衍生物的治疗性组合物用于制造用以治疗慢性疼痛的药剂的用途，所述梭菌属神经毒素衍生物包含多肽，所述多肽包含：结合结构域、易位结构域、第一内肽酶结构域以及第二内肽酶结构域，其中所述第一内肽酶结构域和所述第二内肽酶结构域各自具有针对SNARE蛋白的选择性蛋白水解活性且识别SNARE蛋白中的不同裂解位点。
根据本发明的优选实施方案，提供一种包含梭菌属神经毒素衍生物的组合物，所述梭菌属神经毒素衍生物包含多肽，所述多肽包含：
a)结合结构域，
b)易位结构域，以及
c)源自梭菌属神经毒素BoNT/A亚型的第一内肽酶结构域，以及
d)源自梭菌属神经毒素BoNT/E亚型的第二内肽酶结构域。
根据本发明的另一个优选实施方案，提供一种编码包含梭菌属神经毒素衍生物的多肽的核酸，所述核酸包含从羧基端至氨基端依次编码以下各项的单个开放阅读框：结合结构域、易位结构域、源自梭菌属神经毒素BoNT/A亚型的第一内肽酶结构域以及源自梭菌属神经毒素BoNT/E亚型的第二内肽酶结构域。
根据本发明的另一优选实施方案，提供一种用于治疗慢性疼痛的包含梭菌属神经毒素衍生物的治疗性组合物，所述梭菌属神经毒素衍生物包含多肽，所述多肽包含：结合结构域、易位结构域、源自梭菌属神经毒素BoNT/A亚型的第一内肽酶结构域以及源自梭菌属神经毒素BoNT/E亚型的第二内肽酶结构域。
根据本发明的另一优选实施方案，提供包含梭菌属神经毒素衍生物的治疗性组合物用于制造用以治疗慢性疼痛的药剂的用途，所述梭菌属神经毒素衍生物包含多肽，所述多肽包含：结合结构域、易位结构域、源自梭菌属神经毒素BoNT/A亚型的第一内肽酶结构域以及源自梭菌属神经毒素BoNT/E亚型的第二内肽酶结构域。
实施例
实施例1
将具有针对在大肠杆菌中的增强表达优化的其密码子和编码Lys残基的三个额外核苷酸(AAA)的合成BoNT/A基因克隆至真核表达载体pET29a(+)的Nde I和Sal I位点中以产生pET-29a-BoNT/A。
然后将pET-29a-BoNT/A进一步修饰以便提供受控的特异性缺口和同时除去由pET-29a克隆载体编码的六组氨酸(His6(SEQ ID NO:15))标签的能力。将编码凝血酶裂解位点的核苷酸序列工程化至编码毒素的HC/LC环的核酸区中。这在以下以核酸和氨基酸形式分别作为SEQ ID NO:1和SEQ ID NO:2示出。
修饰的BoNT/A环核苷酸序列(SEQ ID NO:1)及其编码氨基酸序列(SEQ ID NO:2)
此外，另外的凝血酶位点被插入编码所表达蛋白质的HC/A与His6(SEQ ID NO:15)区之间的区域。这在以下以核酸和氨基酸形式分别作为SEQ ID NO:3和SEQ ID NO:4示出。
融合至BoNT/A基因的3’端的核苷酸序列(SEQ ID NO:3)及其编码氨基酸序列(SEQID NO:4)
以上提供的核苷酸序列从左至右分别包含以下区：
a)核苷酸1-3：编码额外Lys的插入的AAA密码子以提供任选的胰蛋白酶裂解位点，以便除去C末端His6(SEQ ID NO:15)；
b)单下划线：Sal I限制性核酸内切酶位点；
c)双下划线：Hind III限制性核酸内切酶位点
d)粗体：凝血酶识别序列；
e)单下划线：Pst I限制性核酸内切酶位点；
f)双下划线：Xho I限制性核酸内切酶位点；
g)核苷酸49-66：编码His6(SEQ ID NO:15)标签的核苷酸区。对比氨基酸序列在相应核苷酸上方展示。箭头指示凝血酶裂解位点，并且星号表示翻译“终止”密码子。
包含上述BoNT/A开放阅读框且包含SEQ ID NO:1和SEQ ID NO:3的此核酸构建体被称为pET29a-BoNT/A-2T。
PCR产物(扩增子)是从编码LC/E蛋白酶(残基1-411)的合成核酸扩增的，并且两个限制位点(Nde I和Eco RV)在扩增期间分别并入在所述核酸扩增子的5’端和3’端。然后将此PCR扩增子通过Nde I和Eco RV消化且克隆至也用Nde I和Eco RV消化的pET29a(+)载体中。所得中间载体构建体被称为pET29a-LC/E。
将BoNT/A-2T的上述完整“单链”开放阅读框BoNT基因区使用pET29a-BoNT/A-2T作为模板用一对引物(噬菌体T7末端反向引物和含有BoNT/A5’编码序列上游的EcoRV限制序列的正向引物)通过PCR进行扩增。将所得PCR扩增子通过EcoRV和Xho I酶消化，纯化且插入Eco RV-和Xho I-裂解的pET29a-LC/E质粒中。此最终构建体被称为pET29a-LC/E-BoNT/A，并且开放核酸阅读框被公开为SEQ ID NO:5，而相应氨基酸序列在本文公开为SEQ ID NO:6。
实施例2
为了表达LC/E-BoNT/A，将序列验证的构建体转化至大肠杆菌菌株BL21(DE3)中，并且使用Studier的自动诱导培养基诱导靶蛋白质的表达(Studier,F.W.,41ProteinExpr.Purif.207(2005))。用固定金属(Co2+)亲和色谱法(IMAC)使用Talon超流树脂实现细菌溶解产物中的His6(SEQ ID NO:15)标记的蛋白质的部分纯化(约60％)。通过大于或等于50mM咪唑洗脱Mr约200kDa的主要蛋白质；这在图2A中示出，其示出SDS-PAGE和凝胶的考马斯蓝染色。凝胶泳道是如下：泳道1：在施加至IMAC柱之前的澄清溶解产物；泳道2：IMAC柱流过级分；泳道3：IMAC柱洗涤级分；泳道4-9，来自IMAC柱的使用咪唑洗脱的级分。
将汇集的IMAC洗脱级分缓冲交换至0.02M磷酸钠缓冲液(pH6.5)中，且然后通过负载至UNO-S1阳离子交换柱上进一步纯化，接着用达150mM NaCl洗涤，且然后用NaCl梯度洗脱；将毒素用等于或大于220mM的NaCl浓度进行洗脱。图2B示出LC/E-BoNT/A单链多肽随时间变化的洗脱曲线(在280nm下的吸光度)，其中NaCl梯度的传导率增加叠加。箭头示出含有LC/E-BoNT/A的吸光度峰的位置。
实施例3
在将洗脱的完整毒素缓冲交换至25mM HEPES/145mM NaCl(pH 7.4)中之后，将纯化的单链(“SC”)蛋白质储存在-80℃下，且取得等分试样以用于SDS-PAGE分析。图3示出纯化的多肽的还原(+)和非还原(-)SDS-PAGE以及蛋白质印迹分析的结果，从而证实这种纯化的蛋白质确实以SC形式表达，如通过以约200kDa的表观分子量迁移的单一条带所揭示。此条带在不存在或存在还原剂的情况下观察到。参见例如图3的考马斯亮蓝染色的凝胶照片的泳道SC(-)和SC(+)。
通过与生物素化的凝血酶(1单位/mg蛋白质)在22℃下孵育3小时来尝试这种SC多肽的缺口；然后通过用链霉亲和素琼脂糖处理样品来除去凝血酶蛋白酶。具有约100KDa表观分子量的条带在还原条件下在SDS-PAGE凝胶上运行的样品中的蛋白质的凝血酶处理之后出现；约200KDa条带在这些条件下未观察到，但存在于在非还原条件下运行的凝胶中，而约100KDa条带在这些后者样品中不存在。参见例如图3的考马斯亮蓝染色的凝胶照片的泳道DC(-)和DC(+)。
约100KDa条带据信表示LC/E-LC/A和HC/A链，其具有类似大小。此条带中的多肽的身份通过使用针对假定单链多肽LC/E和BoNT/A中的每种特异性的抗体在缺口的和未缺口的LC/E-BoNT/A上运行的SDS-PAGE凝胶的蛋白质印迹得以证实。
如图3中所示，在还原剂不存在下缺口的样品基序以约200kDa迁移，从而指示LC/E-LC/A与HC/A之间的链间二硫键形成，且在所有样品中存留，如使用抗-LC/E或抗-BoNT/A抗体在蛋白质印迹标记的(-)和显影的泳道中所示。因此，在还原和非还原条件下的SDS-PAGE和蛋白质印迹突出在无复合毒素的降解的情况下发生的环区域处的特异性缺口。未缺口的和缺口的蛋白质的迁移率的略微差异是由于凝血酶处理的样品中His6(SEQ ID NO:15)标签的除去；这使用针对此标签的特异性抗体得以证实。参见图3的使用抗-His6(SEQID NO:15)抗体的蛋白质印迹，其中His6(SEQ ID NO:15)标签不可检测。此实验因此还证明凝血酶蛋白酶可同时使HC与第一LC之间的二硫键的连接的半胱氨酸残基之间的毒素缺口，且除去His6(SEQ ID NO:15)。
实施例4
将重组产生的LC/E-BoNT/A和BoNT/A各自以0.01pM至1000pM毒素的10倍连续稀释浓度与培养的大鼠小脑颗粒神经元(CGN)孵育过夜。将这些细胞从7–8天龄大鼠的小脑解离并且以约1×106/ml悬浮于3份的基础伊格尔培养基和1份的40mM HEPES-NaOH(pH7.3)、78.4mM KCl、37.6mM D-葡萄糖、2.8mM CaCl2、1.6mM MgSO4以及1.0mM NaH2PO4以及1x N2补充物、1mM L-谷氨酰胺、60单位/ml青霉素、60μg/ml链霉素以及2％(v/v)马透析血清中。将此细胞悬浮液的等分部分(1ml)添加至16-mm-直径聚-D-赖氨酸涂覆的孔(即24–格式)中的每个，并且在5％(v/v)CO2中培养20–24小时之后添加胞嘧啶-β-D-阿拉伯呋喃糖苷水解酶(40μM)；通过每10天用相同新鲜制备的培养基置换来维持神经元。在规定的情况下，将所述神经元暴露于培养基中的BoNT/A或LC/E-BoNT/A(灭菌的0.2-μm过滤器)持续24小时。
在与BoNT/A或LC/E-BoNT/A蛋白质孵育24小时之后，然后收获细胞且使用识别完整SNAP-25的抗-SNAP-25抗体以及LC/A-裂解的SNAP-25和LC/E-裂解的SNAP-25使其经受SDS-PAGE和蛋白质印迹。SNARE蛋白质突触融合蛋白1用作阳性内部负载对照。
使用抗-SNAP-25抗体进行蛋白质印迹。如可在图4中观察到，在裂解完整SNAP-25方面LC/E-BoNT/A几乎与BoNT/A活性一样，其中在每种情况下显著裂解在高于1pM的毒素浓度下发生。值得注意的，如可观察到，当使用低于约1pM的毒素时，用LC/E-BoNT/A处理CGN还得到LC/A裂解产物。当LC/E-BoNT/A毒素的浓度升高至约0.01nM以上时，此裂解产物(“SNAP-25A”)似乎通过共同递送LC/E蛋白酶基本上进一步裂解成LC/E的裂解产物(“SNAP-25E”)(图4)。这些结果表明BoNT/A重链易位结构域能够将共价连接的LC/A和LC/E蛋白酶递送至CGN的细胞溶质，其中所述蛋白酶保持活性以裂解SNAP-25，从而使SNARE蛋白全部或部分失活。
实施例5
LC/E-BoNT/A的特异性神经毒性通过以据此以引用的方式并入的Maisey,E.A.,等人,177EUR.J.BIOCHEM.683–691(1988)中描述的方式腹膜内注射至小鼠中来测定。在4天内杀死50％小鼠的毒素的最低量被定义为一个最小致死剂量(mLD50)。毒素的特异性活性可表示为mLD50单位的数目/mg毒素。
LC/E-BoNT/A制剂的mLD50据观察为0.7x 108。这种特异性活性介于针对重组BoNT/E所观察到的特异性活性(0.4x 108)与针对BoNT/A所观察到的特异性活性(2x 108)之间。使用例如据此以引用的方式并入的Aoki,K.R.,39 TOXICON 1815-1820(2001)中描述的小鼠趾外展评分(DAS)测定来评定体外神经性麻痹作用的持续时间。
将重组LC/E-BoNT/A以0.5mLD50单位的剂量注射至小鼠腓肠肌中，其是可施用至实验动物而不产生全身症状的最大耐受剂量。此剂量的LC/E-BONT/A引起持续约27天的麻痹；类似于由6单位的天然BoNT/A诱导的作用；参见图5。相较于BoNT/E，LC/E-BONT/A的长效作用似乎是由于融合蛋白中的LC/A部分稳定化连接的LC/E部分的能力；单独BoNT/E得到比其他毒素更短的麻痹；参见图5中BoNT/E对LC/E-BoNT/A的比较。
实施例6
使用三叉神经神经节神经元(TGN)检查LC/E-BONT/A蛋白的抗伤害性潜力。这些细胞是用于此实验的良好模型，这是由于由于其参与疼痛传播和培养中的这些细胞提供用于研究通过不同刺激物触发的疼痛肽(CGRP，SP)的释放的良好模型；参见例如，Bacccaglini和Hogan,80PROC NATL ACAD SCI U.S.A.594-598(1983)。从红辣椒分离的辣椒素活化TRPV1，其主要在感觉神经元的C-纤维上表达。因此，复合毒素阻断由其激动剂辣椒素引发的CGRP的释放的能力应是其抑制活性的良好指示。
BoNT/A仅从SNARE蛋白SNAP-25的C末端除去9个氨基酸残基(“/A-截短的”SNAP-25裂解产物)，并且不会影响由TGN中的辣椒素引发的CGRP胞外分泌。相比之下，通过LC/E蛋白酶除去17个另外残基(产生“/E-截短的”SNAP-25裂解产物)阻断这种辣椒素刺激的CGRP释放；参见例如据此以引用的方式并入的Meng等人,29J NEUROSCI 4981-4992(2009)。
因为长效毒素LC/E-BoNT/A的主要SNAP-25裂解产物是“/E-截短的”SNAP-25裂解产物，而不是CGN中的“/A-截短的”SNAP-25裂解产物(残基图4)，所以预期LC/E-BoNT/A将阻断CGRP疼痛肽的释放。
简言之，在用腹膜内注射Dolethal(50mg/kg体重)深度麻醉之后从出生后第5天的Wistar大鼠解剖TGN。将所述组织置于冰冷的L15培养基中，且然后在冰冷的无菌CMF-HBSS中洗涤两次，之后在170g下离心1分钟。在将所述组织切成小片且通过预先涂覆有L15培养基的10-ml Falcon移液管之后，将所述组织在振荡下在37℃下在含有2.4U/ml分散酶II和1mg/ml胶原酶I的不含钙和镁的Hanks平衡盐溶液(CMF-HBSS)的1:1混合物中孵育30分钟。然后将悬浮液温和研磨通过预先涂覆L15培养基的10-ml Falcon移液管直到浑浊，之后添加1mg/ml DNA酶I持续15分钟。
在170g下离心5分钟之后，将细胞沉淀悬浮且在培养基[含有10％(v/v)热灭活的胎牛血清(FBS)、100IU/ml青霉素和100μg/ml链霉素的Ham's F12溶液(Sigma-Aldrich,St.Louis,MO)]中洗涤三次。将细胞接种到补充有神经生长因子(NGF)(50ng/ml)的F12培养基中的预先涂覆有聚-L-赖氨酸(0.1mg/ml)和层粘连蛋白(20μg/ml)的24孔板上并且在37℃下维持在CO2孵育箱中。在24小时之后(且其后的每天)，用含有抗有丝分裂剂胞嘧啶-β-D-阿拉伯呋喃糖苷(10μM)的新鲜培养基替换培养上清液。
在37℃下在用LC/E-BoNT/A的连续稀释液过夜孵育大鼠TGN之后，通过SDS-PAGE、接着使用能够结合完整以及A-截短的和E-截短的产物的抗-SNAP-25抗体进行蛋白质印迹来监测裂解程度。
如图6A中所示，LC/E-BoNT/A得到SNAP-25的剂量依赖性裂解，具有主要“/E-截短的”SNAP-25裂解产物。
此外，如所预期，复合毒素以剂量依赖性方式通过由60mM KCl或辣椒素引发的TGN阻断CGRP的释放(图6B)。通过用HBS(用NaCl等渗平衡)中的60mM KCl处理刺激Ca2+-依赖性CGRP释放。为了用辣椒素刺激，分别在乙醇或二甲亚砜中制备储备液(1mM)并且在BR-HBS中稀释至所需浓度。在所有情况下，将媒介物的最终浓度保持在0.1％；当测量基础流出时这也包括于BR-HBS中。
将细胞用K+或辣椒素刺激并且监测CGRP的释放持续30分钟。为了测定所释放的CGRP的量，将0.1ml的样品添加至涂覆有针对CGRP的单克隆抗体的96孔板，并且按照试剂盒的说明书进行酶免疫测定。
所述结果表明LC/E-BoNT/A多肽抑制从大致密核心囊泡释放疼痛肽的能力，而用BoNT/A类似处理细胞在活化TRPV1阳离子通道时未能抑制CGRP的释放。参见图6B。
实施例7
在持久性外周神经性疼痛，即保留神经损伤(SNI)测定的大鼠模型中评价LC/E-BoNT/A的抗伤害性活性。此模型是基于以下观察结果：实质上所有神经性疼痛(除了由通过截肢的完全损害引起的幻肢痛的特殊情况)由部分神经损伤造成。这些神经性疼痛包括糖尿病性神经病变、治疗后神经痛、中毒性神经病、压迫性神经病和创伤，并且特征在于自发刺痛、灼痛和休克样疼痛以及痛觉过敏，包括触觉异常痛敏、针刺痛觉过敏和痛觉过敏。
SNI手术在麻醉的成年大鼠(如Spague-Dawley大鼠)上进行，并且涉及坐骨神经的末端远端分支中的两个(胫骨和常见腓神经)的连接和横断，其流而下第三分支(腓肠神经)完整；参见以引用的方式并入本文的Decosterd,I.&Woolf,C.J.,87PAIN 580-587(2000)。此模型具有技术上易于进行且经受所产生的损失程度的最小变化的优点。
将所述毒素注射至末端后肢的趾(掌)侧。LC/E-BoNT/A和BoNT/A(不影响运动功能)的最大趾内剂量据发现分别是75和15小鼠LD50单位/kg。相较于假对照小鼠(其经受坐骨神经的暴露而无任何损伤)，具有SNI的大鼠显示长效神经性疼痛样行为。
神经性疼痛的两个模型是冷异常性疼痛和机械异常性疼痛。在第一测试中，冷超敏性的那些，将手术的爪与在4℃下的冷板相接触，并且在不同时间点记录爪缩回持续时间，如图7A中所示。作为冷超敏性调节的测量，处理后值被表示为处理前值的百分比。
如图7A所示，在处理之后冷超敏性通过LC/E-BoNT/A有效降低持续2周(相较于盐水处理的P<0.001)，特别是持续前10天。LC/E-BoNT/A的抗伤害性作用显著大于由BoNT/A诱导的抗伤害性作用(在注射后第5天和第7天P<0.05)。无论给予毒素还是盐水，在假对照中未观察到冷诱导的异常性疼痛。
在第二测试中，通过将动物置于升高的丝栅上且用一组von Frey毛发刺激处理的爪的趾表面以测定在检测到疼痛(由爪的敏锐缩回指示)之前能够耐受的感觉刺激的量来测量机械异常性疼痛。将Von Frey毛发(或单丝)校准以提供大约实际力的对数尺度，以及感知强度的线性尺度。机械阈值表示为引起爪缩回所需的平均最小克的力的50％。
如在图7B中所示，机械阈值通过神经损伤显著降低(将假对照与仅给予盐水的SNI大鼠相比较)。令人鼓舞地，LC/E-BoNT/A开始在注射之后2天内逆转这种机械超敏性，并且在处理后7天观察到镇痛作用的最大值。在注射之后3至10天记录比盐水处理的大鼠显著更高的机械阈值(对比盐水P<0.001)。此外，即使用BoNT/A处理诱导损伤后机械阈值的适度增加，但LC/E-BoNT/A据发现显著更有效(P<0.05)。
当施用至假动物时，毒素和盐水均不影响通过冷和机械刺激触发的疼痛行为(图7A、B)。LC/E-BoNT/A证明在降低冷缩回持续时间方面比BoNT/A更有效(图7A)并且尤其增加机械缩回阈值(图7B)。重要地，将LC/E-BoNT/A注射至对冷和机械刺激具有SNI标准化灵敏度的大鼠中在第3天和第7天至类似于所有假对照的那些的值。总之，LC/E-BoNT/A诱导在慢性神经性疼痛的大鼠模型中诱导强效抗伤害性作用。
实施例8
以下提供的复合合成神经毒素开放阅读框LC/E-BoNT/A基因序列及其编码氨基酸(分别SEQ ID NO:5和6)分布包含以下区(相对于核苷酸氨基鉴定的)：残基1-1233，LC/E；残基1240-5130，BoNT/A。包含核苷酸(1234-1239)的DNA序列作为接头引入且确保正确阅读框。对比氨基酸序列在相应核苷酸上方展示。将凝血酶蛋白酶识别序列插入LC/A与HN/A之间的环中；类似地，将另一个凝血酶位点工程化为具有BoNT/A基因的羧基位点的裂解序列；这些允许同时缺口和C-末端His6(SEQ ID NO:15)的去除。
复合神经毒素基因(LC/E-BoNT/A)序列及其编码氨基酸(SEQ ID NO:5和6)
本发明的此实施例解决了现有技术提出的至少两个主要问题。首先，它提供长效BoNT嵌合体，其具有扩大的抗伤害性治疗潜力。第二，它提供对于慢性疼痛治疗具有独特潜力的长效BoNT来源的治疗剂。
管理慢性疼痛对现代医疗保健提出主要挑战，因为患者代表超过20％的成人群体。相当大部分的群体对通常使用的止痛药无反应。另外，与处方鸦片制剂的挥霍相关的药物依赖和滥用的增加和在大多数情况下针对疼痛原始开处方的许多麻醉剂的短半衰期使类鸦片制剂和非类固醇抗炎药物的使用成为无吸引力的选择。
BoNT/A复合物的治疗性用途证明有益于一些而不是所有偏头痛患者，这是由于假定疼痛途径的假定干扰。BoNT/A未能减弱由由疼痛肽或原位C-纤维的TRPV1活化引发的神经元方便并且不能阻断来自培养的神经元的CGRP释放突出有必要开发长效且更广泛有效的形式。
BoNT/A和BoNT/E的BoNT-衍生物嵌合体成功进入TGN，并且得到/E-样SNAP-25裂解产物，其进而抑制疼痛介体的释放；然而，其短作用持续时间限制临床应用。
本发明将不同血清型的至少两种BoNT的结构域组合在一起以产生新颖治疗剂。这种创新策略可用于产生其他嵌合多链治疗剂，包括包含来自不同BoNT血清型的多个LC以产生具有所需特性的治疗剂的构建体；例如多-SNARE-裂解毒素(裂解不同的SNARE蛋白质)治疗剂，其可例如通过将LC/C1连接至BoNT/A而不是LC/E来构建。
实施例9
在另一个实施例中，以基本上类似于上述的方式通过用合成LC/B基因取代LC/E-BoNT/A核酸中的LC/E基因以产生编码作为单一开放阅读框的LC/B-BoNT/A的最终质粒来产生多内肽酶构建体。
为了表达LC/B-BoNT/A，将序列验证的构建体转化至大肠杆菌菌株BL21(DE3)中，并且如先前针对LC/E-BoNT/A所描述表达所得蛋白质。部分纯化来自澄清的细菌溶解产物的His6-标记的毒素使用IMAC亲和分离步骤使用Talon超流树脂实现。通过≥150mM咪唑洗脱Mr约200k的主要蛋白质；这在图8B中示出，其示出在还原条件下的SDS-PAGE和凝胶的考马斯蓝染色。凝胶泳道是如下：泳道1：在施加至IMAC柱之前的澄清溶解产物；2：IMAC柱流过级分；3：IMAC柱洗涤级分；4-8，使用咪唑洗脱的级分。
将汇集的IMAC洗脱液缓冲交换至25mM HEPES/145mM NaCl(pH 7.4)中并且通过SDS-PAGE分析等分部分。图8C示出纯化的蛋白质的SDS-PAGE，其中等分部分在还原(+)和非还原(-)下电泳。电泳证实蛋白质确实以单链(“SC”)形式表达，如由异约200kDa的表观分子量迁移的主要条带揭示。此条带在不存在或存在还原剂的情况下观察到。参见例如图8C中的考马斯亮蓝染色的凝胶的泳道SC(-)和SC(+)。
通过与生物素化的凝血酶(1单位/mg毒素)在22℃下孵育3小时来实现这种单链蛋白质的缺口(和His6标签的除去)；然后通过用固定在琼脂糖上的链霉亲和素处理样品来除去凝血酶蛋白酶。具有约100K表观分子量的两个条带(未通过SDS-PAGE良好解析，这是由于两个蛋白质链的迁移率的相似性)在于还原条件下在SDS-PAGE凝胶上运行的样品中蛋白质的凝血酶处理之后出现；约200K条带未在这些条件下观察到，但存在于在非还原条件下运行的凝胶中，而约100KDa条带在这些后者样品中不存在。参见例如图8C中的考马斯亮蓝染色的凝胶的泳道DC(-)和DC(+)。约100K条带据信表示LC/B-LC/A和HC/A链，其具有大小的较小差异。
将大鼠培养的小脑颗粒神经元(CGN)与凝血酶处理的LC/B-BoNT/A以0.32pM至5000pM的5倍连续稀释浓度孵育。在37℃下在与LC/B-BoNT/A孵育24小时之后，然后守活细胞且使其经受SDS-PAGE和蛋白质印迹，使用a)识别完整SNAP-25用LC/A处理的大裂解产物的抗-SNAP-25抗体和b)拾取完整型式的抗-VAMP2抗体。抗突触融合蛋白1抗体用于检测SNARE蛋白突触融合蛋白1，其用作阳性内部负载对照。来自多个印迹的代表性蛋白质印迹(图8D)和定量数据(图8E)表明LC/B-BoNT/A裂解SNAP-25以及VAMP2；然而，VAMP2在较高浓度的LC/B-BoNT/A下有效裂解。虽然不希望受理论约束，但这一结果可能起因于将降低VAMP裂解的BoNT/A的LC[Fernández-Salas等人,Proc.Natt.Acad.Sci.USA.2004,101(9):3208-3213]。
实施例10
如由来自LC/E-BoNT/A(识别同一底物的两个不同序列的两种活性蛋白酶)和LC/B-BoNT/A(裂解两种不同底物的两种蛋白酶)的阳性功能结果所说明，且鉴于本专利申请的公开内容，本领域的技术人员将意识到本发明的另外实施例可涉及用于通过组合用于抑制来自不同神经类型(例如感觉神经元和交感神经元)的疼痛肽、细胞因子和神经递质的释放的不同梭菌属神经毒素或梭菌属神经毒素亚型来产生各种其他多内肽酶治疗剂的组合物和方法。此外，多蛋白酶毒素的作用活性将间接阻断细胞因子释放细胞的这类介体的活性。
例如，使所有三种SNARE蛋白质失活的单一治疗剂通过将BoNT/D的轻链(LC/D)经由接头重组融合至BoNT/C1的N末端来产生(残基图9)。简言之，将编码LC/D内肽酶的核酸“框内”插入LC/E-BoNT/A中以置换LC/E。编码LC/D的合成基因被设计为具有针对在大肠杆菌中最佳表达优化的密码子。所得质粒编码包含LC/D-BoNT/A的中间体蛋白质。
随后，编码BoNT/C1的合成基因(像BoNT/A构建体，在其环区域中具有凝血酶裂解位点)用于置换LC/D-BoNT/A中的BoNT/A基因以产生包含LC/D-BoNT/C1开放阅读框的最终核酸构建体。所表达的纯化的和缺口的LC/D-BoNT/C1治疗剂将具有通过用LC/D裂解使VAMP1-3失活的能力；LC/C1蛋白酶将裂解突触融合蛋白1-3和SNAP-25。这种构建体将适合用于治疗慢性炎性和神经性疼痛。
实施例11
60岁男性在左髋中具有严重慢性关节疼痛，并且行走困难。在检查之后，患者被诊断为患有髋臼股(髋)关节的类风湿性关节炎。
通过直接注射至股骨神经节和坐骨神经节中来向所述患者施用有效量的梭菌属神经毒素衍生物LC/E/BoNT/A。如上所述制备基因构建体且在其表达之后使用His6标签(SEQ ID NO:15)亲和纯化梭菌属毒素衍生物，接着凝血酶缺口且在使用之前离子交换色谱法。
在48小时内，存在疼痛程度和剧烈的显著改善，并且在一周内患者能够不费力的行走。
实施例12
用于人使用的足够量的梭菌属神经毒素衍生物LC/E/BoNT/A的计划最终需求使用于表达和纯化与在良好生产规范(GMP符合的)设备中生产相容的LC/E-BoNT/A蛋白质的生产/纯化平台成为必要。LC/E-BoNT/A蛋白质的按比例扩大的生产和纯化实质上如上针对工作台规模实验所述进行。此过程产生在SDS-PAGE中具有预期表观分子量(约200kDa)的纯活化产物。在还原链间二硫键之后，HC链和LC/E-LC/A链在还原SDS PAGE凝胶上共迁移，各自具有约100kDa的表观分子量；用考马斯亮蓝染色揭示与图3中所示的迁移图案基本上相同的迁移图案。使用适于GMP符合生产的方法制造的LC/E-BoNT/A被称为“PK”。
用于裂解SNAP-25的GMP PK蛋白的活性及其在小鼠中的特异性神经毒性匹配在工作台规模下产生的相同蛋白质的活性和特异性神经毒性。类似地，PK的抗伤害性潜力通过其结合且进入感觉神经元的能力得以证明，从而主要产生LC/E-截短的SNAP-25且抑制去极化或辣椒素刺激的CGRP释放，如通过用PK材料重复实施例6的实验并且获得与图6A和6B中所示的那些基本上相同的结果所示。
最重要地，这种有前景的PK蛋白向在工作台规模下产生的LC/E-BoNT/A蛋白还证明体内同等稳健抗伤害。在慢性疼痛的保留神经损伤(SNI)模型(参见例如实施例7和图7A和7B)将PK单次注射至大鼠的一个后爪中不会影响运动活性(如在旋转棒上所定量)或诱导任何可检测的副作用，但在14天的延长时间段内减轻对假组的对照水平的机械超敏性。此外，在SNI模型中升高水平的冷异常性疼痛也类似地减弱，如通过缩回持续时间的显著减少所示。将盐水媒介物注射至假手术动物不会改变在例如图7A和7B中测量的两个伤害性参数的基线水平。PK蛋白令人信服地减轻升高水平的疼痛。
这些发现证明是从多组广泛动物实验可再现的并且突出PK用于逆转由于严重神经损伤所致的剧烈疼痛的体内治疗功效，并且揭示单独BoNT/A用于治疗疼痛、特别是慢性疼痛的不适当。
实施例13
这种新颖GMP-样抗伤害性的高效率进一步通过在涉及每日全身(I.P.)施用10mg/Kg普瑞巴林的单次注射(75U/Kg)PK的SNI模型中评定来证明，普瑞巴林是在临床上用作神经性疼痛的一线治疗、还已知施加显著不良反应且在一定比例的患者中具有有限镇痛作用的镇痛药物。
再次使用大鼠中慢性疼痛的保留神经损伤(SNI)和冷异常性疼痛模型以及如在先前段落中相同剂量的活性剂，单次足底注射PK产生比每日普瑞巴林的益处持续时间长得多的益处持续时间，与PK相比，普瑞巴林不能显著实现机械超敏性的逆转(图10A)并且诱导对冷的升高反应性的更适度减弱(图10B)。PK的第二注射延长其在机械敏感性(图11)和冷异常性疼痛(未图示)方面的强效镇痛作用，从而产生在初始治疗之后持续超过25天的显著高于对照基线的疼痛缓解。
本发明不限于本文所述的实施方案，而是可在不脱离本发明的范围的情况下修正或修改。
现将通过下文以权利要求格式提出的以下组的实施方案描述本发明。
1)一种组合物，其包含梭菌属神经毒素衍生物，所述梭菌属神经毒素衍生物包含多肽，所述多肽包含：结合结构域、易位结构域、第一内肽酶结构域以及第二内肽酶结构域，其中所述第一内肽酶结构域和所述第二内肽酶结构域各自具有针对SNARE蛋白的选择性蛋白水解活性且识别SNARE蛋白中的不同裂解位点。
2)如权利要求1所述的组合物，其中所述结合结构域、所述易位结构域、所述第一内肽酶结构域以及所述第二内肽酶结构域包含在单一多肽链中。
3)如权利要求2所述的组合物，其中所述多肽还包含选择性内肽酶裂解位点，所述选择性内肽酶裂解位点位于包含所述结合结构域和所述易位结构域的第一区域与包含所述第一内肽酶结构域和所述第二内肽酶结构域的第二区域之间。
4)如权利要求1所述的组合物，其中所述结合结构域、所述易位结构域、所述第一内肽酶结构域以及所述第二内肽酶结构域包含在多于一个多肽链中。
5)如权利要求4所述的组合物，其中至少两个所述多肽链通过二硫键连接。
6)如权利要求1所述的组合物，其包含第一多肽链，所述第一多肽链包含所述结合结构域和所述易位结构域；以及第二多肽链，所述第二多肽链包含所述第一内肽酶结构域和所述第二内肽酶结构域。
7)如权利要求5所述的组合物，其包含第一多肽链，所述第一多肽链包含所述结合结构域和所述易位结构域；以及第二多肽链，所述第二多肽链包含所述第一内肽酶结构域和所述第二内肽酶结构域。
8)如权利要求1所述的组合物，其中所述结合结构域和所述易位结构域源自第一梭菌属神经毒素或梭菌属神经毒素亚型，并且其中所述第一内肽酶结构域和所述第二内肽酶结构域中的至少一个源自第二梭菌属神经毒素或梭菌属神经毒素亚型。
9)如权利要求8所述的组合物，其中所述结合结构域、所述易位结构域以及所述第一内肽酶结构域和所述第二内肽酶结构域中的至少一个源自第一梭菌属神经毒素或梭菌属神经毒素亚型。
10)如权利要求9所述的组合物，其中所述结合结构域、所述易位结构域和所述第一内肽酶结构域源自第一梭菌属神经毒素或梭菌属神经毒素亚型，并且所述第二内肽酶结构域源自第二梭菌属神经毒素或梭菌属神经毒素亚型。
11)如权利要求10所述的组合物，其中所述第一梭菌属神经毒素或梭菌属神经毒素亚型是BoNT/A，并且所述第二梭菌属神经毒素或梭菌属神经毒素亚型是BoNT/E。
12)如权利要求11所述的组合物，其中所述第一梭菌属神经毒素或梭菌属神经毒素亚型是BoNT/A，并且所述第二梭菌属神经毒素或梭菌属神经毒素亚型是BoNT/C1。
13)如权利要求11所述的组合物，其包含第一多肽链，所述第一多肽链包含所述结合结构域和所述易位结构域；以及第二多肽链，所述第二多肽链包含所述第一内肽酶结构域和所述第二内肽酶结构域。
14)如权利要求13所述的组合物，其中所述第一多肽链和所述第二多肽链通过二硫键连接。
15)如权利要求11所述的组合物，其中所述结合结构域、所述易位结构域、所述第一内肽酶结构域以及所述第二多肽链全部包含在单一多肽链中。
16)如权利要求11所述的组合物，其包含第一氨基酸序列，所述第一氨基酸序列包含位于所述易位结构域与所述第一内肽酶结构域之间的第一蛋白酶裂解位点。
17)如权利要求11所述的组合物，其还包含：
a)聚组氨酸氨基酸序列，其位于所述结合结构域的羧基端侧上或所述第二内肽酶结构域的氨基端处；
b)第一氨基酸序列，其包含位于所述易位结构域与所述第一内肽酶结构域之间的第一蛋白酶裂解位点；以及
c)第二氨基酸序列，其包含位于所述第二内肽酶结构域与所述聚组氨酸氨基酸序列之间或所述结合结构域与所述聚组氨酸氨基酸序列之间的第二蛋白酶裂解位点。
18)一种编码包含梭菌属神经毒素衍生物的多肽的核酸，所述核酸包含从羧基端至氨基端依次编码以下各项的单个开放阅读框：结合结构域、易位结构域、第一内肽酶结构域以及第二内肽酶结构域，其中所述第一内肽酶结构域和所述第二内肽酶结构域各自具有针对SNARE蛋白的选择性蛋白水解活性且识别SNARE蛋白中的不同裂解位点。
19)如权利要求18所述的核酸，其中编码所述结合结构域、所述易位结构域、所述第一内肽酶结构域以及所述第二内肽酶结构域中的每个的密码子针对在选自由以下各项组成的组的细胞类型中表达而进行优化：细菌细胞、哺乳动物细胞、酵母细胞以及昆虫细胞。
20)如权利要求19所述的核酸，其中所述密码子针对在大肠杆菌细菌细胞中表达而进行优化。
21)如权利要求18所述的核酸，其中至少两个选自由所述结合结构域、所述易位结构域、所述第一内肽酶结构域以及所述第二内肽酶结构域组成的组的结构域由源自选自由以下组成的组的不同梭菌属神经毒素或梭菌属神经毒素亚型的核酸序列编码：BoNT/A、BoNT/B、BoNT/C1、BoNT/D、BoNT/E、BoNT/F、BoNT/G以及TeTX。
22)如权利要求21所述的核酸，其中所述第一内肽酶结构域和所述第二内肽酶结构域由源自选自由以下组成的组的不同梭菌属神经毒素或梭菌属神经毒素亚型的核酸序列编码：BoNT/A、BoNT/B、BoNT/C1、BoNT/D、BoNT/E、BoNT/F、BoNT/G以及TeTX。
23)如权利要求22所述的核酸，其中所述第一内肽酶结构域由源自BoNT/A的核酸序列编码，并且所述第二内肽酶结构域由源自BoNT/C1的核酸序列编码。
24)如权利要求22所述的核酸，其中所述第一内肽酶结构域由源自BoNT/A的核酸序列编码，并且所述第二内肽酶结构域由源自BoNT/E的核酸序列编码。
25)如权利要求24所述的核酸，其中所述开放阅读框编码核苷酸序列(所述核苷酸序列编码内肽酶结合结构域)与终止密码子之间的至少六个组氨酸残基。
26)一种治疗慢性疼痛的方法，所述方法包括施用包含梭菌属神经毒素衍生物的治疗性组合物，所述梭菌属神经毒素衍生物包含多肽，所述多肽包含：结合结构域、易位结构域、第一内肽酶结构域以及第二内肽酶结构域，其中所述第一内肽酶结构域和所述第二内肽酶结构域各自具有针对SNARE蛋白的选择性蛋白水解活性且识别SNARE蛋白中的不同裂解位点。
27)如权利要求26所述的方法，其中所述慢性疼痛选自由以下组成的组：炎性伤害性疼痛和神经性疼痛。
28)如权利要求27所述的方法，其中所述慢性疼痛是神经性疼痛。
29)如权利要求28所述的方法，其中所述神经性疼痛选自由以下组成的组：癌症疼痛、术后疼痛、神经性疼痛、异常性疼痛、疱疹后神经痛、肠易激综合症以及其他内脏痛、骨痛、周围神经病变、循环系统附属疼痛以及头痛疼痛。
30)如权利要求27所述的方法，其中所述慢性疼痛是炎性伤害性疼痛。
31)如权利要求27所述的方法，其中所述慢性疼痛是关节炎疼痛。
32)如权利要求26所述的方法，其中所述治疗性组合物的所述结合结构域和所述易位结构域源自第一梭菌属神经毒素或梭菌属神经毒素亚型，并且其中所述组合物的所述第一内肽酶结构域和所述第二内肽酶结构域中的至少一个源自第二梭菌属神经毒素或梭菌属神经毒素亚型。
尽管已参考所公开的实施方案描述了本发明的各个方面，但本领域的技术人员将显而易见，所公开的特定实施例仅说明所述方面且决不限制本发明。可在不脱离本发明的精神的情况下进行各种修改。本文描述的每个和各个特征以及这类特征的每个和各个组合包括在本发明的范围内，条件是包括在所述组合中的特征不是互相对立的。此外，本发明的任何组合物或装置应理解为包括权利要求的一个或多个要素、基本上由权利要求的一个或多个要素组成或由权利要求的一个或多个要素组成，并且此外未明确包括作为权利要求的要素的每个和各个要素应视为在本文具有明确排除对所述权利要求的负面限制的基础。
在本说明书中引用的任何和所有专利、公布、专利申请以及通过登录号提及的核苷酸和/或氨基酸序列据此以引用的方式作为本说明书的一部分整体并入。
序列表
<110> 都柏林城市大学
<120> 用于慢性疼痛的多蛋白酶治疗剂
<130> A-05047
<140>
<141>
<150> 61/920,053
<151> 2013-12-23
<160> 15
<170> PatentIn 3.5版
<210> 1
<211> 78
<212> DNA
<213> 人工序列
<220>
<223> 人工序列的描述：合成寡核苷酸
<220>
<221> CDS
<222> (1)..(78)
<400> 1
tgt gtc cgc ggt att atc acc agc aaa acc aaa tcc ttg gtg ccc cgc 48
Cys Val Arg Gly Ile Ile Thr Ser Lys Thr Lys Ser Leu Val Pro Arg
1 5 10 15
ggc tct aac aag gcg ctc aat gat tta tgc 78
Gly Ser Asn Lys Ala Leu Asn Asp Leu Cys
20 25
<210> 2
<211> 26
<212> PRT
<213> 人工序列
<220>
<223> 人工序列的描述：合成肽
<400> 2
Cys Val Arg Gly Ile Ile Thr Ser Lys Thr Lys Ser Leu Val Pro Arg
1 5 10 15
Gly Ser Asn Lys Ala Leu Asn Asp Leu Cys
20 25
<210> 3
<211> 69
<212> DNA
<213> 人工序列
<220>
<223> 人工序列的描述：合成寡核苷酸
<220>
<221> CDS
<222> (1)..(66)
<400> 3
aaa gtc gac aag ctt ctg gta ccg cgc ggc agc aaa ctg cag ctc gag 48
Lys Val Asp Lys Leu Leu Val Pro Arg Gly Ser Lys Leu Gln Leu Glu
1 5 10 15
cac cac cac cac cac cac tga 69
His His His His His His
20
<210> 4
<211> 22
<212> PRT
<213> 人工序列
<220>
<223> 人工序列的描述：合成肽
<400> 4
Lys Val Asp Lys Leu Leu Val Pro Arg Gly Ser Lys Leu Gln Leu Glu
1 5 10 15
His His His His His His
20
<210> 5
<211> 5199
<212> DNA
<213> 人工序列
<220>
<223> 人工序列的描述：合成多核苷酸
<220>
<221> CDS
<222> (1)..(5196)
<400> 5
atg cct aaa atc aat tcg ttc aac tat aat gac ccg gtt aac gat cgc 48
Met Pro Lys Ile Asn Ser Phe Asn Tyr Asn Asp Pro Val Asn Asp Arg
1 5 10 15
acg atc ctg tat atc aag cca ggt gga tgt caa gaa ttt tat aaa tca 96
Thr Ile Leu Tyr Ile Lys Pro Gly Gly Cys Gln Glu Phe Tyr Lys Ser
20 25 30
ttc aac atc atg aaa aat att tgg att atc ccg gaa cgc aac gtg atc 144
Phe Asn Ile Met Lys Asn Ile Trp Ile Ile Pro Glu Arg Asn Val Ile
35 40 45
ggc acg acg cct caa gat ttt cac ccg ccg acc tcc ctg aaa aat ggc 192
Gly Thr Thr Pro Gln Asp Phe His Pro Pro Thr Ser Leu Lys Asn Gly
50 55 60
gac agt tcc tac tat gac ccg aat tat tta caa tcg gat gaa gaa aaa 240
Asp Ser Ser Tyr Tyr Asp Pro Asn Tyr Leu Gln Ser Asp Glu Glu Lys
65 70 75 80
gat cgt ttc ctc aag atc gtc acg aaa att ttc aac cgc atc aat aac 288
Asp Arg Phe Leu Lys Ile Val Thr Lys Ile Phe Asn Arg Ile Asn Asn
85 90 95
aat ctg tcc ggt ggc atc tta ctt gag gaa tta tct aaa gct aat ccg 336
Asn Leu Ser Gly Gly Ile Leu Leu Glu Glu Leu Ser Lys Ala Asn Pro
100 105 110
tat ctg ggg aac gat aat acc ccg gat aat cag ttc cac att ggc gat 384
Tyr Leu Gly Asn Asp Asn Thr Pro Asp Asn Gln Phe His Ile Gly Asp
115 120 125
gcg agc gct gtg gaa att aaa ttc agc aac ggc agt caa gat att ctt 432
Ala Ser Ala Val Glu Ile Lys Phe Ser Asn Gly Ser Gln Asp Ile Leu
130 135 140
ctc cca aac gtg att atc atg ggg gct gaa cct gat ctt ttc gaa act 480
Leu Pro Asn Val Ile Ile Met Gly Ala Glu Pro Asp Leu Phe Glu Thr
145 150 155 160
aat agt tcc aat att tca ctg cgc aat aat tat atg ccg tcg aac cat 528
Asn Ser Ser Asn Ile Ser Leu Arg Asn Asn Tyr Met Pro Ser Asn His
165 170 175
ggc ttt ggc tca atc gca att gtg acg ttc tca cct gaa tat agt ttt 576
Gly Phe Gly Ser Ile Ala Ile Val Thr Phe Ser Pro Glu Tyr Ser Phe
180 185 190
cgt ttt aac gac aac agc atg aat gaa ttt atc caa gac ccg gcg ctg 624
Arg Phe Asn Asp Asn Ser Met Asn Glu Phe Ile Gln Asp Pro Ala Leu
195 200 205
act ttg atg cat gaa ctg atc cat agc ttg cac ggc ctg tat ggc gct 672
Thr Leu Met His Glu Leu Ile His Ser Leu His Gly Leu Tyr Gly Ala
210 215 220
aaa ggc atc act acc aaa tac acg att acg caa aaa caa aat ccc tta 720
Lys Gly Ile Thr Thr Lys Tyr Thr Ile Thr Gln Lys Gln Asn Pro Leu
225 230 235 240
atc acc aac atc cgc ggc acc aac att gaa gaa ttt ctg acc ttc ggc 768
Ile Thr Asn Ile Arg Gly Thr Asn Ile Glu Glu Phe Leu Thr Phe Gly
245 250 255
gga acg gat ctg aac atc att aca tct gcc caa agc aac gac atc tat 816
Gly Thr Asp Leu Asn Ile Ile Thr Ser Ala Gln Ser Asn Asp Ile Tyr
260 265 270
acc aat ctg tta gca gat tat aag aaa atc gcc agc aaa tta tct aaa 864
Thr Asn Leu Leu Ala Asp Tyr Lys Lys Ile Ala Ser Lys Leu Ser Lys
275 280 285
gtt cag gtc agc aat ccg ctg tta aac ccg tat aaa gat gtg ttc gaa 912
Val Gln Val Ser Asn Pro Leu Leu Asn Pro Tyr Lys Asp Val Phe Glu
290 295 300
gcg aaa tac ggc ttg gac aaa gac gct agt ggc atc tat tcc gtc aat 960
Ala Lys Tyr Gly Leu Asp Lys Asp Ala Ser Gly Ile Tyr Ser Val Asn
305 310 315 320
att aat aaa ttt aac gat att ttc aaa aaa tta tat tcc ttc acc gaa 1008
Ile Asn Lys Phe Asn Asp Ile Phe Lys Lys Leu Tyr Ser Phe Thr Glu
325 330 335
ttt gat ttg gcc acc aaa ttc cag gtc aaa tgt cgt caa acc tat att 1056
Phe Asp Leu Ala Thr Lys Phe Gln Val Lys Cys Arg Gln Thr Tyr Ile
340 345 350
ggc caa tac aaa tat ttt aaa ctg agc aac ctg ctt aat gat tcc atc 1104
Gly Gln Tyr Lys Tyr Phe Lys Leu Ser Asn Leu Leu Asn Asp Ser Ile
355 360 365
tac aat att agt gaa ggt tac aat att aat aac ctg aaa gtt aac ttt 1152
Tyr Asn Ile Ser Glu Gly Tyr Asn Ile Asn Asn Leu Lys Val Asn Phe
370 375 380
cgt ggg caa aat gcg aat ctg aac ccc cgc atc att aca ccc atc acg 1200
Arg Gly Gln Asn Ala Asn Leu Asn Pro Arg Ile Ile Thr Pro Ile Thr
385 390 395 400
ggc cgt ggg ttg gtc aaa aaa att att cgc ttt gat atc atg ccg ttc 1248
Gly Arg Gly Leu Val Lys Lys Ile Ile Arg Phe Asp Ile Met Pro Phe
405 410 415
gta aac aaa cag ttc aac tat aaa gac cca gtc aac ggc gtg gac att 1296
Val Asn Lys Gln Phe Asn Tyr Lys Asp Pro Val Asn Gly Val Asp Ile
420 425 430
gcc tat atc aaa atc ccg aat gcg ggt caa atg cag ccc gtg aaa gca 1344
Ala Tyr Ile Lys Ile Pro Asn Ala Gly Gln Met Gln Pro Val Lys Ala
435 440 445
ttt aaa atc cat aac aaa att tgg gtg atc ccg gag cgc gat acg ttc 1392
Phe Lys Ile His Asn Lys Ile Trp Val Ile Pro Glu Arg Asp Thr Phe
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acg aac ccg gaa gaa gga gat tta aac cca ccg cct gag gct aaa cag 1440
Thr Asn Pro Glu Glu Gly Asp Leu Asn Pro Pro Pro Glu Ala Lys Gln
465 470 475 480
gtc ccg gtg tct tac tat gat agc aca tac ctg agt acc gac aat gaa 1488
Val Pro Val Ser Tyr Tyr Asp Ser Thr Tyr Leu Ser Thr Asp Asn Glu
485 490 495
aag gac aac tac ctg aaa ggt gtt acc aaa ctg ttc gag cgc att tat 1536
Lys Asp Asn Tyr Leu Lys Gly Val Thr Lys Leu Phe Glu Arg Ile Tyr
500 505 510
tcg aca gat ctc ggt cgc atg ttg ctg act tct att gtg cgc ggc att 1584
Ser Thr Asp Leu Gly Arg Met Leu Leu Thr Ser Ile Val Arg Gly Ile
515 520 525
ccg ttt tgg ggt ggt agc acc atc gat aca gaa ctc aaa gtg att gac 1632
Pro Phe Trp Gly Gly Ser Thr Ile Asp Thr Glu Leu Lys Val Ile Asp
530 535 540
acc aac tgc atc aat gtg att cag cct gat ggg agc tac cgg tcc gaa 1680
Thr Asn Cys Ile Asn Val Ile Gln Pro Asp Gly Ser Tyr Arg Ser Glu
545 550 555 560
gag ctt aac ctc gta atc att ggc ccg agc gcg gat att atc caa ttc 1728
Glu Leu Asn Leu Val Ile Ile Gly Pro Ser Ala Asp Ile Ile Gln Phe
565 570 575
gaa tgt aaa tct ttt ggg cat gaa gtc ctg aat ctg acg cgg aat ggc 1776
Glu Cys Lys Ser Phe Gly His Glu Val Leu Asn Leu Thr Arg Asn Gly
580 585 590
tat gga tcg acg cag tat att cgt ttt tct cca gat ttc aca ttt gga 1824
Tyr Gly Ser Thr Gln Tyr Ile Arg Phe Ser Pro Asp Phe Thr Phe Gly
595 600 605
ttt gaa gaa agc ctc gaa gtt gat acg aac cct ctt tta ggc gcg gga 1872
Phe Glu Glu Ser Leu Glu Val Asp Thr Asn Pro Leu Leu Gly Ala Gly
610 615 620
aaa ttc gcg acg gac cca gcg gtg acc ttg gca cat gaa ctt att cat 1920
Lys Phe Ala Thr Asp Pro Ala Val Thr Leu Ala His Glu Leu Ile His
625 630 635 640
gcc ggg cat cgc ttg tat gga atc gcc att aac ccg aac cgt gtt ttc 1968
Ala Gly His Arg Leu Tyr Gly Ile Ala Ile Asn Pro Asn Arg Val Phe
645 650 655
aag gtg aat acg aac gcg tat tac gag atg tcg ggc tta gaa gtg tcc 2016
Lys Val Asn Thr Asn Ala Tyr Tyr Glu Met Ser Gly Leu Glu Val Ser
660 665 670
ttt gaa gaa ctg cgc acg ttt ggc ggt cat gat gca aaa ttt att gat 2064
Phe Glu Glu Leu Arg Thr Phe Gly Gly His Asp Ala Lys Phe Ile Asp
675 680 685
agt ctg caa gaa aac gaa ttt cgg ctg tac tat tac aat aaa ttc aaa 2112
Ser Leu Gln Glu Asn Glu Phe Arg Leu Tyr Tyr Tyr Asn Lys Phe Lys
690 695 700
gac att gca tca acc tta aac aag gcg aaa agc att gtg ggt acc acg 2160
Asp Ile Ala Ser Thr Leu Asn Lys Ala Lys Ser Ile Val Gly Thr Thr
705 710 715 720
gct agc tta caa tat atg aaa aac gtt ttc aaa gaa aaa tac ctc ctt 2208
Ala Ser Leu Gln Tyr Met Lys Asn Val Phe Lys Glu Lys Tyr Leu Leu
725 730 735
agc gaa gac act tcc ggc aaa ttc tct gtc gat aaa ctg aaa ttt gat 2256
Ser Glu Asp Thr Ser Gly Lys Phe Ser Val Asp Lys Leu Lys Phe Asp
740 745 750
aaa ctg tat aaa atg ctc acc gag atc tac aca gag gat aac ttt gtc 2304
Lys Leu Tyr Lys Met Leu Thr Glu Ile Tyr Thr Glu Asp Asn Phe Val
755 760 765
aaa ttc ttc aag gtc ttg aat cgg aaa acc tat ctg aac ttc gat aaa 2352
Lys Phe Phe Lys Val Leu Asn Arg Lys Thr Tyr Leu Asn Phe Asp Lys
770 775 780
gcc gtc ttt aag atc aac atc gta ccg aaa gtt aac tac acc atc tat 2400
Ala Val Phe Lys Ile Asn Ile Val Pro Lys Val Asn Tyr Thr Ile Tyr
785 790 795 800
gat ggc ttt aat ctg cgc aat acg aat ctg gcg gcg aac ttt aac ggc 2448
Asp Gly Phe Asn Leu Arg Asn Thr Asn Leu Ala Ala Asn Phe Asn Gly
805 810 815
cag aac acc gaa atc aac aac atg aac ttt act aaa ctg aaa aat ttt 2496
Gln Asn Thr Glu Ile Asn Asn Met Asn Phe Thr Lys Leu Lys Asn Phe
820 825 830
acc ggc ttg ttt gaa ttt tat aag ctc ctg tgt gtc cgc ggt att atc 2544
Thr Gly Leu Phe Glu Phe Tyr Lys Leu Leu Cys Val Arg Gly Ile Ile
835 840 845
acc agc aaa acc aaa tcc ttg gtg ccc cgc ggc tct aac aag gcg ctc 2592
Thr Ser Lys Thr Lys Ser Leu Val Pro Arg Gly Ser Asn Lys Ala Leu
850 855 860
aat gat tta tgc atc aag gtg aac aac tgg gac ttg ttt ttc tct cca 2640
Asn Asp Leu Cys Ile Lys Val Asn Asn Trp Asp Leu Phe Phe Ser Pro
865 870 875 880
tct gaa gat aat ttt act aac gac ttg aac aaa gga gag gaa att act 2688
Ser Glu Asp Asn Phe Thr Asn Asp Leu Asn Lys Gly Glu Glu Ile Thr
885 890 895
tcc gat acc aac atc gaa gca gcg gaa gag aat att agc ctg gat ctt 2736
Ser Asp Thr Asn Ile Glu Ala Ala Glu Glu Asn Ile Ser Leu Asp Leu
900 905 910
att caa caa tat tac ctg acc ttt aat ttt gat aac gag cct gag aac 2784
Ile Gln Gln Tyr Tyr Leu Thr Phe Asn Phe Asp Asn Glu Pro Glu Asn
915 920 925
att tcc att gag aat ctc agc tct gac atc atc ggc cag ctg gaa ctg 2832
Ile Ser Ile Glu Asn Leu Ser Ser Asp Ile Ile Gly Gln Leu Glu Leu
930 935 940
atg ccg aat atc gaa cgc ttt cct aat gga aag aaa tat gaa ttg gac 2880
Met Pro Asn Ile Glu Arg Phe Pro Asn Gly Lys Lys Tyr Glu Leu Asp
945 950 955 960
aaa tac acc atg ttc cac tat ctc cgc gcg cag gag ttt gag cac ggc 2928
Lys Tyr Thr Met Phe His Tyr Leu Arg Ala Gln Glu Phe Glu His Gly
965 970 975
aag tct cgt att gct ctg acc aat tcg gta aac gaa gcc ctt tta aat 2976
Lys Ser Arg Ile Ala Leu Thr Asn Ser Val Asn Glu Ala Leu Leu Asn
980 985 990
cct tcg cgt gtg tac acc ttt ttc tca agc gat tat gtt aaa aaa gtg 3024
Pro Ser Arg Val Tyr Thr Phe Phe Ser Ser Asp Tyr Val Lys Lys Val
995 1000 1005
aac aag gcg acc gaa gcg gcg atg ttt ttg gga tgg gtg gaa caa 3069
Asn Lys Ala Thr Glu Ala Ala Met Phe Leu Gly Trp Val Glu Gln
1010 1015 1020
ctg gta tat gac ttt acg gat gaa act tct gaa gtc tcg acc acc 3114
Leu Val Tyr Asp Phe Thr Asp Glu Thr Ser Glu Val Ser Thr Thr
1025 1030 1035
gac aaa att gcc gat att acc att atc att ccc tat att ggc cct 3159
Asp Lys Ile Ala Asp Ile Thr Ile Ile Ile Pro Tyr Ile Gly Pro
1040 1045 1050
gca ctg aac att ggt aac atg ctg tat aaa gat gat ttt gtg ggc 3204
Ala Leu Asn Ile Gly Asn Met Leu Tyr Lys Asp Asp Phe Val Gly
1055 1060 1065
gcc ctg atc ttt tca ggc gct gtt atc ctg ctg gaa ttt atc ccg 3249
Ala Leu Ile Phe Ser Gly Ala Val Ile Leu Leu Glu Phe Ile Pro
1070 1075 1080
gaa atc gcc att cca gta ctc ggt acc ttt gcg ctg gtg tcc tat 3294
Glu Ile Ala Ile Pro Val Leu Gly Thr Phe Ala Leu Val Ser Tyr
1085 1090 1095
atc gca aac aaa gtt ttg act gtc cag acg atc gac aac gcg ctc 3339
Ile Ala Asn Lys Val Leu Thr Val Gln Thr Ile Asp Asn Ala Leu
1100 1105 1110
agt aaa cgt aac gaa aaa tgg gat gag gtg tat aag tat att gtt 3384
Ser Lys Arg Asn Glu Lys Trp Asp Glu Val Tyr Lys Tyr Ile Val
1115 1120 1125
acc aac tgg ctc gct aaa gta aac acc cag att gac ctg att cgc 3429
Thr Asn Trp Leu Ala Lys Val Asn Thr Gln Ile Asp Leu Ile Arg
1130 1135 1140
aag aag atg aaa gaa gcg ctg gaa aac caa gca gaa gcg acc aaa 3474
Lys Lys Met Lys Glu Ala Leu Glu Asn Gln Ala Glu Ala Thr Lys
1145 1150 1155
gct att atc aac tat caa tat aac cag tac aca gag gaa gaa aag 3519
Ala Ile Ile Asn Tyr Gln Tyr Asn Gln Tyr Thr Glu Glu Glu Lys
1160 1165 1170
aat aac atc aac ttc aac atc gac gac tta tct tca aag ctg aat 3564
Asn Asn Ile Asn Phe Asn Ile Asp Asp Leu Ser Ser Lys Leu Asn
1175 1180 1185
gaa tct att aac aaa gcg atg att aat att aac aag ttc ttg aac 3609
Glu Ser Ile Asn Lys Ala Met Ile Asn Ile Asn Lys Phe Leu Asn
1190 1195 1200
caa tgt agt gtc agc tat ctg atg aac tcg atg atc cca tat ggt 3654
Gln Cys Ser Val Ser Tyr Leu Met Asn Ser Met Ile Pro Tyr Gly
1205 1210 1215
gtg aaa cgt ctg gaa gac ttc gat gca agc ctt aaa gat gcc ctt 3699
Val Lys Arg Leu Glu Asp Phe Asp Ala Ser Leu Lys Asp Ala Leu
1220 1225 1230
ctg aag tat att tac gat aat cgc gga act ctt att ggc caa gtg 3744
Leu Lys Tyr Ile Tyr Asp Asn Arg Gly Thr Leu Ile Gly Gln Val
1235 1240 1245
gat cgc tta aaa gat aaa gtc aac aac acg ctg agt aca gac atc 3789
Asp Arg Leu Lys Asp Lys Val Asn Asn Thr Leu Ser Thr Asp Ile
1250 1255 1260
cct ttt cag ctg tct aaa tat gtg gac aat cag cgc ctg ctg tcc 3834
Pro Phe Gln Leu Ser Lys Tyr Val Asp Asn Gln Arg Leu Leu Ser
1265 1270 1275
acg ttt acg gaa tac atc aaa aac atc atc aac act agt att ctg 3879
Thr Phe Thr Glu Tyr Ile Lys Asn Ile Ile Asn Thr Ser Ile Leu
1280 1285 1290
aac ttg cgt tac gag agt aac cat ctg att gat ctg agc cgt tac 3924
Asn Leu Arg Tyr Glu Ser Asn His Leu Ile Asp Leu Ser Arg Tyr
1295 1300 1305
gca tct aaa atc aac atc ggc tcg aag gtg aac ttc gat cct atc 3969
Ala Ser Lys Ile Asn Ile Gly Ser Lys Val Asn Phe Asp Pro Ile
1310 1315 1320
gac aaa aac cag att caa ttg ttc aac tta gaa tcg tca aag att 4014
Asp Lys Asn Gln Ile Gln Leu Phe Asn Leu Glu Ser Ser Lys Ile
1325 1330 1335
gaa gtt atc tta aaa aat gcg att gta tat aat tca atg tac gaa 4059
Glu Val Ile Leu Lys Asn Ala Ile Val Tyr Asn Ser Met Tyr Glu
1340 1345 1350
aat ttc tct acg agc ttt tgg att cgt att ccg aaa tat ttc aac 4104
Asn Phe Ser Thr Ser Phe Trp Ile Arg Ile Pro Lys Tyr Phe Asn
1355 1360 1365
agt atc tct tta aac aac gag tat act atc atc aat tgt atg gag 4149
Ser Ile Ser Leu Asn Asn Glu Tyr Thr Ile Ile Asn Cys Met Glu
1370 1375 1380
aat aac agc ggg tgg aaa gtg agc ctt aac tat ggt gaa atc atc 4194
Asn Asn Ser Gly Trp Lys Val Ser Leu Asn Tyr Gly Glu Ile Ile
1385 1390 1395
tgg act ctg cag gac act caa gaa att aaa caa cgc gtg gtg ttt 4239
Trp Thr Leu Gln Asp Thr Gln Glu Ile Lys Gln Arg Val Val Phe
1400 1405 1410
aaa tac tca cag atg att aac atc tcg gat tat att aat cgc tgg 4284
Lys Tyr Ser Gln Met Ile Asn Ile Ser Asp Tyr Ile Asn Arg Trp
1415 1420 1425
att ttt gtg aca att act aac aac cgg ctg aac aac agc aaa att 4329
Ile Phe Val Thr Ile Thr Asn Asn Arg Leu Asn Asn Ser Lys Ile
1430 1435 1440
tac att aac ggt cgc ctg atc gat cag aaa cca atc agt aat ctc 4374
Tyr Ile Asn Gly Arg Leu Ile Asp Gln Lys Pro Ile Ser Asn Leu
1445 1450 1455
ggt aac att cac gca tcg aat aat atc atg ttc aaa ctg gat ggt 4419
Gly Asn Ile His Ala Ser Asn Asn Ile Met Phe Lys Leu Asp Gly
1460 1465 1470
tgt cgc gac acg cac cgt tac att tgg atc aaa tac ttc aat tta 4464
Cys Arg Asp Thr His Arg Tyr Ile Trp Ile Lys Tyr Phe Asn Leu
1475 1480 1485
ttc gac aaa gaa ctc aac gaa aag gag att aag gat ctt tat gac 4509
Phe Asp Lys Glu Leu Asn Glu Lys Glu Ile Lys Asp Leu Tyr Asp
1490 1495 1500
aat cag tct aat tcg ggt att ctg aaa gac ttt tgg ggt gat tac 4554
Asn Gln Ser Asn Ser Gly Ile Leu Lys Asp Phe Trp Gly Asp Tyr
1505 1510 1515
ctt cag tac gat aaa ccg tat tat atg tta aac tta tat gat ccg 4599
Leu Gln Tyr Asp Lys Pro Tyr Tyr Met Leu Asn Leu Tyr Asp Pro
1520 1525 1530
aat aaa tac gtt gac gtc aac aac gtt ggc att cgt ggc tat atg 4644
Asn Lys Tyr Val Asp Val Asn Asn Val Gly Ile Arg Gly Tyr Met
1535 1540 1545
tat ctg aaa ggg ccg cgt ggc agc gtg atg acc act aac att tac 4689
Tyr Leu Lys Gly Pro Arg Gly Ser Val Met Thr Thr Asn Ile Tyr
1550 1555 1560
tta aac tcc tcc ctc tat cgc ggt act aaa ttt att atc aag aaa 4734
Leu Asn Ser Ser Leu Tyr Arg Gly Thr Lys Phe Ile Ile Lys Lys
1565 1570 1575
tat gcc tct ggc aac aag gac aat atc gta cgc aat aac gat cgc 4779
Tyr Ala Ser Gly Asn Lys Asp Asn Ile Val Arg Asn Asn Asp Arg
1580 1585 1590
gtc tac att aac gtg gtg gtg aag aat aaa gaa tat cgt ctg gcg 4824
Val Tyr Ile Asn Val Val Val Lys Asn Lys Glu Tyr Arg Leu Ala
1595 1600 1605
acc aat gct agt cag gcg ggc gtg gag aaa att ctg tct gca ctt 4869
Thr Asn Ala Ser Gln Ala Gly Val Glu Lys Ile Leu Ser Ala Leu
1610 1615 1620
gaa atc ccg gat gtg ggt aat tta tcc cag gtg gtt gtg atg aaa 4914
Glu Ile Pro Asp Val Gly Asn Leu Ser Gln Val Val Val Met Lys
1625 1630 1635
agt aaa aat gac caa ggg atc acc aat aaa tgc aaa atg aat ctg 4959
Ser Lys Asn Asp Gln Gly Ile Thr Asn Lys Cys Lys Met Asn Leu
1640 1645 1650
caa gat aac aac ggc aac gac att ggt ttt atc ggc ttc cac caa 5004
Gln Asp Asn Asn Gly Asn Asp Ile Gly Phe Ile Gly Phe His Gln
1655 1660 1665
ttc aat aat atc gcg aaa ctg gtg gcc tca aat tgg tac aac cgt 5049
Phe Asn Asn Ile Ala Lys Leu Val Ala Ser Asn Trp Tyr Asn Arg
1670 1675 1680
cag att gag cgc agc tcc cgc act tta ggc tgt agc tgg gag ttc 5094
Gln Ile Glu Arg Ser Ser Arg Thr Leu Gly Cys Ser Trp Glu Phe
1685 1690 1695
att ccg gta gat gac ggt tgg gga gaa cgc cca ttg aaa gtc gac 5139
Ile Pro Val Asp Asp Gly Trp Gly Glu Arg Pro Leu Lys Val Asp
1700 1705 1710
aag ctt ctg gta ccg cgc ggc agc aaa ctg cag ctc gag cac cac 5184
Lys Leu Leu Val Pro Arg Gly Ser Lys Leu Gln Leu Glu His His
1715 1720 1725
cac cac cac cac tga 5199
His His His His
1730
<210> 6
<211> 1732
<212> PRT
<213> 人工序列
<220>
<223> 人工序列的描述：合成多肽
<400> 6
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
Gly Phe Gly Ser Ile Ala Ile Val Thr Phe Ser Pro Glu Tyr Ser Phe
180 185 190
Arg Phe Asn Asp Asn Ser 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 Ala 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 Asp Ile Met Pro Phe
405 410 415
Val Asn Lys Gln Phe Asn Tyr Lys Asp Pro Val Asn Gly Val Asp Ile
420 425 430
Ala Tyr Ile Lys Ile Pro Asn Ala Gly Gln Met Gln Pro Val Lys Ala
435 440 445
Phe Lys Ile His Asn Lys Ile Trp Val Ile Pro Glu Arg Asp Thr Phe
450 455 460
Thr Asn Pro Glu Glu Gly Asp Leu Asn Pro Pro Pro Glu Ala Lys Gln
465 470 475 480
Val Pro Val Ser Tyr Tyr Asp Ser Thr Tyr Leu Ser Thr Asp Asn Glu
485 490 495
Lys Asp Asn Tyr Leu Lys Gly Val Thr Lys Leu Phe Glu Arg Ile Tyr
500 505 510
Ser Thr Asp Leu Gly Arg Met Leu Leu Thr Ser Ile Val Arg Gly Ile
515 520 525
Pro Phe Trp Gly Gly Ser Thr Ile Asp Thr Glu Leu Lys Val Ile Asp
530 535 540
Thr Asn Cys Ile Asn Val Ile Gln Pro Asp Gly Ser Tyr Arg Ser Glu
545 550 555 560
Glu Leu Asn Leu Val Ile Ile Gly Pro Ser Ala Asp Ile Ile Gln Phe
565 570 575
Glu Cys Lys Ser Phe Gly His Glu Val Leu Asn Leu Thr Arg Asn Gly
580 585 590
Tyr Gly Ser Thr Gln Tyr Ile Arg Phe Ser Pro Asp Phe Thr Phe Gly
595 600 605
Phe Glu Glu Ser Leu Glu Val Asp Thr Asn Pro Leu Leu Gly Ala Gly
610 615 620
Lys Phe Ala Thr Asp Pro Ala Val Thr Leu Ala His Glu Leu Ile His
625 630 635 640
Ala Gly His Arg Leu Tyr Gly Ile Ala Ile Asn Pro Asn Arg Val Phe
645 650 655
Lys Val Asn Thr Asn Ala Tyr Tyr Glu Met Ser Gly Leu Glu Val Ser
660 665 670
Phe Glu Glu Leu Arg Thr Phe Gly Gly His Asp Ala Lys Phe Ile Asp
675 680 685
Ser Leu Gln Glu Asn Glu Phe Arg Leu Tyr Tyr Tyr Asn Lys Phe Lys
690 695 700
Asp Ile Ala Ser Thr Leu Asn Lys Ala Lys Ser Ile Val Gly Thr Thr
705 710 715 720
Ala Ser Leu Gln Tyr Met Lys Asn Val Phe Lys Glu Lys Tyr Leu Leu
725 730 735
Ser Glu Asp Thr Ser Gly Lys Phe Ser Val Asp Lys Leu Lys Phe Asp
740 745 750
Lys Leu Tyr Lys Met Leu Thr Glu Ile Tyr Thr Glu Asp Asn Phe Val
755 760 765
Lys Phe Phe Lys Val Leu Asn Arg Lys Thr Tyr Leu Asn Phe Asp Lys
770 775 780
Ala Val Phe Lys Ile Asn Ile Val Pro Lys Val Asn Tyr Thr Ile Tyr
785 790 795 800
Asp Gly Phe Asn Leu Arg Asn Thr Asn Leu Ala Ala Asn Phe Asn Gly
805 810 815
Gln Asn Thr Glu Ile Asn Asn Met Asn Phe Thr Lys Leu Lys Asn Phe
820 825 830
Thr Gly Leu Phe Glu Phe Tyr Lys Leu Leu Cys Val Arg Gly Ile Ile
835 840 845
Thr Ser Lys Thr Lys Ser Leu Val Pro Arg Gly Ser Asn Lys Ala Leu
850 855 860
Asn Asp Leu Cys Ile Lys Val Asn Asn Trp Asp Leu Phe Phe Ser Pro
865 870 875 880
Ser Glu Asp Asn Phe Thr Asn Asp Leu Asn Lys Gly Glu Glu Ile Thr
885 890 895
Ser Asp Thr Asn Ile Glu Ala Ala Glu Glu Asn Ile Ser Leu Asp Leu
900 905 910
Ile Gln Gln Tyr Tyr Leu Thr Phe Asn Phe Asp Asn Glu Pro Glu Asn
915 920 925
Ile Ser Ile Glu Asn Leu Ser Ser Asp Ile Ile Gly Gln Leu Glu Leu
930 935 940
Met Pro Asn Ile Glu Arg Phe Pro Asn Gly Lys Lys Tyr Glu Leu Asp
945 950 955 960
Lys Tyr Thr Met Phe His Tyr Leu Arg Ala Gln Glu Phe Glu His Gly
965 970 975
Lys Ser Arg Ile Ala Leu Thr Asn Ser Val Asn Glu Ala Leu Leu Asn
980 985 990
Pro Ser Arg Val Tyr Thr Phe Phe Ser Ser Asp Tyr Val Lys Lys Val
995 1000 1005
Asn Lys Ala Thr Glu Ala Ala Met Phe Leu Gly Trp Val Glu Gln
1010 1015 1020
Leu Val Tyr Asp Phe Thr Asp Glu Thr Ser Glu Val Ser Thr Thr
1025 1030 1035
Asp Lys Ile Ala Asp Ile Thr Ile Ile Ile Pro Tyr Ile Gly Pro
1040 1045 1050
Ala Leu Asn Ile Gly Asn Met Leu Tyr Lys Asp Asp Phe Val Gly
1055 1060 1065
Ala Leu Ile Phe Ser Gly Ala Val Ile Leu Leu Glu Phe Ile Pro
1070 1075 1080
Glu Ile Ala Ile Pro Val Leu Gly Thr Phe Ala Leu Val Ser Tyr
1085 1090 1095
Ile Ala Asn Lys Val Leu Thr Val Gln Thr Ile Asp Asn Ala Leu
1100 1105 1110
Ser Lys Arg Asn Glu Lys Trp Asp Glu Val Tyr Lys Tyr Ile Val
1115 1120 1125
Thr Asn Trp Leu Ala Lys Val Asn Thr Gln Ile Asp Leu Ile Arg
1130 1135 1140
Lys Lys Met Lys Glu Ala Leu Glu Asn Gln Ala Glu Ala Thr Lys
1145 1150 1155
Ala Ile Ile Asn Tyr Gln Tyr Asn Gln Tyr Thr Glu Glu Glu Lys
1160 1165 1170
Asn Asn Ile Asn Phe Asn Ile Asp Asp Leu Ser Ser Lys Leu Asn
1175 1180 1185
Glu Ser Ile Asn Lys Ala Met Ile Asn Ile Asn Lys Phe Leu Asn
1190 1195 1200
Gln Cys Ser Val Ser Tyr Leu Met Asn Ser Met Ile Pro Tyr Gly
1205 1210 1215
Val Lys Arg Leu Glu Asp Phe Asp Ala Ser Leu Lys Asp Ala Leu
1220 1225 1230
Leu Lys Tyr Ile Tyr Asp Asn Arg Gly Thr Leu Ile Gly Gln Val
1235 1240 1245
Asp Arg Leu Lys Asp Lys Val Asn Asn Thr Leu Ser Thr Asp Ile
1250 1255 1260
Pro Phe Gln Leu Ser Lys Tyr Val Asp Asn Gln Arg Leu Leu Ser
1265 1270 1275
Thr Phe Thr Glu Tyr Ile Lys Asn Ile Ile Asn Thr Ser Ile Leu
1280 1285 1290
Asn Leu Arg Tyr Glu Ser Asn His Leu Ile Asp Leu Ser Arg Tyr
1295 1300 1305
Ala Ser Lys Ile Asn Ile Gly Ser Lys Val Asn Phe Asp Pro Ile
1310 1315 1320
Asp Lys Asn Gln Ile Gln Leu Phe Asn Leu Glu Ser Ser Lys Ile
1325 1330 1335
Glu Val Ile Leu Lys Asn Ala Ile Val Tyr Asn Ser Met Tyr Glu
1340 1345 1350
Asn Phe Ser Thr Ser Phe Trp Ile Arg Ile Pro Lys Tyr Phe Asn
1355 1360 1365
Ser Ile Ser Leu Asn Asn Glu Tyr Thr Ile Ile Asn Cys Met Glu
1370 1375 1380
Asn Asn Ser Gly Trp Lys Val Ser Leu Asn Tyr Gly Glu Ile Ile
1385 1390 1395
Trp Thr Leu Gln Asp Thr Gln Glu Ile Lys Gln Arg Val Val Phe
1400 1405 1410
Lys Tyr Ser Gln Met Ile Asn Ile Ser Asp Tyr Ile Asn Arg Trp
1415 1420 1425
Ile Phe Val Thr Ile Thr Asn Asn Arg Leu Asn Asn Ser Lys Ile
1430 1435 1440
Tyr Ile Asn Gly Arg Leu Ile Asp Gln Lys Pro Ile Ser Asn Leu
1445 1450 1455
Gly Asn Ile His Ala Ser Asn Asn Ile Met Phe Lys Leu Asp Gly
1460 1465 1470
Cys Arg Asp Thr His Arg Tyr Ile Trp Ile Lys Tyr Phe Asn Leu
1475 1480 1485
Phe Asp Lys Glu Leu Asn Glu Lys Glu Ile Lys Asp Leu Tyr Asp
1490 1495 1500
Asn Gln Ser Asn Ser Gly Ile Leu Lys Asp Phe Trp Gly Asp Tyr
1505 1510 1515
Leu Gln Tyr Asp Lys Pro Tyr Tyr Met Leu Asn Leu Tyr Asp Pro
1520 1525 1530
Asn Lys Tyr Val Asp Val Asn Asn Val Gly Ile Arg Gly Tyr Met
1535 1540 1545
Tyr Leu Lys Gly Pro Arg Gly Ser Val Met Thr Thr Asn Ile Tyr
1550 1555 1560
Leu Asn Ser Ser Leu Tyr Arg Gly Thr Lys Phe Ile Ile Lys Lys
1565 1570 1575
Tyr Ala Ser Gly Asn Lys Asp Asn Ile Val Arg Asn Asn Asp Arg
1580 1585 1590
Val Tyr Ile Asn Val Val Val Lys Asn Lys Glu Tyr Arg Leu Ala
1595 1600 1605
Thr Asn Ala Ser Gln Ala Gly Val Glu Lys Ile Leu Ser Ala Leu
1610 1615 1620
Glu Ile Pro Asp Val Gly Asn Leu Ser Gln Val Val Val Met Lys
1625 1630 1635
Ser Lys Asn Asp Gln Gly Ile Thr Asn Lys Cys Lys Met Asn Leu
1640 1645 1650
Gln Asp Asn Asn Gly Asn Asp Ile Gly Phe Ile Gly Phe His Gln
1655 1660 1665
Phe Asn Asn Ile Ala Lys Leu Val Ala Ser Asn Trp Tyr Asn Arg
1670 1675 1680
Gln Ile Glu Arg Ser Ser Arg Thr Leu Gly Cys Ser Trp Glu Phe
1685 1690 1695
Ile Pro Val Asp Asp Gly Trp Gly Glu Arg Pro Leu Lys Val Asp
1700 1705 1710
Lys Leu Leu Val Pro Arg Gly Ser Lys Leu Gln Leu Glu His His
1715 1720 1725
His His His His
1730
<210> 7
<211> 1296
<212> PRT
<213> 肉毒杆菌
<400> 7
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
20 25 30
Val Lys Ala Phe Lys Ile His Asn Lys Ile Trp Val Ile Pro Glu Arg
35 40 45
Asp Thr Phe Thr Asn Pro Glu Glu Gly Asp Leu Asn Pro Pro Pro Glu
50 55 60
Ala Lys Gln Val Pro Val Ser Tyr Tyr Asp Ser Thr Tyr Leu Ser Thr
65 70 75 80
Asp Asn Glu Lys Asp Asn Tyr Leu Lys Gly Val Thr Lys Leu Phe Glu
85 90 95
Arg Ile Tyr Ser Thr Asp Leu Gly Arg Met Leu Leu Thr Ser Ile Val
100 105 110
Arg Gly Ile Pro Phe Trp Gly Gly Ser Thr Ile Asp Thr Glu Leu Lys
115 120 125
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
165 170 175
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
290 295 300
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
355 360 365
Phe Asp Lys Ala Val Phe Lys Ile Asn Ile Val Pro Lys Val Asn Tyr
370 375 380
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
Lys Asn Phe Thr Gly Leu Phe Glu Phe Tyr Lys Leu Leu Cys Val Arg
420 425 430
Gly Ile Ile Thr Ser Lys Thr Lys Ser Leu Asp Lys Gly Tyr Asn Lys
435 440 445
Ala Leu Asn Asp Leu Cys Ile Lys Val Asn Asn Trp Asp Leu Phe Phe
450 455 460
Ser Pro Ser Glu Asp Asn Phe Thr Asn Asp Leu Asn Lys Gly Glu Glu
465 470 475 480
Ile Thr Ser Asp Thr Asn Ile Glu Ala Ala Glu Glu Asn Ile Ser Leu
485 490 495
Asp Leu Ile Gln Gln Tyr Tyr Leu Thr Phe Asn Phe Asp Asn Glu Pro
500 505 510
Glu Asn Ile Ser Ile Glu Asn Leu Ser Ser Asp Ile Ile Gly Gln Leu
515 520 525
Glu Leu Met Pro Asn Ile Glu Arg Phe Pro Asn Gly Lys Lys Tyr Glu
530 535 540
Leu Asp Lys Tyr Thr Met Phe His Tyr Leu Arg Ala Gln Glu Phe Glu
545 550 555 560
His Gly Lys Ser Arg Ile Ala Leu Thr Asn Ser Val Asn Glu Ala Leu
565 570 575
Leu Asn Pro Ser Arg Val Tyr Thr Phe Phe Ser Ser Asp Tyr Val Lys
580 585 590
Lys Val Asn Lys Ala Thr Glu Ala Ala Met Phe Leu Gly Trp Val Glu
595 600 605
Gln Leu Val Tyr Asp Phe Thr Asp Glu Thr Ser Glu Val Ser Thr Thr
610 615 620
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
645 650 655
Ile Phe Ser Gly Ala Val Ile Leu Leu Glu Phe Ile Pro Glu Ile Ala
660 665 670
Ile Pro Val Leu Gly Thr Phe Ala Leu Val Ser Tyr Ile Ala Asn Lys
675 680 685
Val Leu Thr Val Gln Thr Ile Asp Asn Ala Leu Ser Lys Arg Asn Glu
690 695 700
Lys Trp Asp Glu Val Tyr Lys Tyr Ile Val Thr Asn Trp Leu Ala Lys
705 710 715 720
Val Asn Thr Gln Ile Asp Leu Ile Arg Lys Lys Met Lys Glu Ala Leu
725 730 735
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
785 790 795 800
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
835 840 845
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
1085 1090 1095
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
1205 1210 1215
Gln Val Val Val Met Lys Ser Lys Asn Asp Gln Gly Ile Thr Asn
1220 1225 1230
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> 8
<211> 1291
<212> PRT
<213> 肉毒杆菌
<400> 8
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> 9
<211> 1291
<212> PRT
<213> 肉毒杆菌
<400> 9
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 Thr Gly Asn Ile Trp Val Ile Pro Asp
35 40 45
Arg Phe Ser Arg Asn 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 Asp Lys Asp Pro 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 Ser 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 Asp
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 Thr Ile Ser Ser Val Thr Ser Asn Ile
245 250 255
Phe Tyr Ser Gln Tyr Asn 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 Thr Val Asn Arg Asn Lys Phe Val Glu Leu Tyr Asn
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 Val Lys Thr Asp Ile Phe Leu Arg Lys
465 470 475 480
Asp Ile Asn Glu Glu Thr Glu Val Ile Tyr 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 Ser Ile Asp Ser Glu Ser Glu Ile 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 Arg Ser Ile Glu Glu Ala Leu Asp Asn Ser Ala
565 570 575
Lys Val Tyr Thr Tyr Phe Pro Thr Leu Ala Asn Lys Val Asn Ala 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 Pro 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 Met Gly Thr Trp Leu Ser Arg Ile Ile Thr Gln Phe
705 710 715 720
Asn Asn Ile Ser Tyr Gln Met Tyr Asp Ser Leu Asn Tyr Gln Ala Gly
725 730 735
Ala Ile Lys Ala 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 Val 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 Glu Phe Asp Arg Asn Thr Lys Ala Lys Leu Ile Asn
805 810 815
Leu Ile Asp Ser His Asn Ile Ile Leu Val Gly Glu Val Asp Lys Leu
820 825 830
Lys Ala Lys Val Asn Asn Ser Phe Gln 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 Asn Ile Asn Asp Ser Lys Ile Leu Ser Leu Gln Asn Arg Lys
865 870 875 880
Asn Thr Leu Val Asp Thr Ser Gly Tyr Asn Ala Glu Val Ser Glu Glu
885 890 895
Gly Asp Val Gln Leu Asn Pro Ile Phe Pro Phe Asp Phe Lys Leu Gly
900 905 910
Ser Ser Gly Glu Asp Arg Gly Lys Val Ile Val Thr Gln Asn Glu Asn
915 920 925
Ile Val Tyr Asn Ser Met Tyr Glu Ser Phe Ser Ile Ser Phe Trp Ile
930 935 940
Arg Ile Asn Lys Trp Val Ser Asn Leu Pro Gly Tyr Thr Ile Ile Asp
945 950 955 960
Ser Val Lys Asn Asn Ser Gly Trp Ser Ile Gly Ile Ile Ser Asn Phe
965 970 975
Leu Val Phe Thr Leu Lys Gln Asn Glu Asp Ser Glu Gln Ser Ile Asn
980 985 990
Phe Ser Tyr Asp Ile Ser Asn Asn Ala Pro Gly Tyr Asn Lys Trp Phe
995 1000 1005
Phe Val Thr Val Thr Asn Asn Met Met Gly Asn Met Lys Ile Tyr
1010 1015 1020
Ile Asn Gly Lys Leu Ile Asp Thr Ile Lys Val Lys Glu Leu Thr
1025 1030 1035
Gly Ile Asn Phe Ser Lys Thr Ile Thr Phe Glu Ile Asn Lys Ile
1040 1045 1050
Pro Asp Thr Gly Leu Ile Thr Ser Asp Ser Asp Asn Ile Asn Met
1055 1060 1065
Trp Ile Arg Asp Phe Tyr Ile Phe Ala Lys Glu Leu Asp Gly Lys
1070 1075 1080
Asp Ile Asn Ile Leu Phe Asn Ser Leu Gln Tyr Thr Asn Val Val
1085 1090 1095
Lys Asp Tyr Trp Gly Asn Asp Leu Arg Tyr Asn Lys Glu Tyr Tyr
1100 1105 1110
Met Val Asn Ile Asp Tyr Leu Asn Arg Tyr Met Tyr Ala Asn Ser
1115 1120 1125
Arg Gln Ile Val Phe Asn Thr Arg Arg Asn Asn Asn Asp Phe Asn
1130 1135 1140
Glu Gly Tyr Lys Ile Ile Ile Lys Arg Ile Arg Gly Asn Thr Asn
1145 1150 1155
Asp Thr Arg Val Arg Gly Gly Asp Ile Leu Tyr Phe Asp Met Thr
1160 1165 1170
Ile Asn Asn Lys Ala Tyr Asn Leu Phe Met Lys Asn Glu Thr Met
1175 1180 1185
Tyr Ala Asp Asn His Ser Thr Glu Asp Ile Tyr Ala Ile Gly Leu
1190 1195 1200
Arg Glu Gln Thr Lys Asp Ile Asn Asp Asn Ile Ile Phe Gln Ile
1205 1210 1215
Gln Pro Met Asn Asn Thr Tyr Tyr Tyr Ala Ser Gln Ile Phe Lys
1220 1225 1230
Ser Asn Phe Asn Gly Glu Asn Ile Ser Gly Ile Cys Ser Ile Gly
1235 1240 1245
Thr Tyr Arg Phe Arg Leu Gly Gly Asp Trp Tyr Arg His Asn Tyr
1250 1255 1260
Leu Val Pro Thr Val Lys Gln Gly Asn Tyr Ala Ser Leu Leu Glu
1265 1270 1275
Ser Thr Ser Thr His Trp Gly Phe Val Pro Val Ser Glu
1280 1285 1290
<210> 10
<211> 1276
<212> PRT
<213> 肉毒杆菌
<400> 10
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 Leu Asp Val Glu Ile Ile Pro Gln Ile Glu Arg Ser 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 Ile 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 Arg His Tyr Leu Pro Val Phe
370 375 380
Ala Asn Ile Leu Asp Asp Asn Ile Tyr Thr Ile Arg Asp Gly Phe Asn
385 390 395 400
Leu Thr Asn 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 Lys Asn Ser Arg Asp Asp Ser
435 440 445
Thr Cys Ile Lys Val Lys Asn Asn Arg Leu Pro Tyr Val Ala Asp Lys
450 455 460
Asp Ser Ile Ser Gln Glu Ile Phe Glu Asn Lys Ile Ile Thr Asp Glu
465 470 475 480
Thr Asn Val Gln Asn Tyr Ser Asp Lys Phe Ser Leu Asp Glu Ser Ile
485 490 495
Leu Asp Gly Gln Val Pro Ile Asn Pro Glu Ile Val Asp Pro Leu Leu
500 505 510
Pro Asn Val Asn Met Glu Pro Leu Asn Leu Pro Gly Glu Glu Ile Val
515 520 525
Phe Tyr Asp Asp Ile Thr Lys Tyr Val Asp Tyr Leu Asn Ser Tyr Tyr
530 535 540
Tyr Leu Glu Ser 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 Val 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 Asn 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 Gln Phe Asn His Ile Asn
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 Arg 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 Met Pro Phe Asn Ile Phe Ser Tyr Thr
835 840 845
Asn Asn Ser Leu Leu Lys Asp Ile Ile Asn Glu Tyr Phe Asn Ser Ile
850 855 860
Asn Asp Ser Lys Ile Leu Ser Leu Gln Asn Lys Lys Asn Ala Leu Val
865 870 875 880
Asp Thr Ser Gly Tyr Asn Ala Glu Val Arg Val Gly Asp Asn Val Gln
885 890 895
Leu Asn Thr Ile Tyr Thr Asn Asp Phe Lys Leu Ser Ser Ser Gly Asp
900 905 910
Lys Ile Ile Val Asn Leu Asn Asn Asn Ile Leu Tyr Ser Ala Ile Tyr
915 920 925
Glu Asn Ser Ser Val Ser Phe Trp Ile Lys Ile Ser Lys Asp Leu Thr
930 935 940
Asn Ser His Asn Glu Tyr Thr Ile Ile Asn Ser Ile Glu Gln Asn Ser
945 950 955 960
Gly Trp Lys Leu Cys Ile Arg Asn Gly Asn Ile Glu Trp Ile Leu Gln
965 970 975
Asp Val Asn Arg Lys Tyr Lys Ser Leu Ile Phe Asp Tyr Ser Glu Ser
980 985 990
Leu Ser His Thr Gly Tyr Thr Asn Lys Trp Phe Phe Val Thr Ile Thr
995 1000 1005
Asn Asn Ile Met Gly Tyr Met Lys Leu Tyr Ile Asn Gly Glu Leu
1010 1015 1020
Lys Gln Ser Gln Lys Ile Glu Asp Leu Asp Glu Val Lys Leu Asp
1025 1030 1035
Lys Thr Ile Val Phe Gly Ile Asp Glu Asn Ile Asp Glu Asn Gln
1040 1045 1050
Met Leu Trp Ile Arg Asp Phe Asn Ile Phe Ser Lys Glu Leu Ser
1055 1060 1065
Asn Glu Asp Ile Asn Ile Val Tyr Glu Gly Gln Ile Leu Arg Asn
1070 1075 1080
Val Ile Lys Asp Tyr Trp Gly Asn Pro Leu Lys Phe Asp Thr Glu
1085 1090 1095
Tyr Tyr Ile Ile Asn Asp Asn Tyr Ile Asp Arg Tyr Ile Ala Pro
1100 1105 1110
Glu Ser Asn Val Leu Val Leu Val Gln Tyr Pro Asp Arg Ser Lys
1115 1120 1125
Leu Tyr Thr Gly Asn Pro Ile Thr Ile Lys Ser Val Ser Asp Lys
1130 1135 1140
Asn Pro Tyr Ser Arg Ile Leu Asn Gly Asp Asn Ile Ile Leu His
1145 1150 1155
Met Leu Tyr Asn Ser Arg Lys Tyr Met Ile Ile Arg Asp Thr Asp
1160 1165 1170
Thr Ile Tyr Ala Thr Gln Gly Gly Glu Cys Ser Gln Asn Cys Val
1175 1180 1185
Tyr Ala Leu Lys Leu Gln Ser Asn Leu Gly Asn Tyr Gly Ile Gly
1190 1195 1200
Ile Phe Ser Ile Lys Asn Ile Val Ser Lys Asn Lys Tyr Cys Ser
1205 1210 1215
Gln Ile Phe Ser Ser Phe Arg Glu Asn Thr Met Leu Leu Ala Asp
1220 1225 1230
Ile Tyr Lys Pro Trp Arg Phe Ser Phe Lys Asn Ala Tyr Thr Pro
1235 1240 1245
Val Ala Val Thr Asn Tyr Glu Thr Lys Leu Leu Ser Thr Ser Ser
1250 1255 1260
Phe Trp Lys Phe Ile Ser Arg Asp Pro Gly Trp Val Glu
1265 1270 1275
<210> 11
<211> 1252
<212> PRT
<213> 肉毒杆菌
<400> 11
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
Gly Phe Gly Ser Ile Ala Ile Val Thr Phe Ser Pro Glu Tyr Ser Phe
180 185 190
Arg Phe Asn Asp Asn Ser 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 Ala 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 Leu 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 Leu Gln Asp Asn Ala 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 Asn Cys Thr Met Asn Phe Lys Asn
1190 1195 1200
Asn Asn Gly Asn Asn Ile Gly Leu Leu Gly Phe Lys Ala Asp Thr
1205 1210 1215
Val Val Ala Ser Thr Trp Tyr Tyr Thr His Met Arg Asp His Thr
1220 1225 1230
Asn Ser Asn Gly Cys Phe Trp Asn Phe Ile Ser Glu Glu His Gly
1235 1240 1245
Trp Gln Glu Lys
1250
<210> 12
<211> 1274
<212> PRT
<213> 肉毒杆菌
<400> 12
Met Pro Val Ala Ile Asn Ser Phe Asn Tyr Asn Asp Pro Val Asn Asp
1 5 10 15
Asp Thr Ile Leu Tyr Met Gln Ile Pro Tyr Glu Glu Lys Ser Lys Lys
20 25 30
Tyr Tyr Lys Ala Phe Glu Ile Met Arg Asn Val Trp Ile Ile Pro Glu
35 40 45
Arg Asn Thr Ile Gly Thr Asn Pro Ser Asp Phe Asp Pro Pro Ala 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 Thr Ile Lys Leu Phe Lys
85 90 95
Arg Ile Asn Ser Asn Pro Ala Gly Lys Val Leu Leu Gln Glu Ile Ser
100 105 110
Tyr Ala Lys Pro Tyr Leu Gly Asn Asp His Thr Pro Ile Asp Glu Phe
115 120 125
Ser Pro Val Thr Arg Thr Thr Ser Val Asn Ile Lys Leu Ser Thr Asn
130 135 140
Val Glu Ser Ser Met Leu Leu Asn Leu Leu Val Leu Gly Ala Gly Pro
145 150 155 160
Asp Ile Phe Glu Ser Cys Cys Tyr Pro Val Arg Lys Leu Ile Asp Pro
165 170 175
Asp Val Val Tyr Asp Pro Ser Asn Tyr Gly Phe Gly Ser Ile Asn Ile
180 185 190
Val Thr Phe Ser Pro Glu Tyr Glu Tyr Thr Phe Asn Asp Ile Ser Gly
195 200 205
Gly His Asn Ser 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 Arg
225 230 235 240
Gly Val Thr Tyr Glu Glu Thr Ile Glu Val Lys Gln Ala 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
Gln Asp Leu Asn Ile Ile Thr Ser Ala Met Lys Glu Lys Ile Tyr Asn
275 280 285
Asn Leu Leu Ala Asn Tyr Glu Lys Ile Ala Thr Arg Leu Ser Glu Val
290 295 300
Asn Ser Ala Pro Pro Glu Tyr Asp Ile Asn Glu Tyr Lys Asp Tyr Phe
305 310 315 320
Gln Trp Lys Tyr Gly Leu Asp Lys Asn Ala Asp Gly Ser Tyr Thr Val
325 330 335
Asn Glu Asn Lys Phe Asn Glu Ile Tyr Lys Lys Leu Tyr Ser Phe Thr
340 345 350
Glu Ser Asp Leu Ala Asn Lys Phe Lys Val Lys Cys Arg Asn Thr Tyr
355 360 365
Phe Ile Lys Tyr Glu Phe Leu 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 Ser Ile Lys Leu Asn Pro Lys Ile Ile Asp Ser Ile
405 410 415
Pro Asp Lys Gly Leu Val Glu Lys Ile Val Lys Phe Cys Lys Ser Val
420 425 430
Ile Pro Arg Lys Gly Thr Lys Ala Pro Pro Arg Leu Cys Ile Arg Val
435 440 445
Asn Asn Ser Glu Leu Phe Phe Val Ala Ser Glu Ser Ser Tyr Asn Glu
450 455 460
Asn 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
Gln 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 Asp Ile Phe Phe Ser Ser Glu
565 570 575
Phe Ile Asp Thr Ile Asn Lys Pro Val Asn Ala Ala Leu Phe Ile Asp
580 585 590
Trp Ile Ser Lys Val Ile Arg Asp Phe Thr Thr Glu Ala Thr Gln Lys
595 600 605
Ser Thr Val Asp Lys Ile Ala Asp Ile Ser Leu Ile Val Pro Tyr Val
610 615 620
Gly Leu Ala Leu Asn Ile Ile Ile Glu Ala Glu Lys Gly Asn Phe Glu
625 630 635 640
Glu Ala Phe Glu Leu Leu Gly Val Gly Ile Leu Leu Glu Phe Val Pro
645 650 655
Glu Leu Thr Ile Pro Val Ile Leu Val Phe Thr Ile Lys Ser Tyr Ile
660 665 670
Asp Ser Tyr Glu Asn Lys Asn Lys Ala Ile Lys Ala Ile Asn Asn Ser
675 680 685
Leu Ile Glu Arg Glu Ala Lys Trp Lys Glu Ile Tyr Ser Trp Ile Val
690 695 700
Ser Asn Trp Leu Thr Arg Ile Asn Thr Gln Phe Asn Lys Arg Lys Glu
705 710 715 720
Gln Met Tyr Gln Ala Leu Gln Asn Gln Val Asp Ala Ile Lys Thr Ala
725 730 735
Ile Glu Tyr Lys Tyr Asn Asn Tyr Thr Ser Asp Glu Lys Asn Arg Leu
740 745 750
Glu Ser Glu Tyr Asn Ile Asn Asn Ile Glu Glu Glu Leu Asn Lys Lys
755 760 765
Val Ser Leu Ala Met Lys Asn Ile Glu Arg Phe Met Thr Glu Ser Ser
770 775 780
Ile Ser Tyr Leu Met Lys Leu Ile Asn Glu Ala Lys Val Gly Lys Leu
785 790 795 800
Lys Lys Tyr Asp Asn His Val Lys Ser Asp Leu Leu Asn Tyr Ile Leu
805 810 815
Asp His Arg Ser Ile Leu Gly Glu Gln Thr Asn Glu Leu Ser Asp Leu
820 825 830
Val Thr Ser Thr Leu Asn Ser Ser Ile Pro Phe Glu Leu Ser Ser Tyr
835 840 845
Thr Asn Asp Lys Ile Leu Ile Ile Tyr Phe Asn Arg Leu Tyr Lys Lys
850 855 860
Ile Lys Asp Ser Ser Ile Leu Asp Met Arg Tyr Glu Asn Asn Lys Phe
865 870 875 880
Ile Asp Ile Ser Gly Tyr Gly Ser Asn Ile Ser Ile Asn Gly Asn Val
885 890 895
Tyr Ile Tyr Ser Thr Asn Arg Asn Gln Phe Gly Ile Tyr Asn Ser Arg
900 905 910
Leu Ser Glu Val Asn Ile Ala Gln Asn Asn Asp Ile Ile Tyr Asn Ser
915 920 925
Arg Tyr Gln Asn Phe Ser Ile Ser Phe Trp Val Arg Ile Pro Lys His
930 935 940
Tyr Lys Pro Met Asn His Asn Arg Glu Tyr Thr Ile Ile Asn Cys Met
945 950 955 960
Gly Asn Asn Asn Ser Gly Trp Lys Ile Ser Leu Arg Thr Val Arg Asp
965 970 975
Cys Glu Ile Ile Trp Thr Leu Gln Asp Thr Ser Gly Asn Lys Glu Asn
980 985 990
Leu Ile Phe Arg Tyr Glu Glu Leu Asn Arg Ile Ser Asn Tyr Ile Asn
995 1000 1005
Lys Trp Ile Phe Val Thr Ile Thr Asn Asn Arg Leu Gly Asn Ser
1010 1015 1020
Arg Ile Tyr Ile Asn Gly Asn Leu Ile Val Glu Lys Ser Ile Ser
1025 1030 1035
Asn Leu Gly Asp Ile His Val Ser Asp Asn Ile Leu Phe Lys Ile
1040 1045 1050
Val Gly Cys Asp Asp Glu Thr Tyr Val Gly Ile Arg Tyr Phe Lys
1055 1060 1065
Val Phe Asn Thr Glu Leu Asp Lys Thr Glu Ile Glu Thr Leu Tyr
1070 1075 1080
Ser Asn Glu Pro Asp Pro Ser Ile Leu Lys Asn Tyr Trp Gly Asn
1085 1090 1095
Tyr Leu Leu Tyr Asn Lys Lys Tyr Tyr Leu Phe Asn Leu Leu Arg
1100 1105 1110
Lys Asp Lys Tyr Ile Thr Leu Asn Ser Gly Ile Leu Asn Ile Asn
1115 1120 1125
Gln Gln Arg Gly Val Thr Glu Gly Ser Val Phe Leu Asn Tyr Lys
1130 1135 1140
Leu Tyr Glu Gly Val Glu Val Ile Ile Arg Lys Asn Gly Pro Ile
1145 1150 1155
Asp Ile Ser Asn Thr Asp Asn Phe Val Arg Lys Asn Asp Leu Ala
1160 1165 1170
Tyr Ile Asn Val Val Asp Arg Gly Val Glu Tyr Arg Leu Tyr Ala
1175 1180 1185
Asp Thr Lys Ser Glu Lys Glu Lys Ile Ile Arg Thr Ser Asn Leu
1190 1195 1200
Asn Asp Ser Leu Gly Gln Ile Ile Val Met Asp Ser Ile Gly Asn
1205 1210 1215
Asn Cys Thr Met Asn Phe Gln Asn Asn Asn Gly Ser Asn Ile Gly
1220 1225 1230
Leu Leu Gly Phe His Ser Asn Asn Leu Val Ala Ser Ser Trp Tyr
1235 1240 1245
Tyr Asn Asn Ile Arg Arg Asn Thr Ser Ser Asn Gly Cys Phe Trp
1250 1255 1260
Ser Ser Ile Ser Lys Glu Asn Gly Trp Lys Glu
1265 1270
<210> 13
<211> 1297
<212> PRT
<213> 肉毒杆菌
<400> 13
Met Pro Val Asn Ile Lys Asn 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
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Val Lys Asp Tyr Gly Tyr Val Trp Asp Thr Tyr Asp Asn Tyr Phe
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Gly Trp Thr Glu
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Leu Ile Glu Gly Ala Ser Glu Tyr Tyr Asp Pro Asn Tyr Leu Arg Thr
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Arg Ile Lys Asn Asn Val Ala Gly Glu Ala Leu Leu Asp Lys Ile Ile
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Asn Ala Ile Pro Tyr Leu Gly Asn Ser Tyr Ser Leu Leu Asp Lys Phe
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Asp Thr Asn Ser Asn Ser Val Ser Phe Asn Leu Leu Glu Gln Asp Pro
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Ser Gly Ala Thr Thr Lys Ser Ala Met Leu Thr Asn Leu Ile Ile Phe
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Gly Pro Gly Pro Val Leu Asn Lys Asn Glu Val Arg Gly Ile Val Leu
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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
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Gln Glu Ile Tyr Met Gln His Thr Tyr Pro Ile Ser Ala Glu Glu Leu
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Phe Thr Phe Gly Gly Gln Asp Ala Asn Leu Ile Ser Ile Asp Ile Lys
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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
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405 410 415
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420 425 430
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435 440 445
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450 455 460
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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
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Tyr Gln Tyr Leu Tyr Ala Gln Lys Ser Pro Thr Thr Leu Gln Arg Ile
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Tyr Ser Tyr Phe Pro Ser Val Ile Ser Lys Val Asn Gln Gly Ala Gln
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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
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Ser Ile Ala Glu Ser Ser Thr Gln Lys Glu Lys Ile Ile Lys Thr Ile
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705 710 715 720
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740 745 750
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Ser Lys Ile Asn Lys Val Phe Ser Thr Pro Ile Pro Phe Ser Tyr Ser
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1010 1015 1020
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Gly Ser Ala Glu Ile Thr Gly Leu Gly Ala Ile Arg Glu Asp Asn
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Asn Ile Thr Leu Lys Leu Asp Arg Cys Asn Asn Asn Asn Gln Tyr
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1 5
Claims (21)
1.一种核酸，其具有包括核苷酸序列SEQ ID NO:5的单个开放阅读框核酸序列。
2.如权利要求1所述的核酸，其中所述开放阅读框核酸序列由SEQ ID NO:5组成。
3.一种多肽，其包括氨基酸序列SEQ ID NO:6。
4.如权利要求3所述的多肽，其由氨基酸序列SEQ ID NO:6组成。
5.一种多肽，其具有BoNT/A内肽酶活性和BoNT/E内肽酶活性，所述BoNT/A内肽酶活性和BoNT/E内肽酶活性源自包括氨基酸序列SEQ ID NO:6的多肽用凝血酶的蛋白水解消化。
6.治疗性组合物在制备用于治疗慢性疼痛的药物中的用途，其中所述治疗性组合物包括权利要求5所述的多肽。
7.如权利要求6所述的用途，其中所述慢性疼痛选自由以下组成的组：炎性伤害性疼痛和神经性疼痛。
8.如权利要求7所述的用途，其中所述神经性疼痛选自由以下组成的组：癌症疼痛、术后疼痛、异常性疼痛、疱疹后神经痛、肠易激综合症以及其他内脏痛、骨痛、周围神经病变、循环系统附属疼痛以及头痛疼痛。
9.如权利要求7所述的用途，其中所述慢性疼痛是炎性伤害性疼痛。
10.如权利要求9所述的用途，其中所述慢性疼痛是关节炎疼痛。
11.一种核酸，其包括：
a)单个开放阅读框核苷酸序列，所述单个开放阅读框核苷酸序列编码具有下述的多肽：
i)具有肉毒杆菌神经毒素血清型A(BoNT/A)HC细胞表面结合活性的结构域，
ii)具有BoNT/A HN易位活性的结构域；
iii)具有BoNT/A内肽酶活性的第一内肽酶结构域；
iv)具有肉毒杆菌神经毒素血清型E(BoNT/E)内肽酶活性的第二内肽酶结构域；和
v)通过第一氨基酸序列与所述多肽的N末端和/或羧基端分开的至少六个连续组氨酸残基，所述第一氨基酸序列可被第一非肉毒梭菌衍生的内肽酶裂解；
所述单个开放阅读框核苷酸序列被优化用于在大肠杆菌中表达。
12.一种多肽，其由权利要求11中的单个开放阅读框核苷酸序列编码。
13.如权利要求12所述的多肽，其进一步用所述第一非肉毒梭菌衍生的内肽酶消化。
14.如权利要求12所述的多肽，其中所述第一内肽酶结构域和所述第二内肽酶结构域被第二氨基酸序列分开，所述第二氨基酸序列可被第二非肉毒梭菌衍生的内肽酶裂解。
15.如权利要求14所述的多肽，其中所述第一氨基酸序列和所述第二氨基酸序列可被相同的非肉毒梭菌衍生的内肽酶裂解。
16.如权利要求14所述的多肽，其进一步用所述第二非肉毒梭菌衍生的内肽酶裂解。
17.治疗性组合物在制备用于治疗慢性疼痛的药物中的用途，其中所述治疗性组合物包括权利要求16所述的多肽。
18.如权利要求17所述的用途，其中所述慢性疼痛选自由以下组成的组：炎性伤害性疼痛和神经性疼痛。
19.如权利要求18所述的用途，其中所述神经性疼痛选自由以下组成的组：癌症疼痛、术后疼痛、异常性疼痛、疱疹后神经痛、肠易激综合症以及其他内脏痛、骨痛、周围神经病变、循环系统附属疼痛以及头痛疼痛。
20.如权利要求18所述的用途，其中所述慢性疼痛是炎性伤害性疼痛。
21.如权利要求18所述的用途，其中所述慢性疼痛是关节炎疼痛。
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| CN201480073447.XA CN105916875A (zh) | 2013-12-23 | 2014-12-19 | 用于慢性疼痛的多蛋白酶治疗剂 |
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- 2014-12-19 PL PL14821171T patent/PL3087089T3/pl unknown
- 2014-12-19 EP EP14821171.7A patent/EP3087089B1/en active Active
- 2014-12-19 CN CN202011545696.8A patent/CN112708630A/zh active Pending
- 2014-12-19 CN CN201480073447.XA patent/CN105916875A/zh active Pending
- 2014-12-19 PT PT148211717T patent/PT3087089T/pt unknown
- 2014-12-19 WO PCT/EP2014/078732 patent/WO2015097087A1/en active Application Filing
- 2014-12-19 DK DK14821171.7T patent/DK3087089T3/en active
- 2014-12-19 JP JP2016541634A patent/JP6378772B2/ja active Active
- 2014-12-19 AU AU2014372689A patent/AU2014372689B2/en not_active Ceased
- 2014-12-19 ES ES14821171.7T patent/ES2671493T3/es active Active
- 2014-12-19 KR KR1020167019888A patent/KR101900582B1/ko active IP Right Grant
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2015
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2016
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Also Published As
| Publication number | Publication date |
|---|---|
| PT3087089T (pt) | 2018-05-28 |
| AU2014372689A1 (en) | 2016-07-21 |
| US9216210B2 (en) | 2015-12-22 |
| PL3087089T3 (pl) | 2018-10-31 |
| ZA201605051B (en) | 2017-09-27 |
| US10457927B2 (en) | 2019-10-29 |
| US20160230159A1 (en) | 2016-08-11 |
| ES2671493T3 (es) | 2018-06-06 |
| KR101900582B1 (ko) | 2018-09-19 |
| EP3087089B1 (en) | 2018-02-21 |
| CN105916875A (zh) | 2016-08-31 |
| EP3087089A1 (en) | 2016-11-02 |
| JP2017501715A (ja) | 2017-01-19 |
| JP6378772B2 (ja) | 2018-08-22 |
| AU2014372689B2 (en) | 2018-02-01 |
| CA2934986A1 (en) | 2015-07-02 |
| WO2015097087A1 (en) | 2015-07-02 |
| CA2934986C (en) | 2019-08-20 |
| KR20160096201A (ko) | 2016-08-12 |
| DK3087089T3 (en) | 2018-06-06 |
| US20150174217A1 (en) | 2015-06-25 |
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Application publication date: 20210427 |