一种预防和治疗免疫相关疾病的组合物的制作方法

本发明涉及一种能够有效预防或治疗免疫相关疾病的组合物。
背景技术：
：免疫球蛋白由四条多肽链组成，即两条重链和两条轻链，它们通过链间二硫键相互连接。每个轻链有两个区域，即轻链可变区(vl)和轻链恒定区(cl)；每个重链有两个区域，即重链可变区和重链恒定区。重链恒定区(ch)包含由数字(参见，例如us6,086,875(blumbbergr.s.等)、us5,624,821(winterg.p.等)和us5,116,964(capond.j.和laskyl.a.))指定的重链恒定区(例如ch1、ch2、ch3等)。免疫球蛋白根据其生物学特性、在生物体中的位置和处理不同抗原的能力被分为不同的同种型(即igg、igm、iga、igd和ige)。根据免疫球蛋白的同种型，重链恒定区(ch)可能有3或4个重链恒定区。此外，在一些同种型(iga、igd和igg)中，重链包含增加分子灵活性的铰链区(janeway等，2001，免疫生物学，纽约加兰出版社，纽约)。在人类中，有四个igg亚类(igg1、2、3和4)，这些igg按照它们在血清中的浓度高低(即igg1浓度最高)来命名。igg同种型由两条轻链和两条重链组成，其中每条重链包括三个重链恒定区(ch1、ch2和ch3)。igg的两条重链通过二硫键(-s-s-)相互连接，且每条重链通过二硫键与一条轻链连接。igg的抗原结合位点位于抗原结合片段区(fab区)，包括轻链(vl)和重链(vh)的可变区以及轻链(cl)和重链(ch1)的恒定区。igg的可结晶片段区(fc区)是包含ch2和ch3结构域的重链的一部分，这些结构域与某些细胞表面的fc受体结合，包括新生fc受体(fcrn)。igg的重链在ch1和ch2之间还有一个铰链区，它将fab区和fc区分开，并通过二硫键将两条重链连接在一起。铰链区的结构有助于四个igg亚类中每一个的独特生物特性。igg是作为一种体积小的单体分泌的，从而其更容易的渗透进入组织。它是唯一一种具有可以穿过人类胎盘的受体(新生儿fc受体(fcrn))的同种型，从而为子宫内的胎儿提供保护。通过胎盘吸收的igg在新生儿自身免疫系统发育之前可以为其提供体液免疫。igg新生儿fc受体结合位点位于抗体的fc区。fcrn通常在人胎盘和上皮细胞中表达，并参与阻止igg降解的内吞补救途径。这种补救途径是通过在酸性ph下igg对fcrn的高度ph依赖性的结合亲和力来介导的。在酸性ph下，igg对fcrn的高度亲和力被认为是导致内化的igg再被吸收到酸性内体后对fcrn的结合(goeblna.等，2008；junghansrp等，1996)。大多数可溶性蛋白质在内化后被导向溶酶体；然而，内化的fcrn结合的igg返回到质膜，并被有效地从潜在的降解途径中拯救出来。当暴露于细胞外空间的中性ph环境时，igg可从fcrn中解离出来并返回到循环中。因此，使得抗体的延长血清半衰期特性保留在fc片段中。补救途径为开发下一代蛋白质药物提供了一种机制，与未修饰的蛋白质药物相比，这种药物在血液循环中具有更长的半衰期。特别地，未修饰的蛋白质药物具有较短的循环半衰期，因此需要在所需的长期治疗期间内频繁给药。目前已经进行了大量的努力、使用了大量的方法来延长蛋白质药物的半衰期，包括聚乙二醇化和融合蛋白技术(美国食品和药物管理局；osbornbl等，2002)；然而，这些努力并没有产生理想的结果。免疫疾病是由哺乳动物免疫系统的成分引起、介导或以其他方式导致哺乳动物病理状况的疾病。特别的，炎症性疾病是世界上最重要的健康问题之一。炎症通常是身体组织对外来物质或有害刺激入侵宿主的局部保护性反应。炎症的诱因包括传染性物质，如细菌、病毒和寄生虫等；物理因素，如烧伤或辐射；化学品，如毒素、药物或工业制剂；免疫反应，如过敏和自身免疫反应；或与氧化应激相关的疾病。炎症的特征是疼痛、发红现象、肿胀、发热以及炎症区域最终功能的丧失。这些症状是免疫系统中细胞之间一系列复杂相互作用的结果。细胞反应使得几组炎症介质之间形成相互作用的网络，所述炎症介质包括：蛋白质(例如细胞因子、酶(例如蛋白酶、过氧化物酶))、主要碱性蛋白、粘附分子(icam、vcam)、脂质介质(例如类花生酸、前列腺素、白三烯、血小板活化因子(paf))、活性氧(例如氢过氧化物、超氧阴离子o2-、一氧化氮(no)等)。然而，大多数炎症介质也是正常细胞活动的调节剂。因此，炎症反应的缺乏将导致宿主处于不受控制的状态，从而使宿主受损(即被感染)。因此，慢性炎症部分导致上述几种介质的过量产生，从而导致炎症性疾病。此外，自身免疫性疾病作为免疫性疾病之一，其特征是免疫系统攻击自身器官引起的自发反应。这些反应是由于t淋巴细胞对自身抗原的识别，从而引起的体液免疫反应(产生自身抗原)和细胞免疫反应(淋巴细胞和巨噬细胞的细胞毒性活性的增加)。自身免疫性疾病的示例可以包括：风湿性疾病、牛皮癣、系统性皮肌炎、多发性硬化、红斑狼疮、或由抗原引起的免疫反应恶化，即哮喘、药物或食物过敏等。所有这些疾病都是限制性疾病和慢性疾病，其在某些情况下是致命的。迄今为止，还没有有效的治疗方法可以治疗上述疾病。因此，能够在疾病发展过程中减少或缓解这些疾病的药物、药剂或介质将是对患者健康的重要解决方案。技术问题通过寻找自身免疫性疾病的治疗方法，许多研究人员一直在努力寻找合适的药物和方法。如今，自身免疫性疾病的治疗主要基于免疫抑制药物的使用，如糖皮质激素、钙调神经磷酸酶抑制剂和抗增殖药-抗代谢药物。然而，这种药物疗法作用于多个靶点，因此可能导致整体免疫功能的下降。另外，在长期使用这种药物疗法的情况下，多种细胞毒性反应会引起问题并以非特异性的方式抑制免疫系统，使得患者可能有感染疾病或免疫相关疾病的风险。由于钙调神经磷酸酶和糖皮质激素的肾毒性和致糖尿病特性，其可能引起其他问题，因此它们被限制仅在某些临床症状(例如，肾功能不全、糖尿病等)下使用。因此，作为能够治疗免疫相关疾病如自身免疫性疾病、炎性疾病和移植排斥反应的物质，需要开发新的具有优异的治疗效果而没有副作用的治疗剂。技术实现要素：本发明的目的是提供一种预防、改善或治疗免疫相关疾病的组合物，其包含作为活性成分的融合蛋白，所述融合蛋白包含富含亮氨酸和免疫球蛋白样结构域-1(lrig-1)蛋白的胞外结构域和免疫球蛋白fc区。本发明的另一个目的是提供一种预防、改善或治疗免疫相关疾病的方法。然而，本发明要实现的技术问题不限于上述问题，并且本领域普通技术人员将从以下描述中清楚地理解未提及的其他问题。1.预防、改善或治疗免疫相关疾病的组合物在本发明的一个实施方式中，提供了一种预防、改善或治疗免疫相关疾病的组合物。本发明的组合物可以用作药物组合物、食物组合物、或者化妆品组合物。本发明的组合物包含作为活性成分的：融合蛋白，所述融合蛋白包含富含亮氨酸和免疫球蛋白样结构域-1(lrig-1)蛋白的胞外结构域和免疫球蛋白fc区；编码融合蛋白的核酸分子；包含核酸分子的表达载体；或者用表达载体转化的宿主细胞。在下文中，将对本发明的每个配置进行详细描述。活性成分1)融合蛋白lrig-1蛋白的胞外结构域在本发明中，lrig-1蛋白是由存在于调节性t免疫细胞表面的1091个氨基酸组成的跨膜蛋白，其是由富含亮氨酸的重复序列(lrrs)和细胞外或管腔侧的三个免疫球蛋白样结构域、细胞跨膜序列和胞质尾区组成。lrig基因家族包括lrig1、lrig2和lrig3，它们之间的氨基酸高度保守。lrig1基因在正常皮肤中高度表达，并可在基底细胞和毛囊细胞中表达，以调节上皮干细胞的增殖。在本发明的一个示例中，lrig-1蛋白的胞外结构域可以是来源于哺乳动物的lrig-1蛋白的胞外结构域，所述哺乳动物包括灵长类动物如人类和猴子，啮齿类动物如小鼠和大鼠等。就本发明的目的来说，lrig-1蛋白的胞外蛋白可以是，但不限于，来源于人或小鼠的lrig-1蛋白的胞外结构域。在本发明的一个实例中，lrig-1蛋白的胞外结构域可以由，但不限于，seqidno:1表示，其对应于人源性lrig-1蛋白的氨基酸35～794的序列，并且可以由seqidno:2表示的核酸序列编码(见表1)。[表1]在本发明的另一个示例中，lrig-1蛋白的胞外结构域可以由，但不限于，seqidno:3表示，其对应于小鼠来源的lrig-1蛋白的氨基酸35～794的序列，并且可以由seqidno:4表示的核酸序列编码(见表2)。[表2]免疫球蛋白fc区如本文所用，术语“免疫球蛋白fc区”是指免疫球蛋白的一个区域，其包括重链恒定区2(ch2)和/或重链恒定区3(ch3)，不包括重链可变区和轻链可变区。免疫球蛋白fc区可以是构成本发明蛋白质组合的一部分的组分。在本发明中，免疫球蛋白fc区可以包括重链恒定区中的铰链部分，以便不仅可以影响最终制备的融合蛋白的结构灵活性，而且可以进一步增加融合蛋白的生产率和稳定性。然而，本发明不限于此。此外，本发明的免疫球蛋白fc区可以是免疫球蛋白的延伸fc区，其包括重链恒定区1(ch1)和/或轻链恒定区1(cl1)中的部分或全部，仅不包括重链可变区和轻链可变区，只要免疫球蛋白fc区与其原生型相比具有基本相同或改善的效果。此外，免疫球蛋白fc区可以是通过除去相当长的对应于ch2和/或ch3的部分氨基酸序列而获得的区域。例如，本发明的免疫球蛋白fc区可以是：1)ch1结构域、ch2结构域、ch3结构域和ch4结构域；2)ch1结构域和ch2结构域；3)ch1结构域和ch3结构域；4)ch2结构域和ch3结构域；5)免疫球蛋白铰链区(或铰链区的一部分)与ch1结构域、ch2结构域、ch3结构域和ch4结构域的一个或两个或多个结构域的组合；和6)由重链恒定区和轻链恒定区中的每个结构域形成的二聚体。然而，本发明不限于此。在本发明中，本发明的免疫球蛋白fc区包括其天然氨基酸序列及其序列衍生物。氨基酸序列衍生物是指通过缺失、插入或至少一个氨基酸残基的非保守或保守取代或其组合而不同于其天然氨基酸序列的氨基酸序列。在本发明中，例如，对于iggfc来说，已知对结合十分重要的214～238、297～299、318～322或327～331位的氨基酸残基可用作合适的修饰位点。在本发明中，多种类型的衍生物都是可行的，包括通过缺失能够形成二硫键的位点获得的衍生物、通过缺失天然fc的n末端的一些氨基酸残基获得的衍生物、通过在天然fc的n末端添加甲硫氨酸残基获得的衍生物等。此外，为了去除其中的效应子功能，可以删除补体结合位点，例如c1q结合位点，或者可以删除抗体依赖性细胞介导的细胞毒性(adcc)位点。公开号为wo97/34631和wo96/32478等的国际专利公开了制备免疫球蛋白fc区的这种序列衍生物的技术。在本发明中，本领域公知的，蛋白质和肽中的氨基酸交换在整体上不改变分子活性(h.neurath,r.l.hill，《蛋白质》，学术出版社，纽约，1979)。最常见的交换发生在氨基酸残基ala/ser、val/ile、asp/glu、thr/ser、ala/gly、ala/thr、ser/asn、ala/val、ser/gly、thy/phe、ala/pro、lys/arg、asp/asn、leu/ile、leu/val、ala/glu或asp/gly之间。根据具体情况，修饰可以通过磷酸化反应、硫酸化反应、丙烯酰化反应、糖基化反应、甲基化反应、法尼基化反应、乙酰化反应、酰胺化反应等来实现。在本发明中，上述fc衍生物表现出了与本发明的fc区等同的生物活性，并且其可以是那些对热、ph等具有增强的结构稳定性的衍生物。在本发明中，fc区可以从动物体内分离的原生型中获得，所述动物如人、牛、山羊、猪、小鼠、兔子、仓鼠、大鼠或豚鼠的，或者可以是从转化的动物细胞或微生物或其衍生物中获得的重组体。这里，从原生型获得fc区的方法可以是从活的人或动物体中分离整个免疫球蛋白，然后用蛋白酶处理以获得fc区的方法。在用木瓜蛋白酶处理的情况下，整个免疫球蛋白被切割成fab和fc；在用胃蛋白酶处理的情况下，整个免疫球蛋白被切割成pf'c和f(ab)2。可以使用尺寸排阻色谱法等分离fc或pf'c。在一个更具体的实施方式中，免疫球蛋白fc区是使用人源化的或小鼠衍生的fc区从微生物中获得的重组免疫球蛋白fc区。在本发明中，免疫球蛋白fc区可以具有原生型聚糖，或者具有与原生型相比更高的或更低的聚糖水平，或者可以是去糖基化的形式。常规方法如化学方法、酶方法和使用微生物的基因工程方法可用于增加或减少免疫球蛋白fc中的聚糖或去糖基化。此处，已经去除聚糖的免疫球蛋白fc区表现出显著降低的与补体(c1q)结合的能力，并降低或消除了抗体依赖性细胞毒性或补体依赖性细胞毒性；因此不会在体内引起任何不必要的免疫反应。从这个观点来看，去糖基化或糖基化的免疫球蛋白fc区将是更适合作为本发明的原始目的，即药物载体。如本文所用，术语“去糖基化”是指被酶促去除糖的fc区，术语“糖基化”是指在更具体的实施方式中，在原核生物即大肠杆菌中产生的未糖基化的fc区。同时，免疫球蛋白fc区可以源自人或其他动物，如牛、山羊、猪、小鼠、兔子、仓鼠、大鼠和豚鼠。在一个更具体的实施方式中，其来源于人类或小鼠。此外，本发明的免疫球蛋白fc区可以是igg-，iga-，igd-，ige-，或igm-衍生的fc区，重链恒定区2(ch2)，重链恒定区3(ch3)，铰链区及其片段，或其组合，或包括该组合的杂化fc。同时，如本文所用，术语“组合”是指编码相同来源的单链免疫球蛋白fc区、重链恒定区2(ch2)或重链恒定区3(ch3)的多肽，其具有相同的来源，当它们形成二聚体或多聚体时，与不同来源的单链多肽形成键。也就是说，可以从选自igg-、iga-、igm-、igd-或ige-衍生的fc区、重链恒定区2(ch2)或重链恒定区3(ch3)的两个或多个片段制备二聚体或多聚体。在本发明中，“杂化fc”可以来源于人igg亚类的组合或人igd和igg的组合。在一个实施方式中，杂化fc可以包括例如igd铰链区和ch2氮端区+ig4ch2和ch3区。例如，在no.0897938号韩国专利(该专利在此引入作为参考)中公开的杂化fc形式可以以相同的方式被采用和使用。在本发明中，在杂化fc结合生物活性分子、多肽等的情况下，当多肽由编码fc-多肽融合蛋白的核苷酸序列表达时，它具有增加生物活性分子的血清半衰期的效果以及增加多肽表达水平的效果。作为本发明的一个示例，免疫球蛋白fc区可以是igg-、iga-、igm-、igd-或ige-衍生的fc区，或者可以包括igg-、iga-、igm-、igd-或ige-衍生的重链恒定区2(ch2)和重链恒定区3(ch3)。然而，本发明不限于此。作为本发明的一个示例，免疫球蛋白fc区可以是在人血液中最丰富的igg-或igm-衍生的fc区，或者可以包括igg-或igm-衍生的重链恒定区2(ch2)和重链恒定区3(ch3)。作为另一个示例，免疫球蛋白fc区可以是已知可以增强配体结合蛋白半衰期的igg衍生的fc区，或者可以包括igg衍生的重链恒定区2(ch2)和重链恒定区3(ch3)。作为又一个示例，免疫球蛋白fc区可以是igg1-、igg2-、igg3-、或igg4-衍生的fc区，或者可以包括igg1-、igg2-、igg3-、或igg4-衍生的重链恒定区2(ch2)和重链恒定区3(ch3)。作为又一个示例，免疫球蛋白fc区可以包括igg1-或igg2-衍生的重链恒定区2(ch2)和重链恒定区3(ch3)。作为本发明的优选示例，免疫球蛋白fc区可包括，但不限于，人igg1衍生的重链恒定区2(ch2)和重链恒定区3(ch3)，其由seqidno:5表示，或包括小鼠igg2衍生的重链恒定区2(ch2)和重链恒定区3(ch3)，其由seqidno:6表示(见下表3)。[表3]作为本发明的一个示例，免疫球蛋白fc区可以包括igg-、iga-、igm-、igd-、ige-、或阿巴西普(abatacept)衍生的铰链区；作为另一个示例，免疫球蛋白fc区可以包括igg-、igd-、或阿巴西普衍生的铰链区，或者可以包括igg1-、igg2-、igg3-、igg4-、igd-、或阿巴西普衍生的铰链区。然而，本发明不限于此。作为本发明的优选实例，免疫球蛋白fc区可以包括一个或多个选自下组的区域，该组包括：由seqidno:7表示的人igg1衍生的铰链区、由seqidno:8表示的小鼠igg2衍生的铰链区、由seqidno:9表示的人类igd衍生的铰链区、和由seqidno:10表示的阿巴西普的铰链区(见下表4)，从而增加最终制备的融合蛋白的结构灵活性，并显著提高融合蛋白的生产率和稳定性。然而，本发明不限于此。[表4]在本发明中，在lrig-1蛋白的胞外结构域和fc区通过接头连接的情况下，接头可以连接到fc片段的氮末端、碳末端或自由基，并且可以连接到lrig-1蛋白的胞外结构域的氮末端、碳末端或自由基。在接头是肽接头的情况下，连接可以发生在任何位点。例如，接头可以连接到lrig-1蛋白胞外结构域的碳末端和免疫球蛋白fc区的氮末端，或者可以连接到免疫球蛋白fc区的碳末端和lrig-1蛋白胞外结构域的氮末端。连接物在本发明中，“接头”可以减少融合蛋白中lrig-1蛋白胞外结构域和免疫球蛋白fc区之间的干扰，从而增加目标细胞中lrig-1蛋白胞外结构域的所需活性。此外，在本发明中，接头可包括可被目标疾病组织或细胞中过表达的酶切割的序列。在接头可以被上述过表达的酶切割的情况下，可以有效地防止多肽的活性由于fc部分而降低的情况。作为本发明的实例，接头优选具有1～100个氨基酸；然而，本发明不限于此。可以使用任何能够从免疫球蛋白fc区分离lrig-1蛋白胞外结构域的肽。虽然对构成接头的氨基酸序列没有特别的限制，但是优选包括甘氨酸和丝氨酸，或者以重复或随机的方式包括它们。作为这样的示例，接头可以包括由seqidno:11和seqidno:12表示的肽接头中的至少一种(见下表5)，或者可以是选自包含肽接头的组中的至少一种，每个肽接头包含式1至式4中任一个表示的氨基酸序列。[式1](g)n；[式2](ggggs)m；[式3](eaaak)p；[式4](xp)q；其中所述n、m和p各自独立地为1或更大的整数；q是5～40的整数；x是选自a(ala)、c(cys)、d(asp)、e(glu)、f(phe)、g(gly)、h(his)、i(ile)、k(lys)、l(leu)、m(met)、n(asn)、o(pyl)、p(pro)、q(gln)、r(arg)、s(ser)、t(thr)、u(sec)、v(val)、w(trp)和y(tyr)中的任意一种氨基酸。[表5]seqidno序列信息seqidno:11gsseqidno:12ggg在本发明中，式1-3中的n、m和q可以是，但不限于，1或更大的整数，优选1～20的整数。在本发明中，式4中的x可以是a(ala)，但不限于此。此外，作为本发明的一个示例，接头可以包括至少一种选自，但不限于，由seqidno:96表示的肽接头(a(eaaak)4alea(eaaak)4a)、由seqidno:97表示的肽接头(papap)、由seqidno:98表示的肽接头(aeaaakeaaaka)、由seqidno:99表示的肽接头(iegrmd)、和由seqidno:100表示的肽接头(diegrmd)。在本发明中，在融合蛋白进一步包括肽接头的情况下，可以增加细胞中活性物质的稳定性，同时进一步提高其生产率。此外，作为本发明中接头的示例，可以采用这样的肽接头，即由位于人白蛋白282～314位的33个氨基酸组成，更优选地由位于292～304位的13个氨基酸组成，所述人白蛋白在血液中含量最高。从三维结构来看，这部分中的大部分暴露于外部，因此在体内诱导免疫反应的可能性最小。然而，本发明不限于此。此外，在本发明中，在接头和fc区分别表达然后彼此连接的情况下，接头可以是本领域已知的交联剂。交联剂可以是例如1,1-双(重氮乙酰基)-2-苯基乙烷、戊二醛、n-羟基琥珀酰亚胺酯(如4-叠氮水杨酸)、包括二琥珀酸亚胺酯(如3,3’-二硫代双(琥珀酰亚胺基丙酸酯))的酰亚胺酯、和双官能马来酰亚胺(如双-n-马来酰亚胺-1,8-辛烷)。然而，交联剂不限于此。包含lrig-1胞外结构域和免疫球蛋白的融合蛋白作为本发明提供的融合蛋白的一个示例，融合蛋白包括由seqidno:1表示的lrig-1蛋白的胞外结构域；由seqidno:7至seqidno:10中的任何一个表示的铰链区；并且可以采用由seqidno:5表示的人igg1衍生的重链恒定区2(ch2)和重链恒定区3(ch3)(见下表6)。下面表6中由seqidno:13至seqidno:16表示的融合蛋白可以由下面表7中由seqidno:17至seqidno:20表示的核酸序列编码(见下表7)。[表6][表7]本发明提供的融合蛋白的一个示例是，一种融合蛋白，包括由seqidno:3表示的lrig-1蛋白的胞外结构域；由seqidno:7至seqidno:10中的任何一个表示的铰链区；可以采用由seqidno:5表示的人igg1衍生的重链恒定区2(ch2)和重链恒定区3(ch3)(见下表8)。下表8中由seqidno:21至seqidno:24表示的融合蛋白可以由下表9中由seqidno:25至seqidno:28表示的核酸序列编码(见下表9)。[表8][表9]作为本发明提供的融合蛋白的另一个示例，融合蛋白包括由seqidno:3表示的lrig-1蛋白的胞外结构域；由seqidno:7至seqidno:10中的任何一个表示的铰链区；和可以采用由seqidno:6表示的小鼠igg2衍生的重链恒定区2(ch2)和重链恒定区3(ch3)(见下表10)。下表10中由seqidno:29至seqidno:32表示的融合蛋白可以由下表11中由seqidno:33至seqidno:36表示的核酸序列编码(见下表11)。[表10][表11]作为本发明提供的融合蛋白的又一个示例，融合蛋白包括由seqidno:1表示的lrig-1蛋白的胞外结构域；由seqidno:11表示的接头；由seqidno:7至seqidno:10中的任何一个表示的铰链区；并且可以采用由seqidno:5表示的人igg1衍生的重链恒定区2(ch2)和重链恒定区3(ch3)(见下表12)。下表12中由seqidno:37至seqidno:40表示的融合蛋白可以由下表13中由seqidno:41至seqidno:44表示的核酸序列编码(见下表13)。[表12][表13]作为本发明提供的融合蛋白的又一个示例，融合蛋白包括由seqidno:3表示的lrig-1蛋白的胞外结构域；由seqidno:11表示的接头；由seqidno:7至seqidno:710中的任何一个表示的铰链区；并且可以采用由seqidno:5表示的人igg1衍生的重链恒定区2(ch2)和重链恒定区3(ch3)(见下表14)。下面表14中由seqidno:45至seqidno:48表示的融合蛋白可以由下面表15中由seqidno:49至seqidno:52表示的核酸序列编码(见下表15)。[表14][表15]作为本发明提供的融合蛋白的又一个示例，融合蛋白包括由seqidno:3表示的lrig-1蛋白的胞外结构域；由seqidno:11表示的接头；由seqidno:7至seqidno:10中的任何一个表示的铰链区；并且可以采用由seqidno:6表示的小鼠igg2衍生的重链恒定区2(ch2)和重链恒定区3(ch3)(见下表16)。下面表16中由seqidno:53至seqidno:56表示的融合蛋白可以由下表17中由seqidno:57至seqidno:60表示的核酸序列编码(见下表17)。[表16][表17]作为本发明提供的融合蛋白的又一个示例，融合蛋白包括由seqidno:1表示的lrig-1蛋白的胞外结构域；由seqidno:12表示的接头；由seqidno:11表示的接头；由seqidno:7至seqidno:10中的任何一个表示的铰链区；并且可以采用由seqidno:5表示的人igg1衍生的重链恒定区2(ch2)和重链恒定区3(ch3)(见下表18)。下表18中由seqidno:61至seqidno:64表示的融合蛋白可以由表19中由seqidno:65至seqidno:68表示的核酸序列编码(见下表19)。[表18][表19]作为本发明提供的融合蛋白的又一个示例，融合蛋白包括由seqidno:3表示的lrig-1蛋白的胞外结构域；由seqidno:12表示的接头；由seqidno:11表示的接头；由seqidno:7至seqidno:10中的任何一个表示的铰链区；并且可以采用由seqidno:5表示的人igg1衍生的重链恒定区2(ch2)和重链恒定区3(ch3)(见下表20)。下表20中由seqidno:69至seqidno:72表示的融合蛋白可以由下表21中由seqidno:73至seqidno:76表示的核酸序列编码(见下表21)。[表20][表21]作为本发明提供的融合蛋白的又一个示例，融合蛋白包括由seqidno:3表示的lrig-1蛋白的胞外结构域；由seqidno:12表示的接头；由seqidno:11表示的接头；由seqidno:7至seqidno:10中的任何一个表示的铰链区；并且可以采用由seqidno:6表示的小鼠igg2衍生的重链恒定区2(ch2)和重链恒定区3(ch3)(见下表22)。下面表22中由seqidno:77至seqidno:80表示的融合蛋白可以由下表23中由seqidno:81至seqidno:84表示的核酸序列编码(见下表23)。[表22][表23]2)核酸分子本发明的组合物包含编码本发明提供的融合蛋白的核酸分子。本发明的核酸分子包括通过将本发明提供的融合蛋白的氨基酸序列转化为本领域技术人员已知的多核苷酸序列而获得的任何核酸分子。因此，由于开放阅读框(orf)的原因，可以制备多种多核苷酸序列，所有这些也包括在本发明的核酸分子中。3)表达载体本发明的组合物包含表达载体，其中插入了本发明提供的分离的核酸分子。在本发明中，“载体”是能够运输可与其连接的另一种核酸的核酸分子。一种载体是“质粒”，它是指可以连接额外dna片段的环状双链dna。另一种载体是噬菌体载体。还有另一种类型的载体是病毒载体，其中额外的dna片段可以连接到病毒基因组中。某些载体能够在引入它们的宿主细胞中自主复制(例如，细菌载体是具有细菌复制起点的游离哺乳动物载体)。其他载体(例如，非游离哺乳动物载体)在导入宿主细胞后可整合到宿主细胞的基因组中，并因此与宿主基因组一起复制。此外，某些载体能够指导与其有效连接的基因的表达。这种载体在本文中被称为“重组表达载体”或简称为“表达载体”。通常，在重组dna技术中有用的表达载体通常是质粒的形式。在本说明书中，“质粒”和“载体”可以互换使用，因为质粒是最常用的载体形式。本发明中表达载体的具体实例可以选自，但不限于，商业上广泛使用的pcdna载体、f、r1、rp1、col、pbr322、tol、ti载体；粘粒、噬菌体(如λ噬菌体)、λ噬菌体、m13、mu、p1p22、qμ、t-偶数(t-even)、t2、t3、t7；植物病毒。本领域技术人员已知的任何可作为表达载体的表达载体都可以用于本发明，并且可以根据目标宿主细胞的性质选择表达载体。可以通过磷酸钙转染、病毒感染、deae-葡聚糖介导的转染、脂质体转染或电穿孔将载体引入宿主细胞。然而，本发明不限于此，本领域技术人员可以采用和使用适合于所用表达载体和宿主细胞的导入方法。载体可以优选包含至少一个选择标记。然而，本发明不限于此，并且可以使用不包含选择标记的载体进行选择，这取决于是否产生了产品。根据目标宿主细胞进行选择标记的选择，这是使用本领域技术人员已知的方法完成的，因此本发明对此没有限制。为了便于纯化本发明的核酸分子，可以将标签序列插入并融合到表达载体中。所述标签包括，但不限于，六组氨酸标签、血凝素标签、myc标签或flag标签，并且本领域技术人员已知的有助于纯化的任何标签可用于本发明。4)宿主细胞本发明的组合物包含用本发明提供的表达载体转染得到的宿主细胞。在本发明中，“宿主细胞”包括单个细胞或细胞培养物，它们可能会或已经是用于掺入多肽插入物的载体的受体。宿主细胞包括单个宿主细胞的后代，由于自然突变、偶然突变或有意突变，后代可能不一定与原始亲本细胞完全相同(在形态学或基因组dna互补方面)。宿主细胞包括用本文的多核苷酸进行体内转染得到的细胞。在本发明中，宿主细胞可以包括哺乳动物、植物、昆虫、真菌或细胞来源的细胞，并且可以是例如细菌细胞，例如大肠杆菌、链霉菌、鼠伤寒沙门氏菌；真菌细胞，如酵母细胞和毕赤酵母；昆虫细胞如果蝇和甜菜夜蛾sf9细胞；动物细胞如中国仓鼠卵巢(cho)细胞、sp2/0(小鼠骨髓瘤)、人淋巴母细胞、cos、nso(小鼠骨髓瘤)、293t、bowes黑色素瘤细胞、ht-1080、幼仓鼠肾(bhk)细胞、人胚胎肾(hek)细胞或perc.6(人视网膜细胞)，或者植物细胞。然而，宿主细胞不限于此，本领域技术人员已知的可用作宿主细胞系的任何细胞都可用作宿主细胞。5)与t细胞激活的v结构域免疫球蛋白抑制剂(vista)的组合在本发明中，所述组合物可以进一步包含t细胞活化的v结构域ig抑制剂(vista)或其片段。在本发明中，所述组合物可以进一步包含融合蛋白，所述融合蛋白包括vista或其片段和免疫球蛋白fc区。这里，vista或其片段和免疫球蛋白fc区之间还可以包含接头。在本发明中，“t细胞活化的v-结构域ig抑制剂(vista)”对应免疫检查点蛋白，其功能是抑制针对t细胞的免疫活性。vista相当于一种表面蛋白，它包括一个含有igg-v结构域的胞外结构域和一个不含itam和itim的短胞质结构域。vista可以在cd11b+髓样树突状细胞(dc)、cd4+和cd8+t细胞、foxp3+cd4+调节性t细胞中表达，并可用于抑制t细胞活化后细胞因子的分泌和增殖。vista缺陷敲除的小鼠由于慢性炎症表现出器官功能的下降，并且表现出多发性硬化症状的速度比正常小鼠快得多。在本发明的一个示例中，vista可以来源于哺乳动物，包括灵长类动物如人类和猴子，啮齿类动物如小鼠和大鼠等。在本发明的一个示例中，vista可能由seqidno:85表示的氨基酸序列组成，其是人来源的vista，或者可以由seqidno:87表示的核苷酸编码。然而，本发明不限于此。在本发明的一个示例中，vista可由seqidno:86表示的氨基酸序列组成，其是小鼠衍生的vista，或者可由seqidno:88表示的核苷酸编码。然而，本发明不限于此。在本发明的一个示例中，vista的片段可以是，但不限于，vista的胞外结构域。在本发明的一个示例中，vista的胞外结构域可以由，但不限于，seqidno:89表示的氨基酸序列组成，该氨基酸序列对应于人来源的vista的氨基酸33～194的序列。在本发明的一个示例中，vista的胞外结构域可以由，但不限于，seqidno:90表示的氨基酸序列组成，其对应于小鼠来源的vista的氨基酸33～191的序列。在本发明的一个示例中，vista的片段可以是，但不限于，vista胞外结构域的片段。在本发明中，vista胞外结构域的片段可以由seqidno:91至seqidno:93中任一个表示的氨基酸序列组成，所述氨基酸序列是人来源的vista胞外结构域的一些片段。然而，本发明不限于此。在本发明中，vista胞外结构域的片段可以由seqidno:94或seqidno:95表示的氨基酸序列组成，该氨基酸序列是小鼠来源的vista胞外结构域的片段。然而，本发明不限于此。在此，免疫球蛋白fc区和接头的描述与上述内容重叠，因此将被省略以避免说明书过于复杂。在本发明中，vista或其片段或包含其的融合蛋白可以通过在宿主细胞中插入表达载体而容易地获得，所述表达载体中插入核酸分子，所述核酸分子通过将本发明中提供的氨基酸序列转化为本领域技术人员已知的多核苷酸序列，培养宿主细胞，然后使用色谱法等进行纯化而获得。这里，核酸分子、表达载体和宿主细胞的描述也与上述内容重叠，因此将被省略以避免说明书过于复杂。6)免疫相关疾病及组合免疫相关疾病在本发明中，“免疫相关疾病”是由各种免疫细胞，例如效应t细胞或细胞毒性t细胞和炎症细胞的过度激活和/或增殖引起的疾病，并且可以包括但不限于自身免疫性疾病、移植物抗宿主病、器官移植排斥病、哮喘、特应性，或者急性或慢性炎症性疾病。在本发明中，“自身免疫性疾病”可以是选自但不限于类风湿性关节炎、1型糖尿病、系统性硬皮病、系统性红斑狼疮、特应性皮炎、牛皮癣、斑秃、哮喘、克罗恩病、白塞病、干燥综合征、吉兰-巴雷综合症、慢性甲状腺炎、多发性硬化、多发性肌炎、强直性脊柱炎、纤维肌炎和结节性多动脉炎中的至少一种。此外，在本发明中，“自身免疫性疾病”可以由活化的t细胞渗透构成神经的细胞从而诱导炎症或凋亡的过程引起，并且可以是例如神经退行性疾病或神经炎症性疾病(参见neuromolecularmed.2005；7(3):255-64)。在本发明中，神经退行性疾病或神经炎症性疾病可以选自但不限于中风、痴呆、阿尔茨海默病、帕金森病、亨廷顿病、niemann-pick病、朊病毒病、库贾氏病、额颞叶痴呆、路易斯痴呆、肌萎缩性侧索硬化、副癌综合征、皮质基底节变性、多系统萎缩、进行性核麻痹、神经系统自身免疫性疾病、脊髓小脑性共济失调、炎性和神经性疼痛、脑血管疾病、脊髓损伤和tau蛋白病的至少一种。在本发明中，与健康对照相比，免疫相关疾病，例如自身免疫性疾病，可由疾病患者中高频率的自身免疫性t细胞(例如效应t细胞或细胞毒性t细胞)的存在或其活性显著增加而引起，这反过来诱导过度的免疫反应或破坏特定器官的细胞(参见clinical&experimentalimmunology,180:353-360.,immunity,vol.17,1-6,july,2002.,annrheumdis2004；63(supplii):96-101.,immunolres.2013december；57(0):12-22)。在本发明中，可以通过干扰对t细胞(例如，效应t细胞或细胞毒性t细胞)的活化和/或增殖至关重要的细胞内信号途径来预防、改善或治疗免疫相关疾病，所述细胞内信号途径优选为自动反应性t细胞(参见annrheumdis2004；63(supplii):96-101)。具体而言，本发明的融合蛋白可以在效应t细胞中诱导共抑制信号，从而抑制效应t细胞的增殖并调节其活化过程。因此，融合蛋白可用于有效预防、改善或治疗各种免疫相关疾病，这些疾病可能由t细胞(例如，效应t细胞或细胞毒性t细胞)的过度激活和/或增殖引起。与免疫相关疾病的治疗剂的组合本发明的组合物可与其它药物联合使用，用于治疗免疫相关疾病。例如，可以用本发明至少一些实施方式的分子，连同(但不限于)免疫抑制剂如皮质类固醇、环孢菌素、环磷酰胺、泼尼松、硫唑嘌呤、甲氨蝶呤、雷帕霉素和他克莫司，生物制剂如tnf-α阻断剂或拮抗剂，或任何其它靶向任何炎性细胞因子的生物制剂，非甾体抗炎药/cox-2抑制剂，羟氯喹，柳氮磺胺吡啶，金盐，依那西普，英夫利昔单抗，霉酚酸酯、巴西利昔单抗、阿他西普、利妥昔单抗、环磷酰胺、干扰素β-1a、干扰素β-1b、醋酸格拉替雷、盐酸米托蒽醌、阿那白滞素和/或其他生物物质和/或静脉注射免疫球蛋白(ivig)。这种已知治疗剂的非限制性例子包括干扰素，如干扰素-β-1a(和)和干扰素-β-1b(和)；一种多肽–醋酸格拉替雷那他珠单抗和细胞毒剂–米托蒽醌此外，本发明的组合物可以与任何已知的治疗多发性硬化的治疗剂或方法结合使用。用于治疗多发性硬化症的所述已知治疗剂或方法的非限制性例子包括干扰素，例如干扰素-β-1a(和)和干扰素-β-1b(和)；一种多肽–醋酸格拉替雷那他珠单抗和细胞毒剂–米托蒽醌氨吡啶其他药物包括皮质类固醇、甲氨蝶呤、环磷酰胺、硫唑嘌呤和静脉注射免疫球蛋白(ivig)、肌苷、奥沙利珠单抗(r1594)、米力奈mylinax(caldribine)、阿仑单抗(campath)、达克珠单抗(zenapax)、panaclar/富马酸二甲酯(bg-12)、特立氟胺(hmr1726)、芬戈莫德(fty720)、拉喹莫德(abr216062)以及造血干细胞移植、neurovx、利妥昔单抗(rituxan)、卡介苗、低剂量纳曲酮、驱虫疗法、血管成形术、静脉支架、和替代疗法例如维生素d、多不饱和脂肪和医用大麻。此外，本发明的组合物可以与任何已知的治疗类风湿性关节炎的治疗剂或方法结合使用。用于治疗类风湿性关节炎的所述已知治疗剂或方法的非限制性实例包括糖皮质激素、非甾体抗炎药(nsaid)如水杨酸盐或环加氧酶-2抑制剂、布洛芬和萘普生、双氯芬酸、吲哚美辛、依托度酸；改善病情的抗风湿药(dmards)-口服dmards:醋硫葡金硫唑嘌呤环孢菌素(and每种都是通用的)、d-青霉胺羟氯喹im硫代苹果酸金钠金硫代葡萄糖来氟米特甲氨蝶呤米诺环素葡萄球菌蛋白a免疫吸附(柱)、柳氮磺吡啶生物dmards:tnf-α阻断剂，包括阿达木单抗依那西普英夫利昔单抗戈利木单抗赛妥珠单抗和其他生物dmards，阿那白滞素利妥昔单抗拖珠单抗cd28抑制剂，包括阿巴西普和贝拉西普。此外，本发明的组合物可以与任何已知的1型糖尿病治疗剂或方法结合使用。用于治疗1型糖尿病的所述已知治疗剂或方法的非限制性实例包括胰岛素、胰岛素类似物、胰岛移植、包括在内的干细胞疗法、非胰岛素疗法例如il-1β抑制剂包括阿那白滞素阿巴西普diamyd、阿法西普奥替利单抗、diapep277(hsp60衍生肽)、α1-抗胰蛋白酶、泼尼松、硫唑嘌呤、环孢素、e1-int(一种包含表皮生长因子类似物和胃泌素类似物的可注射胰岛新生疗法)、他汀类药物包括(二肽酶(dpp-4)抑制剂)、抗cd3单抗(例如替普珠单抗)；ctla4-ig(阿巴西普)、抗il-1β(康纳单抗)、抗cd20单抗(如利妥昔单抗)。此外，本发明的组合物可以与任何已知的治疗干燥综合征的治疗剂或方法结合使用。用于治疗干燥综合征的所述已知治疗剂或方法的非限制性实例包括环孢菌素、匹鲁卡品和西维美林羟氯喹可的松(泼尼松等)和/或硫唑嘌呤或环磷酰胺地塞米松、沙利度胺、脱氢表雄酮、ngx267、瑞巴派特、fid114657、依那贝利单抗、(利妥昔单抗)，静脉注射免疫球蛋白(ivig)，同种异体间充质干细胞(allomscs)，通过“saliwellcrown”自动神经电刺激。此外，本发明的组合物可以与任何已知的治疗系统性红斑狼疮的治疗剂或方法结合使用。用于治疗系统性红斑狼疮的所述已知治疗剂或方法的非限制性实例包括皮质类固醇和改善病情的抗风湿药(dmards)、通常的抗疟疾药(如羟氯喹)和免疫抑制剂(如氨甲喋呤和硫唑嘌呤)羟氯喹、细胞毒性药(如环磷酰胺和霉酚酸酯)、羟氯喹(hcq)、贝利司他(贝利单抗)、非甾体抗炎药、泼尼松、麦考酚酸莫酯、他克莫司、阿塞西普、鲁普唑、静脉注射免疫球蛋白(ivig)、(霉酚酸酯)、ctla4-igg4m(rg2077)、利妥昔单抗、奥瑞珠单抗、依帕珠单抗、cnto136、西法木单抗(medi-545)、a-623(以前的amg623)、amg557、隆利组单抗、帕喹莫德(abr-215757)、ly2127399、cep-33457、脱氢表雄酮、左旋甲状腺素、阿贝莫司纳(ljp394)、美金刚、阿片类、雷帕霉素、肾移植和干细胞移植。7)术语和组成在本发明中，“预防”可以包括，但不限于，使用本发明的组合物阻断疾病症状或抑制或延迟症状的任何行为。在本发明中，“改善”或“治疗”可以包括，但不限于，使用本发明的组合物改善或有益地改变疾病症状的任何行为。在本发明中，药物组合物可以是胶囊、片剂、颗粒剂、注射剂、药膏、粉剂或饮料的形式，并且药物组合物可以靶向人。在本发明中，药物组合物可以根据常规方法分别配制成口服制剂的形式，例如粉剂、颗粒剂、胶囊、片剂和水悬浮液、外用制剂、栓剂和无菌注射溶液，并使用。然而，药物组合物不限于此。本发明的药物组合物可以进一步包含药学上可接受的载体。作为药学上可接受的载体，粘合剂、助流剂、崩解剂、赋形剂、增溶剂、分散剂、稳定剂、悬浮剂、颜料、香料等可用于口服给药；缓冲剂、防腐剂、止痛剂、增溶剂、等渗剂、稳定剂等可以混合用于注射；并且碱、赋形剂、润滑剂、防腐剂等可以用于局部给药。本发明药物组合物的制剂可以通过与如上所述的药学上可接受的载体混合以多种方式制备。例如，对于口服给药，药物组合物可以配制成片剂、锭剂、胶囊、酏剂、混悬剂、糖浆、薄饼等形式。对于注射给药，药物组合物可以配制成单位剂量安瓿或多种剂型的形式。或者，药物组合物可以配制成溶液、悬浮液、片剂、胶囊、缓释制剂等。同时，作为适于制备制剂的载体、赋形剂或稀释剂的示例，可以使用乳糖、葡萄糖、蔗糖、山梨醇、甘露醇、木糖醇、赤藓糖醇、麦芽糖醇、淀粉、阿拉伯胶、藻酸盐、明胶、磷酸钙、硅酸钙、纤维素、甲基纤维素、微晶纤维素、聚乙烯吡咯烷酮、水、羟基苯甲酸甲酯、羟基苯甲酸丙酯、滑石、硬脂酸镁、矿物油等。此外，可以进一步包含填料、抗凝剂、润滑剂、润湿剂、香料、乳化剂、防腐剂等。在本发明中，药物组合物的给药途径包括但不限于口服、静脉内、肌内、动脉内、髓内、硬膜内、心内、经皮、皮下、腹膜内、鼻内、肠内、局部、舌下或直肠途径。优选口服或肠胃外给药。在本发明中，所述“胃肠外”包括皮下、皮内、静脉内、肌内、关节内、囊内、胸骨内、硬膜内、病变内和颅内注射或输注技术。本发明的药物组合物也可以以用于直肠给药的栓剂的形式给药。本发明的药物组合物可以根据多种因素而有很大变化，包括所使用的某种化合物的活性、患者的年龄、体重、一般健康状况、性别、饮食、给药时间、给药途径、排泄速率、药物组合以及要预防或治疗的某种疾病的严重程度。药物组合物的剂量可以根据患者的病情、体重、疾病的严重程度、药物形式、给药途径和持续时间而变化，并且可以由本领域技术人员适当选择。药物组合物可以以每天0.0001mg/kg～50mg/kg或0.001mg/kg～50mg/kg的量给药。给药可以一天一次或一天几次。该剂量无意以任何方式限制本发明的范围。本发明的药物组合物可以配制成丸剂、糖衣片、胶囊、液体、凝胶、糖浆、浆液或悬浮液的形式。在本发明中，所述食品组合物可以制备成各种食品的形式，例如饮料、树胶、茶、维生素复合物、粉末、颗粒、片剂、胶囊、糖果、米糕、面包等。在本发明中，在食品组合物中含有活性成分的情况下，其添加量可以是，但不限于，食品组合物总重量的0.1％-50％。在本发明中，在食品组合物以饮料形式制备的情况下，除了饮料含有指定比例的食品组合物之外，没有特别的限制，并且饮料可以含有各种调味剂或天然碳水化合物等作为类似于常规饮料的附加成分。具体地，天然碳水化合物的示例可以包括诸如葡萄糖的单糖、诸如果糖的二糖、诸如蔗糖的多糖、诸如糊精和环糊精的常规糖，以及诸如木糖醇、山梨醇和赤藓糖醇的糖醇。调味剂的示例可以包括天然调味剂(甜菊糖、甜叶菊提取物(如莱鲍迪苷a)、甘草甜素等)和合成调味剂(糖精、阿斯巴甜等)。在本发明中，食品组合物可进一步包含多种营养物、维生素、矿物质(电解质)、调味剂如合成调味剂和天然调味剂、着色剂、果胶酸及其盐、海藻酸及其盐、有机酸、保护性胶体增稠剂、ph调节剂、稳定剂、防腐剂、甘油、酒精、碳酸饮料中使用的碳化剂等。在本发明中，上述成分可以单独使用或组合使用。所述添加剂的比例不对应于本发明的关键要素，并且可以选自，但不限于，每100重量份本发明的食品组合物0.1～约50重量份的范围。在本发明中，化妆品组合物可以制备成皮肤软化剂、营养洗剂、营养香精、按摩霜、美容沐浴水添加剂、身体洗剂、身体乳液、沐浴油、婴儿油、婴儿粉、沐浴露、沐浴霜、日晒洗液、日晒霜、晒霜、皮肤洗剂、皮肤霜、紫外线阻挡化妆品、清洁乳液、毛发去除剂(用于美容目的)、面部和身体乳液、面部和身体乳液、皮肤增白乳液、手部乳液、头发乳液、美容乳液，茉莉油、沐浴皂、液体皂、化妆皂、洗发精、洗手液、药用皂(用于非医疗目的)、霜皂、洗面奶、身体清洁剂、头皮清洁剂、洗发香波、香皂、牙齿美白凝胶、牙膏等。本发明的组合物可进一步包含常规用于制备化妆品组合物的溶剂，或合适的载体、赋形剂或稀释剂。在本发明中，可以进一步添加到化妆品组合物中的溶剂的类型没有特别限制，溶剂的示例可以包括水、盐水、二甲基亚砜或其组合。此外，载体、赋形剂或稀释剂的示例包括但不限于纯净水、油、蜡、脂肪酸、脂肪酸醇、脂肪酸酯、表面活性剂、湿润剂、增稠剂、抗氧化剂、粘度稳定剂、螯合剂、缓冲剂、低级醇等。此外，如果需要，本发明的化妆品组合物可以包含增白剂、保湿剂、维生素、紫外线阻断剂、芳香剂、染料、抗生素、抗菌剂和抗真菌剂。在本发明中，油的示例可以包括氢化植物油、蓖麻油、棉籽油、橄榄油、棕榈仁油、荷荷巴油和鳄梨油，蜡的示例可以包括蜂蜡、鲸蜡、巴西棕榈蜡、小烛树蜡、褐煤蜡、地蜡、液体石蜡和羊毛脂。在本发明中，脂肪酸的示例可以包括硬脂酸、亚油酸、亚麻酸和油酸；脂肪酸醇的示例可以包括十六醇、辛基十二醇、油醇、泛醇、羊毛脂醇、硬脂醇和十六醇；脂肪酸酯的示例可以包括肉豆蔻酸异丙酯、棕榈酸异丙酯和硬脂酸丁酯。表面活性剂的示例可以包括本领域已知的阳离子表面活性剂、阴离子表面活性剂和非离子表面活性剂。在这些表面活性剂中，如果可能的话，优选源自天然产物的表面活性剂。此外，本发明的化妆品组合物可以包含湿润剂、增稠剂、抗氧化剂等，它们在化妆品领域是公知的，并且它们的类型和量是本领域已知的2.预防、改善或治疗免疫相关疾病的方法本发明的另一个实施方式提供了一种预防、改善或治疗免疫相关疾病的方法，包括向个体施用本发明的融合蛋白的步骤；编码所述融合蛋白的核酸分子；包含核酸分子的表达载体；或者用表达载体转化得到的宿主细胞；或者包括前述任何一种的组合物。在本发明中，关于融合蛋白、核酸分子、表达载体、宿主细胞、组合物和免疫相关疾病相关的描述与上述药物组合物的描述重叠，因此将被省略以避免说明书过于复杂。在本发明中，“个体”是被怀疑患有免疫相关疾病的个体，被怀疑患有免疫相关疾病的个体是指已经患有或可能患有所述疾病的哺乳动物，例如人类、小鼠和家畜。然而，可以用本发明的融合蛋白或包含该融合蛋白的组合物治疗的任何个体都不受限制地包括在其中。本发明的方法可以包括以药物有效量施用融合蛋白或包含融合蛋白的组合物。主治医师或兽医可在合理的医学判断范围内确定适当的每日总用量，并可一次或多次给药。然而，为了本发明的目的，特定患者的特定治疗有效量优选依据多种因素有区别地应用，所述因素包括要实现的反应的类型和程度，特定组合物包括是否根据具体情况使用其他药剂，患者的年龄、体重、一般健康状况、性别和饮食、给药时间、给药途径、组合物的分泌速率、治疗持续时间、与特定组合物同时或结合使用的药物，以及医学领域中公知的类似因素。同时，一种预防、改善或治疗免疫相关疾病的方法可以是但不限于联合疗法，其进一步包括施用对一种或多种免疫相关疾病具有治疗活性的化合物或物质。在本发明中，“组合”应理解为代表同时、单独或顺序给药。在以顺序或单独方式给药的情况下，第二种成分应间隔给药，以使组合的有益效果不会丧失。在本发明中，融合蛋白的剂量可以是，但不限于，每千克患者体重约0.0001μg至500mg。有益效果本发明提供的融合蛋白与活化的t细胞中存在的lrig-1蛋白的配体相互作用，给活化的t细胞提供共抑制信号，从而诱导活化的t细胞的死亡或抑制的活性，使得有效预防、改善或治疗免疫相关疾病成为可能。附图说明图1示出了本发明一个实施方式中的lrig-1蛋白的结构。图2示出了本发明一个实施方式中的lrig-1蛋白的结构。图3示出了本发明一个实施方式中的lrig-1蛋白的表达水平。图4示出了本发明一个实施方式中的lrig-1mrna的表达水平。图5示出了本发明一个实施方式中的lrig-1mrna的表达水平。图6图示性的示出了通过比较本发明的一个实施方式中的lrig-1、lrig-2和lrig-3mrna的表达水平获得的结果。图7示出了通过比较本发明的一个实施方式中的调节性t细胞和非调节性t细胞中lrig-1蛋白的表达水平获得的结果。图8示出了通过鉴定本发明的一个实施方式中的各种免疫细胞表面上lrig-1蛋白的表达水平获得的结果。图9示出了t细胞的亚群，其中存在可由本发明一个实施方式中的融合蛋白识别的配体。图10示出了在本发明的一个实施方式中，通过使初始t细胞和通过用抗cd3/28抗体活化获得的活化t细胞以各自的浓度用融合蛋白和pd-l1-igg染色而获得的结果。图11示出了在本发明的一个实施方式中，通过对活化的t细胞(act)和th1细胞(th1)进行免疫沉淀，然后用抗vista抗体进行蛋白质印迹分析而获得的结果。图12a和12b分别示出了在本发明的一个实施方式中，通过用抗cd3/28抗体激活t细胞，使vista抗体结合到细胞表面30分钟，用lrig-1-igg对细胞表面进行染色，然后通过流式细胞仪进行分析而获得结果(a)，以及通过使融合蛋白结合到激活的t细胞表面30分钟，用vista抗体对细胞表面进行染色，然后通过流式细胞仪进行分析而获得结果(b)。图13a和13b示出了通过用抗cd3/28抗体活化初始t细胞，每24小时用vista抗体对t细胞表面进行染色，然后通过流式细胞仪测量vista表达水平的变化而获得的结果(a)，以及通过每24小时收集活化t细胞的培养物，然后用vista酶联免疫试剂盒测量vista胞外结构域的表达水平从而测量培养物中存在的胞外结构域的量而获得的结果(b)。图14a和14b图示性的示出了在本发明的一个实施方式中，通过从正常小鼠和已诱发类风湿性关节炎(ra)或炎症性肠病(ibd)的小鼠模型中收集血液，通过离心从其中分离血清，然后使用靶向vista胞外结构域的酶联免疫吸附试验测量血清中vista胞外结构域的浓度而获得的结果。图15示出了在本发明的一个实施方式中，通过活化初始t细胞，然后用流式细胞仪分析在细胞表面诱导的表面蛋白cd25的表达水平获得的结果。图16a、16b、16c和17示出了在本发明的一个实施方式中，通过鉴定本发明的融合蛋白在活化的t细胞中的增殖抑制作用获得的结果。具体实施方式根据本发明的一个实施方式，其提供了一种预防、改善或治疗免疫相关疾病的组合物，其包括作为活性成分的：融合蛋白，所述融合蛋白由seqidno:21表示的氨基酸序列组成；编码所述融合蛋白的核酸分子；包含核酸分子的表达载体；或者用表达载体转化得到的宿主细胞。根据本发明的另一个实施方式，其提供了一种预防、改善或治疗免疫相关疾病的组合物，其包含作为活性成分的：融合蛋白，所述融合蛋白由seqidno:25表示的核苷酸序列编码得到；编码所述融合蛋白的核酸分子；包含核酸分子的表达载体；或者用表达载体转化得到的宿主细胞。在下文中，本发明将通过实施例进行更详细的描述。这些实施例仅用于更详细地描述本发明，并且对于本领域技术人员而言显而易见的是，根据本发明的主旨，本发明的范围不受这些实施例的限制。实施例[制备实施例1]t细胞亚型细胞培养为了确定lrig-1蛋白是否仅在调节性t细胞(treg)中表达，制备了t细胞亚群th0、th1、th2、th17和itreg。与天然分离的ntreg不同，itreg是指在具有以下组分的培养基中人工诱导分化的细胞。通过使用从小鼠脾脏获得的首次分离的初始t细胞诱导t细胞亚群分化为各自的细胞，产生含有10％胎牛血清的rpmi1640(invitrogengibco，grandisland，ny)营养培养基(fbshyclone，logan，ut)，以使其进一步包含下表24的成分，并在37℃，5％co2的培养箱中进行72小时的培养。[表24]分化的细胞组成th0抗-cd3、抗-cd28th1il-12、抗-il-4抗体th2il-4、抗-ifnβth17il-6、tgfβ、抗-ifnβ、抗-il-4itregil-2、tgfβ[实施例1]lrig-1的结构分析预计lrig-1蛋白胞外结构域的三维立体结构将产生包含lrig-1蛋白胞外结构域的融合蛋白，其中所述lrig-1蛋白是调节性t细胞的表面蛋白。首先，为了预测表位的碱基序列，使用了工具uniprot(http://www.uniprot.org)和rcsb蛋白质数据库(http://www.rcsb.org/pdb)来预测lrig-1蛋白的胞外结构域(ecd)的三维立体结构，以便识别ecd的结构。然后，结果在图1和2中示出。如图1所示，lrr1至lrr15共有15个富含亮氨酸的区域存在于lrig-1蛋白胞外结构域的lrig-lrr结构域(41～494位的氨基酸序列)中。每个lrr结构域由23～27个氨基酸组成，其中存在3～5个亮氨酸。此外，如图2所示，三个免疫球蛋白样结构域存在于lrig-1蛋白胞外结构域中lrig-1蛋白第494～781位的氨基酸序列中。[实施例2]调节性t细胞中lrig-1mrna特异性表达的鉴定对lrig-1蛋白是否可以作为调节性t细胞的特异性生物标志物进行了验证。为了验证，使用磁激活细胞分选术(macs)将cd4+t细胞通过cd4珠从小鼠脾脏中分离。随后，用荧光激活细胞分选仪(facs)使用cd25抗体分离调节性t(cd4+cd25+t)细胞和非调节性t(cd4+cd25-t)细胞。对于各个细胞和在制备实施例1中分化的细胞，使用trizol提取mrna，然后根据制造商提供的说明使用gdna提取试剂盒(qiagen)从基因组rna中去除gdna。通过bdsprintcdnasynthesiskit(clonetech)将去除gdna的mrna合成为cdna。采用实时聚合酶链反应(rtpcr)进行cdna中lrig-1mrna表达水平的定量鉴定。使用下表25所示的引物，根据制造商提供的说明，使用sybrgreen(分子探针)在40个循环的条件下进行实时聚合酶链反应，所述循环包括95℃3分钟，61℃15秒，72℃30秒，使用δct方法计算相对基因表达水平，并使用hprt进行标准化。结果如图4～6所示。[表25]如图3所示，可以看出调节性t(cd4+cd25+t)细胞中lrig-1的表达是非调节性t(cd4+cd25-t)细胞的18.1倍。这约是lag3和ikzf4的表达水平的10倍，lag3和ikzf4是以前已知的调节性t细胞的标记。此外，如图4和5所示，与其他类型的免疫细胞相比，调节性t细胞中lrig-1mrna的表达显著更高，并且特别的，与诱导的调节性t细胞相比，天然分离的调节性t细胞中lrig-1mrna的表达显著更高。此外，如图6所示，在对应于lrig家族的lrig-1、lrig-2和lrig-3中，lrig-1的表达水平最高。从上述结果可以看出，本发明的lrig-1蛋白在调节性t细胞，特别是天然存在的调节性t细胞中可以进行特异性表达。[实施例3]调节性t细胞中lrig-1蛋白特异性表达的鉴定已经确定从lrig-1mrna表达的lrig-1蛋白是否仅在调节性t细胞中进行特异性表达。使用foxp3-rfp敲入小鼠，通过将红色荧光蛋白(rfp)偶联到foxp3启动子(一种对调节性t细胞特异的转录因子)获得foxp3-rfp，使用磁激活细胞分选(macs)通过cd4珠从小鼠脾脏分离cd4+t细胞。随后，使用rfp蛋白，通过荧光激活细胞分选仪(facs)进行分离，获得调节性t细胞(cd4+rfp+t)和非调节性t细胞(cd4+rfp-t)。用购买的lrig-1抗体对各自的细胞进行染色，用同种型匹配的对照抗体对阴性对照进行染色，用荧光激活细胞分选仪测量lrig-1的表达水平。结果如图7所示。如图7所示，由虚线表示的非调节性t细胞显示出与阴性对照几乎相同的lrig-1表达水平，而在调节性t细胞中存在大量具有高lrig-1表达水平的细胞。从上述结果可以看出，本发明的lrig-1蛋白在调节性t细胞中可进行特异性表达。[实施例4]在调节性t细胞表面的lrig-1蛋白的特异性表达的鉴定从为了成为细胞治疗的目标这一观点来看，lrig-1蛋白必须在调节性t细胞的表面表达，鉴定了lrig-1蛋白是否可在调节性t细胞的表面表达。用抗cd4-apc和抗lrig-1-pe抗体对制备实施例1的各个分化的t细胞亚群进行染色，并使用荧光激活细胞分选仪(facs)在各个细胞表面测量lrig-1蛋白的表达水平。结果如图8所示。如图8所示，lrig-1在活化的t细胞、th1细胞、th2细胞、th17细胞和初始t细胞中以0.77至15.3的量进行表达，而lrig-1在分化诱导的t细胞(itreg细胞)中表达量高达83.9。从上述结果可以看出，本发明的lrig-1蛋白不仅在调节性t(treg)细胞中可以进行特异性表达，而且特别是在treg细胞表面以更高水平进行特异性表达。[制备实施例]融合蛋白的生产1.表达载体的构建为了生产本发明的融合蛋白，合成了如表26所示的编码各融合蛋白的各核酸序列。在核酸序列的5’端和3’端分别加入nhei和ecori限制性内切酶序列，并在5’端的限制性内切酶序列后插入以下序列：kozak序列(gccacc)，蛋白质翻译的起始密码子，以及允许表达蛋白在细胞外分泌的小鼠iggκ轻链信号肽(atggaaaccgatactctgctgctgtgggtgctgctgctgtgggtgccaggctctaccggg)。随后，如表26所示，在编码每个融合蛋白的核酸序列后插入终止密码子，其中每个融合蛋白包括人源的lrig-1蛋白或vista蛋白的胞外结构域；任选的接头；铰链区；人igg1衍生的重链恒定区2(ch2)和重链恒定区3(ch3)。编码本发明融合蛋白的核酸序列通过使用两个限制性酶序列nhei和ecori克隆到pcdna3.1(+)表达载体中。[表26]2.融合蛋白的纯化用上面编号1中构建的表达载体用聚乙烯亚胺转化293f细胞，然后在37℃和8％co2的条件下培养6天。将培养物上清液过滤，通过蛋白a树脂，用1×pbs洗涤。用0.1m甘氨酸溶液在ph3.5下进行洗脱。然后，向获得的溶液中加入ph9.0的1mtris溶液以中和ph。随后，将该溶液用pbs溶液透析，然后浓缩并使用。[实施例5]本发明的融合蛋白识别的lrig-1配体分布的鉴定为了发现其中存在lrig-1蛋白配体的免疫细胞，诱导被认为是调节性t细胞标靶的初始t细胞分化为活化的t细胞、th1细胞、th2细胞或th17细胞，然后用制备实施例5中的融合蛋白(初级抗体)和抗人pe抗体(次级抗体)对这些分化的细胞进行染色。使用荧光激活细胞分选仪(facs)测量制备实施例5中的融合蛋白结合到各自细胞表面的水平。结果如图9所示。如图9所示，制备实施例5中的融合蛋白几乎不与初始t细胞表面的抗原结合，因此观察到弱染色(0.71％)；并且制备实施例5中的融合蛋白以非常高的水平结合活化的t细胞、th1细胞、th2细胞和th17细胞表面上的抗原，因此观察到96％或更高程度的染色。根据这些结果，可以发现lrig-1蛋白的配体是由t细胞受体刺激诱导的表面蛋白。[实施例6]活化的t细胞中lrig-1蛋白表达水平的鉴定为了进行比较，用pd-l1-igg融合蛋白(产品名称:rmb7-h1/fc嵌合体，由r&dsystems公司制造，类别号:1019-b7)(以下称为“pd-l1-igg”)以浓度相关的方式对初始t细胞和活化的t细胞的表面进行染色，所述融合蛋白可以识别pd-1，其先前已知可在活化的t细胞和t细胞亚群中高度表达，或者在制备实施例5中的融合蛋白中高度表达；并且使用细胞分选仪测量结合到各个细胞表面的制备实施例5中的融合蛋白的水平。结果如图10所示。如图10所示，鉴定出在用制备实施例5中的融合蛋白染色的情况下，与用pd-l1-igg染色的情况下观察到的比例相比，在活化的t细胞的表面上以浓度相关的方式观察到显著高的融合蛋白表达水平。根据这些结果，发现与初始t细胞相比，lrig-1蛋白的配体在活化的t细胞或t细胞亚群的表面上以高表达水平进行表达。[实施例7]活化的t细胞中lrig-1蛋白配体的鉴定在实施例6中，证实了lrig-1蛋白的配体在活化的t细胞表面高度表达的事实。基于这一事实，为了鉴定在活化的t细胞上表达的配体是哪种分子，用制备实施例5中的融合蛋白对活化的t细胞和th1细胞的细胞裂解物进行免疫沉淀。使用lrig-1蛋白候选配体中的各种抗体进行鉴定。因此，蛋白质印迹是通过t细胞活化的v结构域ig抑制因子(vista，一种免疫检查点)的单克隆抗体进行的。结果如图11所示。如图11所示，发现与制备实施例5中的融合蛋白结合的分子是vista。此外，发现在活化的t细胞(act)和th1细胞(th1)中，vista都以非常高的水平与制备实施例5中的融合蛋白结合。从这些结果可以看出，lrig-1蛋白的配体是vista。[实施例8]活化的t细胞中的vista和lrig-1蛋白之间相互作用的鉴定为了鉴定活化的t细胞表面上存在的vista是否直接与lrig-1蛋白相互作用，vista单克隆抗体以浓度相关的方式结合到活化的t细胞表面，然后用制备实施例5中的融合蛋白对活化的t细胞进行染色。然后，用荧光激活细胞分选仪检查染色程度。结果如图12a和12b所示。如图12a所示，发现在细胞表面仅用制备实施例5中的融合蛋白染色的情况下，融合蛋白显示出约95％的结合率，而在用制备实施例5中的融合蛋白染色前vista单克隆抗体以浓度相关性方式结合的情况下，融合蛋白显示出的结合率由于竞争而显著降低。相反，如图12b所示，发现即使在制备实施例5中的融合蛋白首先结合到活化的t细胞的表面，然后vista单克隆抗体结合到其上的情况下，vista染色的速率也降低。从这些结果中，可以发现vista在活化的t细胞表面表达，lrig-1蛋白识别vista并与其相互作用。[实施例9]t细胞表面的vista表达模式的鉴定为了确定vista在t细胞表面的表达模式，用抗cd3/28抗体激活小鼠初始t细胞，然后在各自的时间点检查vista的表达水平。结果如图13a所示。如图13a所示，发现vista的表达水平逐渐增加，直到激活72小时；然而，经过96小时后，其在表面上的表达水平逐渐降低。为了确定上述现象的原因，通过识别vista胞外结构域的酶联免疫吸附试验，在各自的时间点测量活化t细胞的细胞培养基中存在的vista胞外结构域的表达水平。结果如图13b所示。如图13b所示，发现在激活后经过72小时，在培养基中几乎没有检测到vista的胞外结构域；然而，经过96小时后，在培养基中vista胞外结构域的表达水平迅速增加(图13b)。也就是说，从vista胞外结构域的表达水平显示出与活化t细胞表面上存在的vista的表达水平直接相反的模式的观点来看，发现培养基中vista的胞外结构域是通过切割活化t细胞表面上存在的vista而分泌的。[实施例10]vista胞外结构域分泌与自身免疫性疾病发病之间相关性的鉴定为了研究vista胞外结构域的分泌与自身免疫性疾病发病之间的相关性，从小鼠动物模型制备血清，其中所述小鼠动物模型被诱导患有类风湿性关节炎(ra)或炎性肠病(ibd)的自身免疫性疾病，然后通过使用vista特异性抗体的酶联免疫吸附试验分析血清中存在的vista胞外结构域的量。结果如图14所示。如图14所示，发现在诱发类风湿性关节炎或ibd自身免疫性疾病的小鼠血清中，比在正常小鼠血清中检测到更大量的vista胞外结构域。[实施例11]vista胞外结构域分泌与自身免疫性疾病发病之间相关性的鉴定cd4+cd62l+t细胞是初始t细胞，从8周龄c57bl/6小鼠的脾脏中分离，然后使用固定在板上的抗cd3/抗cd28单克隆抗体激活初始t细胞。此后，通过用流式细胞仪分析cd25表面蛋白的表达水平来确定t细胞的活化程度，cd25表面蛋白是通过在t细胞表面诱导表达的。结果如图15所示。如图15所示，对于抑制t细胞活化的对照组，在用环孢菌素(临床实践中使用的免疫抑制剂)处理t细胞的情况下，可以看出t细胞的活化被抑制，导致cd25的表达从43.1％降低到0.33％。从这些结果可以看出，在用作为vista配体的lrig1-igg刺激vista的情况下，在活化的t细胞中诱导共抑制信号，从而显著抑制t细胞的活化，并且制备实施例5中的融合蛋白显示出比刺激pd-1的pd-l1-igg更好的抑制t细胞活化的程度。此外，可以看出，在制备实施例5中的融合蛋白与vista的胞外结构域或其片段联合给药的情况下，或包含vista胞外结构域或其片段和免疫球蛋白的融合蛋白，可以在t细胞中更有效地诱导共抑制信号，从而更有效地诱导t细胞的活化。[实施例12]本发明的融合蛋白对免疫相关疾病的治疗效果cd4+cd62l+t细胞是初始t细胞，从8周龄c57bl/6小鼠的脾脏中分离，然后使用固定在板上的抗cd3/抗cd28单克隆抗体激活初始t细胞。此后，将活化的t细胞分配到96孔板中。然后，用1μg/ml的抗cd3单克隆抗体和制备实施例5中的融合蛋白处理96孔板，所述融合蛋白对应于1μg/ml、5μg/ml或10μg/ml的浓度，然后用csfe染色。然后，在流式细胞仪观察下分析细胞的增殖程度。结果如图16和17所示。这里，作为对照，使用抗flag抗体代替制备实施例5中的融合蛋白。如图17和18所示，在单独用对照和cd3处理的情况下，活化的t细胞的增殖抑制程度最大为7.87％或9.82％，而在用制备实施例5中的融合蛋白lrig-1-igg(ml1-hfc)处理的情况下，活化的t细胞的增殖在5μg/ml的浓度下被抑制18.17％，在10μg/ml的浓度下被抑制47.60％(图17和18)。从这些结果可以看出，在用本发明的融合蛋白处理活化的t细胞的情况下，可以在活化的t细胞中诱导共抑制信号，从而显著抑制t细胞的活化。因此，本发明的融合蛋白可以非常有效地预防、改善或治疗由活化的t细胞引起的免疫相关疾病。尽管上面已经详细描述了本发明，但是本发明的范围不限于此。对于本领域技术人员将显而易见的是，在不脱离权利要求中描述的本发明的技术精神的情况下，可以进行各种修改和改变。工业适用性本发明提供的融合蛋白可以与活化的t细胞中存在的lrig-1蛋白的配体相互作用，以向活化的t细胞提供共抑制信号，从而诱导活化的t细胞的死亡或抑制的活性，这使得该融合蛋白能够非常有效地应用于预防、改善或治疗免疫相关疾病的领域。<110>古德t细胞有限公司<120>一种预防和治疗免疫相关疾病的组合物<130>pdpb187225k01<150>kr2018-0085908<151>2018-07-24<160>100<170>kopatentin3.0<210>1<211>762<212>prt<213>人(homosapiens)<400>1alaglyproargalaprocysalaalaalacysthrcysalaglyasp151015serleuaspcysglyglyargglyleualaalaleuproglyaspleu202530prosertrpthrargserleuasnleusertyrasnlysleuserglu354045ileaspproalaglyphegluaspleuproasnleuglngluvaltyr505560leuasnasnasngluleuthralavalproserleuglyalaalaser65707580serhisvalvalserleupheleuglnhisasnlysileargserval859095gluglyserglnleulysalatyrleuserleugluvalleuaspleu100105110serleuasnasnilethrgluvalargasnthrcyspheprohisgly115120125proproilelysgluleuasnleualaglyasnargileglythrleu130135140gluleuglyalapheaspglyleuserargserleuleuthrleuarg145150155160leuserlysasnargilethrglnleuprovalargalaphelysleu165170175proargleuthrglnleuaspleuasnargasnargileargleuile180185190gluglyleuthrpheglnglyleuasnserleugluvalleulysleu195200205glnargasnasnileserlysleuthraspglyalaphetrpglyleu210215220serlysmethisvalleuhisleuglutyrasnserleuvalgluval225230235240asnserglyserleutyrglyleuthralaleuhisglnleuhisleu245250255serasnasnserilealaargilehisarglysglytrpserphecys260265270glnlysleuhisgluleuvalleuserpheasnasnleuthrargleu275280285aspglugluserleualagluleuserserleuservalleuargleu290295300serhisasnserileserhisilealagluglyalaphelysglyleu305310315320argserleuargvalleuaspleuasphisasngluileserglythr325330335ilegluaspthrserglyalapheserglyleuaspserleuserlys340345350leuthrleupheglyasnlysilelysservalalalysargalaphe355360365serglyleugluglyleugluhisleuasnleuglyglyasnalaile370375380argservalglnpheaspalaphevallysmetlysasnleulysglu385390395400leuhisileserseraspserpheleucysaspcysglnleulystrp405410415leuproprotrpleuileglyargmetleuglnalaphevalthrala420425430thrcysalahisprogluserleulysglyglnserilepheserval435440445proprogluserphevalcysaspasppheleulysproglnileile450455460thrglnprogluthrthrmetalametvalglylysaspileargphe465470475480thrcysseralaalaserserserserserprometthrphealatrp485490495lyslysaspasngluvalleuthrasnalaaspmetgluasnpheval500505510hisvalhisalaglnaspglygluvalmetglutyrthrthrileleu515520525hisleuargglnvalthrpheglyhisgluglyargtyrglncysval530535540ilethrasnhispheglyserthrtyrserhislysalaargleuthr545550555560valasnvalleuproserphethrlysthrprohisaspilethrile565570575argthrthrthrvalalaargleuglucysalaalathr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5240gluasnproglypheglualaserproproalaglnglyileproglu245250255alalysvalarghisproleusertyrvalalaglnargglnproser260265270gluserglyarghisleuleusergluproserthrproleuserpro275280285proglyproglyaspvalphepheproserleuaspprovalproasp290295300serproasnphegluvalile305310<210>86<211>309<212>prt<213>小鼠(musmusculus)<400>86metglyvalproalavalproglualaserserproargtrpglythr151015leuleuleualailepheleualaalaserargglyleuvalalaala202530phelysvalthrthrprotyrserleutyrvalcysprogluglygln354045asnalathrleuthrcysargileleuglyprovalserlysglyhis505560aspvalthriletyrlysthrtrptyrleuserserargglygluval65707580glnmetcyslysgluhisargproileargasnphethrleuglnhis859095leuglnhishisglyserhisleulysalaasnalaserhisaspgln100105110proglnlyshisglyleugluleualaserasphishisglyasnphe115120125serilethrleuargasnvalthrproargaspserglyleutyrcys130135140cysleuvalilegluleulysasnhishisprogluglnargphetyr145150155160glysermetgluleuglnvalglnalaglylysglyserglyserthr165170175cysmetalaserasngluglnaspseraspserilethralaalaala180185190leualathrglyalacysilevalglyileleucysleuproleuile195200205leuleuleuvaltyrlysglnargglnvalalaserhisargargala210215220glngluleuvalargmetaspserserasnthrglnglyilegluasn225230235240proglyphegluthrthrpropropheglnglymetproglualalys245250255thrargproproleusertyrvalalaglnargglnprosergluser260265270glyargtyrleuleuseraspproserthrproleuserproprogly275280285proglyaspvalphepheproserleuaspprovalproaspserpro290295300asnserglualaile305<210>87<211>4714<212>dna<213>人(homosapiens)<400>87gggggcgggtgcctggagcacggcgctggggccgcccgcagcgctcactcgctcgcactc60agtcgcgggaggcttccccgcgccggccgcgtcccgcccgctccccggcaccagaagttc120ctctgcgcgtccgacggcgacatgggcgtccccacggccctggaggccggcagctggcgc180tggggatccctgctcttcgctctcttcctggctgcgtccctaggtccggtggcagccttc240aaggtcgccacgccgtattccctgtatgtctgtcccgaggggcagaacgtcaccctcacc300tgcaggctcttgggccctgtggacaaagggcacgatgtgaccttctacaagacgtggtac360cgcagctcgaggggcgaggtgcagacctgctcagagcgccggcccatccgcaacctcacg420ttccaggaccttcacctgcaccatggaggccaccaggctgccaacaccagccacgacctg480gctcagcgccacgggctggagtcggcctccgaccaccatggcaacttctccatcaccatg540cgcaacctgaccctgctggatagcggcctctactgctgcctggtggtggagatcaggcac600caccactcggagcacagggtccatggtgccatgagctgtcaggtgcagacaggcaaagat660gcaccatccaactgtgtggtgtacccatcctcctcccaggatagtgaaaacatcacggct720gcagccctggctacgggtgcctgcatcgtaggaatcctctgcctccccctcatcctgctc780ctggtctacaagcaaaggcaggcagcctccaaccgccgtgcccaggagctggtgcggatg840gacagcaacattcaagggattgaaaaccccggctttgaagcctcaccacctgcccagggg900atacccgaggccaaagtcaggcaccccctgtcctatgtggcccagcggcagccttctgag960tctgggcggcatctgctttcggagcccagcacccccctgtctcctccaggccccggagac1020gtcttcttcccatccctggaccctgtccctgactctccaaactttgaggtcatctagccc1080agctgggggacagtgggctgttgtggctgggtctggggcaggtgcatttgagccagggct1140ggctctgtgagtggcctccttggcctcggccctggttccctccctcctgctctgggctca1200gatactgtgacatcccagaagcccagcccctcaacccctctggatgctacatggggatgc1260tggacggctcagcccctgttccaaggattttggggtgctgagattctcccctagagacct1320gaaattcaccagctacagatgccaaatgacttacatcttaagaagtctcagaacgtccag1380cccttcagcagctctcgttctgagacatgagccttgggatgtggcagcatcagtgggaca1440agatggacactgggccaccctcccaggcaccagacacagggcacggtggagagacttctc1500ccccgtggccgccttggctcccccgttttgcccgaggctgctcttctgtcagacttcctc1560tttgtaccacagtggctctggggccaggcctgcctgcccactggccatcgccaccttccc1620cagctgcctcctaccagcagtttctctgaagatctgtcaacaggttaagtcaatctgggg1680cttccactgcctgcattccagtccccagagcttggtggtcccgaaacgggaagtacatat1740tggggcatggtggcctccgtgagcaaatggtgtcttgggcaatctgaggccaggacagat1800gttgccccacccactggagatggtgctgagggaggtgggtggggccttctgggaaggtga1860gtggagaggggcacctgccccccgccctccccatcccctactcccactgctcagcgcggg1920ccattgcaagggtgccacacaatgtcttgtccaccctgggacacttctgagtatgaagcg1980ggatgctattaaaaactacatggggaaacaggtgcaaaccctggagatggattgtaagag2040ccagtttaaatctgcactctgctgctcctcccccacccccaccttccactccatacaatc2100tgggcctggtggagtcttcgcttcagagccattcggccaggtgcgggtgatgttcccatc2160tcctgcttgtgggcatgccctggctttgtttttatacacataggcaaggtgagtcctctg2220tggaattgtgattgaaggattttaaagcaggggaggagagtagggggcatctctgtacac2280tctgggggtaaaacagggaaggcagtgcctgagcatggggacaggtgaggtggggctggg2340cagaccccctgtagcgtttagcaggatgggggccccaggtactgtggagagcatagtcca2400gcctgggcatttgtctcctagcagcctacactggctctgctgagctgggcctgggtgctg2460aaagccaggatttggggctaggcgggaagatgttcgcccaattgcttggggggttggggg2520gatggaaaaggggagcacctctaggctgcctggcagcagtgagccctgggcctgtggcta2580cagccagggaaccccacctggacacatggccctgcttctaagccccccagttaggcccaa2640aggaatggtccactgagggcctcctgctctgcctgggctgggccaggggctttgaggaga2700gggtaaacataggcccggagatggggctgacacctcgagtggccagaatatgcccaaacc2760ccggcttctcccttgtccctaggcagaggggggtcccttcttttgttccctctggtcacc2820acaatgcttgatgccagctgccataggaagagggtgctggctggccatggtggcacacac2880ctgtcctcccagcactttgcagggctgaggtggaaggaccgcttaagcccaggtgttcaa2940ggctgctgtgagctgtgttcgagccactacactccagcctggggacggagcaaaactttg3000cctcaaaacaaattttaaaaagaaagaaagaaggaaagagggtatgtttttcacaattca3060tgggggcctgcatggcaggagtggggacaggacacctgctgttcctggagtcgaaggaca3120agcccacagcccagattccggttctcccaactcaggaagagcatgccctgccctctgggg3180aggctggcctggccccagccctcagctgctgaccttgaggcagagacaacttctaagaat3240ttggctgccagaccccaggcctggctgctgctgtgtggagagggaggcggcccgcagcag3300aacagccaccgcacttcctcctcagcttcctctggtgcggccctgcc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pro15<210>98<211>12<212>prt<213>人工序列(artificialsequence)<220><223>肽接头<400>98alaglualaalaalalysglualaalaalalysala1510<210>99<211>6<212>prt<213>人工序列(artificialsequence)<220><223>肽接头<400>99ilegluglyargmetasp15<210>100<211>7<212>prt<213>人工序列(artificialsequence)<220><223>肽接头<400>100aspilegluglyargmetasp15当前第1页12