本公开内容涉及用于增加CASB7439多肽的重组生产的化合物和方法,和利用其的方法。
1.包含修饰的CASB7439多肽的蛋白质构建体,选自:(a)xa0xa0LVL055,其氨基酸序列如SEQxa0IDxa0NO:1所示;(b)xa0xa0LVL111,其氨基酸序列如SEQxa0IDxa0NO:3所示;(c)xa0xa0LVL137,其氨基酸序列如SEQxa0IDxa0NO:5所示;(d)xa0xa0LVL141,其氨基酸序列如SEQxa0IDxa0NO:7所示;(e)xa0xa0LVL144,其氨基酸序列如SEQxa0IDxa0NO:9所示;和(f)xa0xa0LVL168,其氨基酸序列如SEQxa0IDxa0NO:11所示。
2.免疫原性组合物,其包含权利要求1的蛋白质构建体、和药学可接受的载体或赋形剂,其中所述载体或赋形剂可以任选包含缓冲剂。
3.权利要求2的免疫原性组合物,其进一步包含佐剂。
4.权利要求3的免疫原性组合物,其中所述佐剂包含下述中的至少一种:TLR-4激动剂、免疫学活性皂苷级分、TLR-9激动剂。
5.权利要求4的免疫原性组合物,其中所述TLR-4激动剂是3D-MPL和/或所述TLR-9激动剂是CpG寡核苷酸和/或所述免疫学活性皂苷级分是QS21。
6.权利要求5的免疫原性组合物,其包含3D-MPL和/或CpG和/或QS21。
7.权利要求6的免疫原性组合物,其进一步包含胆固醇。
8.核酸分子,其由编码权利要求1的蛋白质构建体的多核苷酸序列组成。
9.包含佐剂和蛋白质的组合物在制备用于在人或非人动物中诱导针对CASB7439的免疫应答的药物中的应用,所述蛋白质由选自下述的多肽序列组成:(a)SEQxa0IDxa0NO:9中所示的多肽序列;和(b)SEQxa0IDxa0NO:11中所示的多肽序列。
10.包含佐剂和蛋白质的组合物在制备用于治疗人或非人动物中CASB7439相关疾病的药物中的应用,所述蛋白质由选自下述的多肽组成:xa0xa0xa0xa0xa0i.xa0SEQxa0IDxa0NO:9中所示的构建体;和xa0xa0xa0xa0xa0ii.xa0SEQxa0IDxa0NO:11中所示的构建体。
11.如权利要求2-7中定义的免疫原性组合物,其在人或非人动物中诱导针对CASB7439的免疫应答的方法中使用,所述方法包括施用有效量的所述免疫原性组合物。
12.根据权利要求11的免疫原性组合物,其包括由选自下述的多肽组成的蛋白质:(a)SEQxa0IDxa0NO:9中所示的构建体;和(b)SEQxa0IDxa0NO:11中所示的构建体。
13.如权利要求2-7中定义的免疫原性组合物在制备用于在人或非人动物中诱导针对CASB7439的免疫应答的方法中使用的药物中的应用,所述方法包括施用有效量的所述免疫原性组合物。背景哺乳动物无刚毛鳞甲同系物(Achaete-Scutexa0homolog)是果蝇无刚毛鳞甲复合物的保守哺乳动物同源物。它们是碱性螺旋-环-螺旋(bHLH或HLH)基因家族的成员,其充当对于发育必需的谱系特异性转录因子。该家族的一个鼠成员MASH2是胎盘发育必需的,但对于胚体发育并不重要。HASH2,MASH2基因的人直向同源物,在1997年由Alders等人进行克隆(由该作者指名为"ASCL2")。Alders等人(1997)Hum.xa0xa0Molec.xa0xa0Genet.xa0xa06:xa0859-867。如WO01/62778中所述,表达研究揭示与相邻正常结肠和其他测试的正常组织比较,HASH2转录物(其中称为CASB7439)在结肠直肠肿瘤中是超表达的。这种基因在具有I至IV期腺癌的患者中是超表达的。因此,该蛋白质可以视为在用于改善受试者的癌症的免疫治疗方法中有用的癌抗原,例如通过使用重组CASB7439作为抗原特异性癌免疫治疗剂(ASCI)。发明概述用于增加CASB7439多肽的重组产生的化合物和方法在本文中提供。在某些实施方案中,提供了修饰的CASB7439多肽,以及包含此类修饰的CASB7439多肽的蛋白质构建体。所述修饰的CASB7439多肽包含用于CASB7439增强产生的至少一个修饰。申请人还公开了包含编码修饰的CASB7439多肽的多核苷酸序列的核酸分子和包含如本文描述的此类修饰的CASB7439多肽的蛋白质构建体。在特定方面,申请人如下公开了具有氨基酸(aa)序列的蛋白质构建体和编码其的核苷酸序列(DNA):●xa0LVL055xa0[SEQxa0IDxa0NO:1(aa);SEQxa0IDxa0NO:2(DNA)];●xa0LVL111xa0[SEQxa0IDxa0NO:3(aa);SEQxa0IDxa0NO:4(DNA)];●xa0LVL137xa0[SEQxa0IDxa0NO:5(aa);SEQxa0IDxa0NO:6(DNA)];●xa0LVL141xa0[SEQxa0IDxa0NO:7(aa);SEQxa0IDxa0NO:8(DNA)];●xa0LVL144xa0[SEQxa0IDxa0NO:9(aa);SEQxa0IDxa0NO:10(DNA)];和●xa0LVL168xa0[SEQxa0IDxa0NO:11(aa);SEQxa0IDxa0NO:12(DNA)]。还公开了利用本文描述的核酸分子用于产生蛋白质构建体的方法和过程。申请人还公开了免疫原性组合物,这些组合物包含本文描述的一种或多种修饰的CASB7439多肽或构建体、和药学可接受的载体或赋形剂,其中载体或赋形剂可以任选包含缓冲剂。在某些实施方案中,公开了本文描述的修饰的CASB7439多肽或蛋白质构建体-或编码其的核酸分子-在制备用于治疗结肠直肠癌的药物中的应用。在某些实施方案中,公开了如本文公开的蛋白质构建体,其用于治疗、特别是结肠直肠癌治疗。在某些实施方案中,公开了用于引发针对具有结肠直肠癌的受试者中的CASB7439的免疫应答的方法,该方法包括:(a)选择具有结肠直肠癌的受试者;和(b)给受试者施用有效量的免疫原性组合物,所述免疫原性组合物包含如本文描述的修饰的CASB7439多肽或构建体、和药学可接受的载体或赋形剂,其中载体或赋形剂可以任选包含缓冲剂。附图简述图1/35。该图呈现了描述CASB7439多肽的各个区域的示意图,具体地:DNA特异性(DNA结合)结构域、bHLH结构域和富含脯氨酸的区域。关于细节参见实施例2。图示还显示了下述区域:核靶向(灰色箭头);α螺旋(灰色圆柱体);卷曲螺旋(黑色圆柱体);固有无序(黑色箭头);和低复合性(灰色框)。图2/35。该图呈现了描述与完全CASB7439多肽比对的CASB7439多肽的多个截短(黑色箭头)的示意图。关于细节参见实施例4。图3/35。该图呈现了CASB7439的示意图,显示富含脯氨酸的区域的近似定位,以及鉴定和预测的表位。各种实施方案包含通过去除富含脯氨酸的区域内的某些或所有氨基酸修饰的CASB7439多肽。此类修饰的CASB7439多肽保留在CASB7439多肽内的高部分表位。图4/35。显示了在未修饰的CASB7439多肽(SEQxa0IDxa0NO:13)序列和起因于对于CASB7439多肽的下列2个可能修饰的多肽序列之间的比对:在第一个可能修饰中21个邻接氨基酸残基(133-153,包括133和153)被缺失;在第二个可能修饰中21个邻接氨基酸残基(131-151,包括131和151)被缺失。进一步地,可以设想对于CASB7439多肽的第三个修饰,其中21个邻接氨基酸残基(132-152,包括132和152)被缺失。如该图中所示,在缺失区域中所得到的修饰的CASB7439多肽序列(插入,有圆圈的)对于所有3个修饰是相同的。这是因为在SEQxa0IDxa0NO:13的位置131-132和152-153上重复的RG氨基酸残基。图5/35。该图呈现了在实施例6的蛋白质构建体之间的氨基酸序列比对。CASB7439xa0=xa0HASH2氨基酸序列(SEQxa0IDxa0NO:13);LVL088(SEQxa0IDxa0NO:27);LVL111(SEQxa0IDxa0NO:3);LVL137(SEQxa0IDxa0NO:5);LVL138(SEQxa0IDxa0NO:33);LVL168(SEQxa0IDxa0NO:11)。图6/35。该图呈现了在HASH2(CASB7439)氨基酸序列(SEQxa0IDxa0NO:13)和下述蛋白质构建体之间的比对:LVL168(SEQxa0IDxa0NO:11);pD1/3(SEQxa0IDxa0NO:39);和LVL144(SEQxa0IDxa0NO:9)。图7/35。在正常(12个)和结肠直肠癌(83个)组织中CASB7439xa0mRNA表达的实时qPCR分析。参见实施例9。图8/35。在各种人结肠直肠(CRC)样品中CASB7439xa0mRNA和蛋白质表达之间的对应。●(黑色圆圈)代表在结肠癌样品中的CASB7439xa0mRNA表达,而○(空心圆圈)代表在正常相邻组织中的CASB7439xa0mRNA表达。通过免疫荧光检测的CASB7439蛋白质的相应水平在每种样品上方指出(-xa0无表达,+/-xa0极低表达,+xa0低表达,++xa0强表达和xa0+++xa0极强表达)。CRC:原发性肿瘤,METS:转移性,NAT:正常相邻组织。除其为粘液癌的样品22440和24762外,所有样品是结肠腺癌。参见实施例9。图9/35:xa0在这个表中阐述了在用各种CASB7439构建体免疫接种后用于脾细胞再刺激的覆盖整个CASB7439蛋白质序列的肽库。参见实施例10。图10/35。显示了用于T细胞免疫原性研究的CASB7439肽矩阵。参见实施例10。图11/35。在用CASB7439重叠肽(库,矩阵法)再刺激后,在用LVL111xa0+xa0AS01B免疫接种的近交小鼠的4个品系(C57BL6、BALBC、CB6F1和C3H)中表示为双重阳性百分比(IFNγ/TNFα)CD4xa0T细胞的CD4应答。参见实施例10,近交小鼠多品系比较实验。图12/35。在用CASB7439重叠肽(库,矩阵法)再刺激后,在用LVL111xa0+xa0AS15免疫接种的近交小鼠的4个品系中表示为双重阳性百分比(IFNγ/TNFα)CD4xa0T细胞的CD4应答。参见实施例10,近交小鼠多品系比较实验。图13/35。在先前段落中讨论的4种近交小鼠品系中CD4免疫原性CASB7439肽的鉴定。淡灰色=xa00.2-0.4xa0%双重阳性(IFNγ/TNFα)CD4xa0T细胞;深灰色≥xa00.5%双重阳性(IFNγ/TNFα)CD4xa0T细胞。参见实施例10,近交小鼠多品系比较实验。图14/35。在远交CD1小鼠(AS01B上图;AS15下图)中CD4免疫原性CASB7439肽的鉴定。淡灰色=xa00.2-0.4xa0%双重阳性(IFNγ/TNFα)CD4xa0T细胞;深灰色≥xa00.5%双重阳性(IFNγ/TNFα)T-CD4细胞。参见实施例10,CASB7439在小鼠中的免疫原性:在远交小鼠中的CASB7439xa0T细胞免疫原性。图15/35。在用CASB7439重叠肽(免疫显性肽的库)再刺激后,在用由AS15配制的LVL111、LVL168或LVL144免疫接种的个别CD1远交小鼠中表示为双重阳性(IFNγ/TNFα)百分比的CD4和CD8xa0T细胞应答。参见实施例10,在远交小鼠中的LVL111、LVL168和LVL144研究。图16/35。在用CASB7439重叠肽(7种肽/库的7个库+肽24(SEQxa0IDxa0NO:76))再刺激后,从用由AS15配制的LVL168xa0(SEQxa0IDxa0NO:11)或LVL144(SEQxa0IDxa0NO:9)免疫接种的HLAxa0A2.1/DR-1转基因小鼠中分离的合并外周血淋巴细胞(PBL)中的CD4xa0T细胞应答(表示为双重阳性百分比(IFNγ/TNFα))。图17/35。在用CASB7439重叠肽(7种肽的7个库+肽24(SEQxa0IDxa0NO:76))再刺激后,从用由AS15配制的LVL168xa0(SEQxa0IDxa0NO:11)或LVL144(SEQxa0IDxa0NO:9)免疫接种的HLAxa0A2.1/DR-1转基因小鼠中分离的合并PBL中的CD8xa0T细胞应答(表示为双重阳性百分比(IFNγ/TNFα))。图18/35。在用CASB7439重叠肽(7种肽的7个库+肽24(SEQxa0IDxa0NO:76))再刺激后,从用由AS15配制的LVL168xa0(SEQxa0IDxa0NO:11)或LVL144(SEQxa0IDxa0NO:9)免疫接种的HLAxa0A2.1/DR-1转基因小鼠中分离的脾细胞中的CD4xa0T细胞应答(表示为双重阳性百分比(IFNγ/TNFα))。图19/35。在用CASB7439重叠肽(7种肽的7个库+肽24(SEQxa0IDxa0NO:76))再刺激后,从用由AS15配制的LVL168xa0(SEQxa0IDxa0NO:11)或LVL144(SEQxa0IDxa0NO:9)免疫接种的HLAxa0A2.1/DR-1转基因小鼠中分离的脾细胞中的CD8xa0T细胞应答(表示为双重阳性百分比(IFNγ/TNFα))。图20/35。在LVL111xa0+xa0AS01B或LVL111xa0+xa0AS15免疫接种后触发的,在CB6f1近交小鼠中的CASB7439特异性抗体应答(IgG1和IgG2a)的时间-过程分析。参见实施例10,在小鼠中CASB7439的免疫原性:CASB7439介导的体液应答。图21/35。在用由AS15佐剂配制的LVL111、LVL168或LVL144或用单独的AS15佐剂免疫接种后,在近交CB6f1小鼠中的CASB7439特异性体液应答(IgG1和IgG2a)。参见实施例10,在小鼠中CASB7439的免疫原性:CASB7439介导的体液应答。图22/35。在用由AS15佐剂配制的LVL111、LVL168或LVL144或用单独的AS15佐剂免疫接种的CD1远交小鼠中的CASB7439特异性体液免疫应答(IgG滴度);首次用于实验的小鼠用作对照。参见实施例10,CD1小鼠研究。图23/35。在用由AS01B(上)或AS15(下)配制的LVL111免疫接种的CB6f1小鼠中的TC1/CASB7439xa0#14肿瘤移植物。参见实施例11,研究#1.1。在上图中,从上到下在曲线图上的曲线次序是‘缓冲液’、xa0LVL111(10μg)、LVL111(10μg)+xa0AS01B、和LVL111(1μg)+xa0ASO1B。在下图中,在下部的曲线是LVL111(10μg)+xa0AS15。图24/35。来自实施例11,研究#1.2的存活曲线呈现于上、中和下图中。TF:无肿瘤。(上)用盐水缓冲液、不含佐剂的LVL111或单独的佐剂(AS01或AS15)免疫接种且用TC1/CASB7439xa0#14细胞攻击的CB6f1小鼠的存活曲线。来自用LVL111免疫接种的组的最后一个存活小鼠首先死亡,随后为来自AS01B组的最后一只存活小鼠,随后为来自AS15组的最后一只存活小鼠,和来自缓冲液组的最后一只存活小鼠。(中)用单独的AS15或用由AS15配制的所示剂量的LVL111免疫接种且用TC1/CASB7439xa0#14细胞攻击的CB6f1小鼠的存活曲线。来自AS15组的最后一个存活小鼠首先断气。在其他组中,30μg组具有最少存活者,随后为1μg组,随后为10μg组,其具有最多的存活者。(下)用单独的AS01B或用由AS01B配制的所示剂量的LVL111免疫接种且用TC1/CASB7439xa0#14细胞攻击的CB6f1小鼠的存活曲线。在该小图中,来自10μg和AS01B的组的最后一个存活小鼠在同一天断气。1μg和30μg组在最后一天具有相同存活百分率。图25/35。呈现了来自实施例11,研究#1.3的存活曲线。TF:无肿瘤。(上)关于用由AS15配制的LVL111、LVL144或LVL168或单独的AS15免疫接种且用TC1/CASB7439#14细胞攻击的CB6f1小鼠的存活曲线。(下)关于用由AS15配制的LVL111、LVL144或LVL168或单独的AS15免疫接种且用MC38/CASB7439#35细胞攻击的CB6f1小鼠的存活曲线。图26/35。呈现了来自实施例11,研究#1.4的存活曲线。TF:无肿瘤。(上)用由AS15配制的LVL144或LVL168或单独的AS15免疫接种且用TC1/CASB7439xa0#14细胞攻击的CB6f1小鼠的存活曲线。用LVL144免疫接种的组具有边缘更大的存活百分比。(中)关于用由AS15配制的LVL144或LVL168或单独的AS15免疫接种且用TC1/CASB7439xa0#14-2细胞攻击的CB6f1小鼠的存活曲线。用LVL144接种的小鼠具有略微更高的存活百分比。(下)关于用由AS15配制的LVL144或LVL168或单独的AS15免疫接种且用MC38/CASB7439xa0#35细胞攻击的CB6f1小鼠的存活曲线。用LVL144接种的小鼠不具有存活者。图27/35。呈现了来自实施例11,研究#2.1的存活曲线。TF:无肿瘤。(上)用由AS15配制的6.25xa0μgxa0LVL168和10xa0μgxa0LVL144或单独的AS15免疫接种且用TC1/CASB7439xa0#14-2细胞攻击的CB6f1小鼠的存活曲线。用LVL168接种的小鼠具有略微更高的存活百分比。(中上)用由AS15配制的3.1xa0μgxa0LVL168和5xa0μgxa0LVL144或单独的AS15免疫接种且用TC1/CASB7439xa0#14-2细胞攻击的CB6f1小鼠的存活曲线。用LVL144接种的小鼠具有略微更高的存活百分比。(中下)用由AS15配制的1.55xa0μgxa0LVL168和2.5xa0μgxa0LVL144或单独的AS15免疫接种且用TC1/CASB7439xa0#14-2细胞攻击的CB6f1小鼠的存活曲线。用LVL144接种的小鼠具有最高的存活百分比。(下)用由AS15配制的0.77xa0μgxa0LVL168和1.25xa0μgxa0LVL144或单独的AS15免疫接种且用TC1/CASB7439xa0#14-2细胞攻击的CB6f1小鼠的存活曲线。用LVL168接种的小鼠具有略微更高的存活百分比。图28/35。呈现了来自实施例11,研究#2.2的存活曲线。TF:无肿瘤。(上)用由AS15配制的6.25xa0μgxa0LVL168或10xa0μgxa0LVL144或单独的AS15免疫接种且用TC1/CASB7439xa0#14-2细胞攻击的C57Bl/6小鼠的存活曲线。(中上)用由AS15配制的3.1xa0μgxa0LVL168或5xa0μgxa0LVL144或单独的AS15免疫接种且用TC1/CASB7439xa0#14-2细胞攻击的C57Bl/6小鼠的存活曲线。(中下)用由AS15配制的1.55xa0μgxa0LVL168或2.5xa0μgxa0LVL144或单独的AS15免疫接种且用TC1/CASB7439xa0#14-2细胞攻击的C57Bl/6小鼠的存活曲线。(下)用由AS15配制的0.77xa0μgxa0LVL168或1.25xa0μgxa0LVL144或单独的AS15免疫接种且用TC1/CASB7439xa0#14-2细胞攻击的C57Bl/6小鼠的存活曲线。图29/35。呈现了来自实施例11,研究#2.3的存活曲线。TF:无肿瘤。(上)用由AS15配制的6.25xa0μgxa0LVL168或10xa0μgxa0LVL144免疫接种且用TC1/CASB7439xa0#14-2细胞攻击的CB6f1小鼠的存活曲线。接受LVL168的小鼠组具有最高存活百分比,随后为接受LVL144的组。在仅接受AS15的组中没有存活者。(中)用由AS15配制的3.1xa0μgxa0LVL168和5xa0μgxa0LVL144免疫接种且用TC1/CASB7439xa0#14-2细胞攻击的CB6f1小鼠的存活曲线。接受LVL168的小鼠组具有最高存活百分比,随后为接受LVL144的组。在仅接受AS15的组中没有存活者。(下)用由AS15配制的1.55xa0μgxa0LVL168和2.5xa0μgxa0LVL144免疫接种且用TC1/CASB7439xa0#14-2细胞攻击的CB6f1小鼠的存活曲线。接受LVL168的小鼠组具有最高存活百分比,随后为接受LVL144的组。在仅接受AS15的组中没有存活者。盐水缓冲液或单独的AS15用作对照。图30/35。来自实施例11,研究#2.3的存活曲线。TF:无肿瘤。(上)用由AS15配制的0.77xa0μgxa0LVL168或1.25xa0μgxa0LVL144免疫接种且用TC1/CASB7439xa0#14-2细胞攻击的CB6f1小鼠的存活曲线。接受LVL168的小鼠组具有最高存活百分比,随后为接受LVL144的组。在仅接受AS15的组中没有存活者。(中)用由AS15配制的0.19xa0μgxa0LVL168或0.31xa0μgxa0LVL144免疫接种且用TC1/CASB7439xa0#14-2细胞攻击的CB6f1小鼠的存活曲线。接受LVL168的小鼠组具有最高存活百分比。来自接受LVL144的组的最后一个存活小鼠活得比来自AS15组和缓冲液组的最后一个存活者久。(下)用由AS15配制的0.048xa0μgxa0LVL168或0.078xa0μgxa0LVL144免疫接种且用TC1/CASB7439xa0#14-2细胞攻击的CB6f1小鼠的存活曲线。接受LVL168的小鼠组具有最高存活百分比。来自接受LVL144的组的最后一个存活小鼠活得比来自AS15组和缓冲液组的最后一个存活者久。盐水缓冲液或单独的AS15用作对照。图31/35。在用由AS15配制的1xa0μgxa0LVL168免疫接种的雄性和雌性CB6f1小鼠中的TC1/CASB7439xa0#14-2肿瘤移植物;单独的AS15用作对照(上)。在用由AS15配制的1xa0μgxa0LVL168免疫接种的C57Bl/6小鼠中的TC1/CASB7439xa0#14-2肿瘤移植物;单独的AS15用作对照(下)。图32/35。上图:用由AS15配制的1xa0μgxa0LVL168免疫接种且用TC1/CASB7439xa0#14-2细胞攻击的雄性和雌性CB6f1小鼠的存活曲线。单独的AS15在雄性和雌性CB6f1小鼠中用作对照。在用LVL168加上AS15免疫接种的CB6f1小鼠中,存在7只无肿瘤(TF)雄性和3只TF雌性。在接受单独的AS15的小鼠中不存在TF。下图:用由AS15配制的1xa0μgxa0LVL168免疫接种且用TC1/CASB7439xa0#14-2攻击的C57Bl/6小鼠的存活曲线。单独的AS15在雄性和雌性C57Bl/6小鼠中用作对照。在用LVL168加上AS15免疫接种的C57Bl/6小鼠中,存在2只TF雄性和1只TF雌性。在接受单独的AS15的小鼠中,存在5只TF雄性和1只TF雌性。图33/35。在用由AS15配制的1xa0μgxa0LVL168免疫接种或用单独的AS15免疫接种的雄性(黑色圆圈)和雌性(灰色圆圈)CB6F1小鼠中的CASB7439特异性体液免疫应答(IgG滴度)(左)。在用由AS15配制的1xa0μgxa0LVL168免疫接种或用单独的AS15免疫接种的雄性(黑色圆圈)和雌性(灰色圆圈)C57/BL6小鼠中的CASB7439特异性体液免疫应答(IgG滴度)(右)。图34/35。在用覆盖整个CASB7439蛋白质序列的46种肽的肽库(参见图9)再刺激后,从用由AS15配制的1xa0μgxa0LVL168xa0(SEQxa0IDxa0NO:11)或单独的AS15免疫接种的CB6F1小鼠中分离的合并PBL中的CD4xa0T细胞应答(表示为双重阳性百分比(IFNγ/TNFα))(上)。在用CASB7439合并肽,覆盖整个CASB7439蛋白质序列的46种肽的肽库(参见图9)(下左);CASB7439肽39(SEQxa0IDxa0NO:91)(中下);或RPMI(下右)再刺激后,从用由AS15配制的1xa0μgxa0LVL168xa0(SEQxa0IDxa0NO:11)或单独的AS15免疫接种的C57/BL6小鼠中分离的合并PBLs中的CD4xa0T细胞应答(表示为双重阳性百分比(IFNγ/TNFα))(下)。图35/35。在用覆盖整个CASB7439蛋白质序列的46种肽的肽库(参见图9)再刺激后,从用由AS15配制的1xa0μgxa0LVL168xa0(SEQxa0IDxa0NO:11)或单独的AS15免疫接种的CB6F1小鼠中分离的合并PBL中的CD8xa0T细胞应答(表示为双重阳性百分比(IFNγ/TNFα))(上)。在用覆盖整个CASB7439蛋白质序列的46种肽的肽库(参见图9)(下左);CASB7439肽39(SEQxa0IDxa0NO:91)(中下);或RPMI(下右)再刺激后,从用由AS15配制的1xa0μgxa0LVL168xa0(SEQxa0IDxa0NO:11)或单独的AS15免疫接种的C57/BL6小鼠中分离的合并PBLs中的CD8xa0T细胞应答(表示为双重阳性百分比(IFNγ/TNFα))(下)。发明详述关于商业可接受的免疫治疗剂的一个障碍是商业可接受量的重组癌抗原的产生。一般而言且非限制性的,关于重组多肽的商业可接受的生产水平是通过宿主细胞产生的总蛋白质的大约5%,如在考马斯蓝染色的SDS-PAGE凝胶上估计的。存在当通过重组方法产生时天然多肽序列为何可仅获得小量的众多原因。增加多肽产生的方法包括改变宿主表达系统或密码子最佳化。然而,这些标准方法并不一定导致可接受的多肽产生,并且关于某些多肽的生产仍是商业上禁止的。如下文更详细地描述的,申请人研究修饰的CASB7439多肽是否将通过重组方法产生可接受的蛋白质水平。在某些实施方案中,提供了修饰的CASB7439多肽,其中修饰由CASB7439多肽的C末端截短组成,或包含CASB7439多肽的C末端截短,从而使得所有或部分富含脯氨酸的区域被去除。在某些实施方案中,CASB7439多肽修饰由所有或部分富含脯氨酸的区域的缺失组成,或包含所有或部分富含脯氨酸的区域的缺失。在某些实施方案中,提供了修饰的CASB7439多肽,其保留SEQxa0IDxa0NO:13的至少氨基酸残基193,但其中所有或部分富含脯氨酸的区域被缺失。在其他实施方案中,提供了包含如本文描述的修饰的CASB7439多肽的蛋白质构建体。在某些实施方案中,此类蛋白质构建体进一步包含一种或多种异源多肽。在某些实施方案中,异源多肽是融合配偶体,如其他地方更详细地描述的。在特别合适的实施方案中,此类蛋白质构建体包含定位于修饰的CASB7439多肽N末端的异源多肽。在进一步特别合适的实施方案中,提供了这样的蛋白质构建体,其中异源多肽是定位于修饰的CASB7439多肽N末端的流感嗜血杆菌(H.xa0xa0influenzae)蛋白质D的片段(如下文更详细地描述的)。在某些实施方案中,提供了其中异源多肽包含多组氨酸区域的蛋白质构建体。在进一步的实施方案中,多组氨酸序列定位于蛋白质构建体的C末端部分。在其他实施方案中,多组氨酸序列定位于蛋白质构建体的C末端。在进一步的实施方案中,多组氨酸序列定位于蛋白质构建体的N末端部分。在其他实施方案中,多组氨酸序列定位于蛋白质构建体的N末端。在合适的实施方案中,多组氨酸区域包含10个或更多连续组氨酸残基。在特别合适的实施方案中,多组氨酸区域包含定位于修饰的CASB7439多肽N末端的10个或更多连续组氨酸残基。在某些实施方案中,超过一个多组氨酸区域可以包括在本文描述的一个或多个位置上。在某些实施方案中,提供了其中异源多肽是与修饰的CASB7439多肽化学缀合的载体蛋白质的蛋白质构建体。在某些实施方案中,提供了包含为多组氨酸区域的异源多肽和为载体蛋白质的异源多肽的蛋白质构建体。在某些实施方案中,提供了包含为多组氨酸区域的异源多肽和为融合配偶体的异源多肽的蛋白质构建体。在某些实施方案中,提供了包含为多组氨酸区域的异源多肽、为融合配偶体的异源多肽和为载体蛋白质的异源多肽的蛋白质构建体。申请人还公开了本文段落中描述的每种构建体的实施方案,其中任何异源多肽例如多组氨酸区域中的一些或所有已被去除。用于去除异源多肽的组合物和方法是本领域已知的,包括但不限于用内或外肽酶消化、化学修饰或在异源多肽和分子其余部分之间的键的断裂等。申请人在本文中还公开了免疫原性组合物,这些组合物包含任何修饰的CASB7439多肽或包含如本文描述的修饰的CASB7439多肽的蛋白质构建体、和药学可接受的载体或赋形剂,其中载体或赋形剂可以任选包含缓冲剂。在特定方面,这些组合物进一步包含佐剂。在特定方面,这些组合物包含引发至少TH1免疫应答的佐剂。在特定方面,本文描述的佐剂包含下述中的至少一种:3D-MPL、QS21和CpG。在某些实施方案中,组合物包含3D-MPL。在其他实施方案中,组合物包含CpG。在某些实施方案中,组合物包含QS21。在某些实施方案中,组合物包含QS21和胆固醇。在某些实施方案中,组合物包含在脂质体制剂中的胆固醇、3D-MPL和QS21。申请人在本文中还公开了包含编码如本文描述的修饰的CASB7439多肽和构建体的多核苷酸序列的核酸分子。在某些实施方案中,公开了包含如本文描述的此类核酸分子的载体。在某些实施方案中,载体包含原核表达载体。在某些实施方案中,载体包含真核表达载体。在某些实施方案中,编码构建体的多核苷酸序列已就在宿主细胞中的表达进行密码子最佳化。申请人还公开了包含下述的宿主细胞:(i)如本文描述的核酸分子,或(ii)包含如本文描述的核酸分子的载体。在某些实施方案中,宿主细胞选自:细菌细胞、昆虫细胞和哺乳动物细胞。某些实施方案提供了包含下述的免疫原性组合物:(i)本文描述的核酸分子,或(ii)包含如本文描述的核酸分子的载体,以及药学可接受的载体或赋形剂。在某些实施方案中,提供了本文描述的修饰的CASB7439多肽或蛋白质构建体(或编码其的核酸分子)在制备用于治疗结肠直肠癌的药物中的应用。在某些实施方案中,公开了用于治疗、特别是结肠直肠癌治疗的本文描述的修饰的CASB7439多肽或蛋白质构建体(或编码其的核酸分子)。在某些实施方案中,提供了用于在具有结肠直肠癌的受试者中引发针对CASB7439的免疫应答的方法,该方法包括:(i)选择具有结肠直肠癌的受试者;和(b)给受试者施用有效量的免疫原性组合物,所述免疫原性组合物包含如本文描述的修饰的CASB7439多肽或蛋白质构建体、和药学可接受的载体或赋形剂,其中载体或赋形剂可以任选包含缓冲剂。在本文公开的方法的某些实施方案中,免疫原性组合物进一步包含佐剂。在本文公开的方法的某些实施方案中,佐剂引发至少TH1免疫应答。在本文公开的方法的某些实施方案中,佐剂包含下述中的至少一种:3D-MPL、QS21和CpG。在本文公开的方法的某些实施方案中,受试者是人受试者。蛋白质构建体CASB7439多肽如其已在本文中命名的,CASB7439也称为HASH2或ASCL2。HASH2是人起源的193氨基酸残基多肽(SEQxa0IDxa0NO:13)。参见例如,登记号AAB86993。此处,对CASB7439特征的提及将就SEQxa0IDxa0NO:13中提供的多肽序列而言进行。富含脯氨酸的区域高脯氨酸周期性的区域在SEQxa0IDxa0NO:13中在氨基酸127-158的区域中发现。申请人将包括133和153在内的从氨基酸133到氨基酸153的SEQxa0IDxa0NO:13区域命名为“富含脯氨酸的”、“多脯氨酸”、“多脯氨酸样的”或“polypro”区域或结构域。相应地,如本文使用的,“富含脯氨酸的”、“多脯氨酸”、“多脯氨酸样的”和“polypro”指CASB7439蛋白质的这个区域(或结构域)。修饰本公开内容提供了包含CASB7439多肽的蛋白质构建体,所述CASB7439多肽包含至少一个表达增强修饰。在某些实施方案中,CASB7439多肽的部分被去除,所述部分包含所有或部分富含脯氨酸的区域。在某些实施方案中,CASB7439多肽的整个C末端部分被去除,导致包含SEQxa0IDxa0NO:13的氨基酸残基1-117的截短的CASB7439多肽。在某些实施方案中,异源多肽置于CASB7439多肽的N末端。如本文使用的,在修饰的CASB7439多肽背景中的“表达增强”或“增强的表达”指,与包含SEQxa0IDxa0NO:13的未修饰的CASB7439多肽的其他方面等价的蛋白质构建体的表达比较,即相同载体、宿主细胞等,预期增加包含所述修饰的CASB7439多肽的蛋白质构建体的表达水平的修饰。用于测定蛋白质数量的本领域已知的任何方法可应用于测定,与包含未修饰的CASB7439多肽的其他方面等价的蛋白质构建体比较,包含修饰的CASB7439多肽的给定构建体是否具有增加的表达水平。在某些实施方案中,使用SDS-PAGE和考马斯蓝染色可以评价生产。富含脯氨酸的区域的去除在某些实施方案中,CASB7439多肽的修饰包含某些富含脯氨酸的区域的缺失。在某些实施方案中,CASB7439多肽的修饰包含所有富含脯氨酸的区域的缺失。在某些实施方案中,除富含脯氨酸的区域的缺失外,CASB7439多肽的修饰还包含在富含脯氨酸的区域外的氨基酸的缺失。在某些实施方案中,修饰通过SEQxa0IDxa0NO:13的C末端部分的截短来完成。因此,在某些实施方案中,生成了蛋白质构建体,其中修饰的CASB7439多肽的C末端氨基酸残基对应于定位于SEQxa0IDxa0NO:13的富含脯氨酸的区域N末端的残基。在某些实施方案中,生成了蛋白质构建体,其中修饰的CASB7439多肽的C末端氨基酸残基对应于定位于SEQxa0IDxa0NO:13的富含脯氨酸的区域中的残基。在某些实施方案中,修饰的CASB7439多肽的C末端氨基酸残基对应于SEQxa0IDxa0NO:13的氨基酸残基117、118、119、120、121、122、123、124、125、126、127、128、129、130、131、132、133、134、135、136、137、138、139、140、141、142、143、144、145、146、147、148、149、150、151或152。在某些实施方案中,修饰包含部分或所有富含脯氨酸的区域的缺失。在某些实施方案中,修饰的CASB7439多肽序列对应于21个或更多邻接氨基酸残基已从其中缺失的SEQxa0IDxa0NO:13。这21个或更多邻接残基对应于从包括端点在内的残基117、118、119、120、121、122、123、124、125、126、127、128、129、130、131、132、133、134、135、136、137、138、139、140、141、142、143、144、145、146、147、148、149、150、151或152中的任何一个开始的SEQxa0IDxa0NO:13的邻接氨基酸序列。在进一步的实施方案中,修饰的CASB7439多肽序列对应于21个邻接氨基酸残基已从其中缺失的SEQxa0IDxa0NO:13,所述21个邻接残基从残基131、132和133中的任何一个开始。在某些实施方案中,修饰的CASB7439多肽序列对应于残基133、134、135、136、137、138、139、140、141、142、143、144、145、146、147、148、149、150、151、152、153中的一个或多个已从其中缺失的SEQxa0IDxa0NO:13。在某些实施方案中,修饰的CASB7439多肽序列对应于从其中2个或更多邻接氨基酸残基已在包括133和153在内的氨基酸残基133-153的区域中缺失的SEQxa0IDxa0NO:13。在某些实施方案中,修饰的CASB7439多肽序列对应于SEQxa0IDxa0NO:xa013的包括133和153在内的残基133到153已从其中缺失的SEQxa0IDxa0NO:13。示例性非限制性实施方案包括下述:●xa0LVL055,SEQxa0IDxa0NO:1(aa);●xa0LVL111,SEQxa0IDxa0NO:3(aa);●xa0LVL137,SEQxa0IDxa0NO:5(aa);●xa0LVL141,SEQxa0IDxa0NO:7(aa);●xa0LVL144,SEQxa0IDxa0NO:9(aa);和●xa0LVL168,SEQxa0IDxa0NO:11(aa)。异源序列在某些实施方案中,修饰的CASB7439多肽与异源多肽组合。术语“异源的”就核酸分子、多肽或另一种细胞组分而言,指示组分在它通常不在自然界中发现处出现和/或它源于与参考分子不同的来源或物种。如本文使用的,“异源”分子包括但不限于融合蛋白、载体蛋白质和纯化标签。在某些实施方案中,异源多肽可以与修饰的CASB7439多肽,即载体蛋白质化学缀合。在其他实施方案中,异源多肽和修饰的CASB7439多肽可以作为单一重组融合蛋白表达。在其他实施方案中,修饰的CASB7439多肽和异源多肽作为单一重组融合蛋白表达且与另一种异源多肽化学缀合。异源多肽可以帮助提供T辅助表位,包括由人识别的T辅助表位。在包含CASB7439多肽和为融合蛋白的异源多肽的蛋白质构建体的情况下,异源多肽(融合配偶体)可以帮助提供此类表位,或帮助以比天然重组蛋白质更高的收率表达蛋白质(表达增强子)。融合配偶体可以是免疫学融合配偶体和表达增强配偶体。载体蛋白质载体蛋白质与另一种目的多肽化学缀合。多肽与载体蛋白质的化学偶联可以以本领域已知的任何方式执行。因此,对于直接共价偶联,可以利用碳二亚胺、戊二醛或N-[γ-马来酰亚胺丁酰氧基]琥珀酰亚胺酯,利用普通商购可得的异双功能接头例如CDAP和SPDP(使用制造商的说明书)。在偶联反应后,借助于透析法、凝胶过滤法、分级分离法等,可以容易地分离且纯化多肽-载体蛋白质缀合物。在某些实施方案中使用的载体蛋白质的类型将是本领域技术人员容易已知的。某些载体蛋白质的功能是提供细胞因子帮助,以便帮助诱导针对偶联多肽的免疫应答。例如,可以用于本发明中的载体蛋白质的非详尽列表包括:钥孔血蓝蛋白(KLH),血清白蛋白例如牛血清白蛋白(BSA),灭活的细菌毒素例如破伤风或白喉毒素(TT和DT)、或其重组片段(例如,TT的片段C的结构域1、或DT的易位结构域),或结核菌素(PPD)的纯化蛋白质衍生物。融合配偶体尽管存在众多基因融合系统的可用性,在大肠埃希杆菌(Escherichiaxa0coli)中的重组蛋白质表达仍是困难的。建立最佳地增强难以表达的蛋白质表达的融合配偶体仍是凭经验的。常见融合配偶体包括麦芽糖结合蛋白(MBP)的C末端、谷胱甘肽S转移酶(GST)、硫氧还蛋白(TRX)、NUSxa0A、泛素(Ub)和小泛素样修饰物(SUMO)标签,其各自在文献中得到描述。参见例如,Marblestone(2006)Prot.xa0xa0Sci.xa0xa015:182-7;Hunt(2005)Proteinxa0Exp.xa0xa0&xa0Purifxa040:1-22;Hammarstom等人(2002)Proteinxa0Sci.xa0xa011:313-321。免疫原性融合配偶体包括来自流感嗜血杆菌B的蛋白质D和来自流感病毒的非结构蛋白质NS1(血凝素)。另一种免疫学融合配偶体是称为LYTA的蛋白质。可以使用分子的C末端部分。LYTA衍生自肺炎链球菌(Streptococcusxa0pneumoniae),其合成N-乙酰基-L-丙氨酸酰胺酶、酰胺酶LYTA(由lytA基因编码García等人(1986)Genexa043:265-272)。可以使用从残基178开始的在C末端中发现的Lyta分子的重复部分,例如残基188-305。另一种合适的融合配偶体是腺苷酸环化酶(CyaA)蛋白质或其片段,其中所述CyaA片段保留所述腺苷酸环化酶蛋白质靶向抗原呈递细胞的性质。参见WO2005089792。在本发明的一个实施方案中,异源多肽是来自流感嗜血杆菌的蛋白质D(EPxa00xa0594xa0610xa0B1),或其片段。蛋白质D是来自流感嗜血杆菌的IgD结合蛋白(WOxa091/18926,授予EPxa00xa0594xa0610xa0B1)。在某些情况下,例如在重组免疫原表达系统中,可能希望使用蛋白质D的N末端片段,例如包含蛋白质D的约100xa0–xa0约110个N末端氨基酸(GBxa09717953.5)(pD1/3,SEQxa0IDxa0NO:39)。流感嗜血杆菌蛋白质D作为具有18氨基酸信号序列的前体(SEQxa0IDxa0NO:41,还参见登记号AAA24998)合成。当信号序列在分泌过程中进行加工时,在前体分子中在位置19上的半胱氨酸残基变成氨基末端残基。在一个实施方案中,异源多肽序列包含经加工的流感嗜血杆菌蛋白质D分子的前约三分之一,或经加工的蛋白质D的N末端100-110个氨基酸。在一个实施方案中,异源蛋白质包含与经加工的蛋白质D的N末端109个氨基酸连接的氨基酸残基Met-Asp-Pro。在另一个实施方案中,异源蛋白质包含与经加工的蛋白质D(SEQxa0IDxa0NO:39)的氨基酸残基2-109连接的氨基酸残基Met-Asp-Pro。在一个实施方案中,修饰的CASB7439多肽或蛋白质构建体与CyaA蛋白质或其片段化学偶联。参见WO2005054851。在另一个实施方案中,修饰的CASB7439多肽或蛋白质构建体与志贺毒素的B亚单位或其免疫学功能等价物化学偶联。参见美国专利号6,613,882;WO02060937;WO2005112991。多组氨酸标签,无关氨基酸包括异源多肽通常是有利的,所述异源多肽含有分泌或前导序列、前序列(pro-sequence)、帮助纯化的序列例如组氨酸标签例如多组氨酸序列(包含多个组氨酸残基)、或用于在重组生产过程中的稳定性的另外序列。组氨酸标签载体和试剂盒是商购可得的。例如,用于将6组氨酸标签加入多肽中的载体可从Roche获得。用于制备且使用加组氨酸标签的多肽的试剂盒可从Qiagen、Sigma、Thermoxa0Scientific、GExa0Healthcare及其他获得。组氨酸标签还可以跟随促进使用内肽酶的多组氨酸序列去除的合适氨基酸序列。外肽酶例如Qiagenxa0TAGZyme可以用于去除末端多组氨酸序列,而无需另外序列。在某些实施方案中,多组氨酸序列定位于蛋白质构建体的N末端区域中。在进一步的实施方案中,多组氨酸序列定位于蛋白质构建体的N末端上。在某些实施方案中,多组氨酸序列包含6、7、8、9、10、11、12、13、14、15个或更多连续组氨酸。在进一步的实施方案中,多组氨酸序列包含10个连续组氨酸。在某些实施方案中,异源多肽包括多组氨酸序列和一个或多个无关氨基酸。“无关氨基酸”意指这样的一个或多个氨基酸,其不是多组氨酸序列、或融合蛋白的部分,并且不是CASB7439多肽序列的天然部分。例如,无关氨基酸可以是包括以提供肽酶位点的那些,它们可以仅仅是外来序列,例如克隆人工产物等。编码CASB7439构建体的核酸分子本公开内容的其他实施方案涉及编码如本文描述的修饰的CASB7439多肽和蛋白质构建体的重组核酸。在特定实施方案中,重组核酸对于在所选原核或真核宿主细胞中的表达进行密码子最佳化。为了促进复制和表达,核酸可以掺入载体内,例如原核或真核表达载体。包括重组修饰的CASB7439多肽或蛋白质构建体-编码核酸的宿主细胞也是本公开内容的特征。有利的宿主细胞包括原核(即细菌)宿主细胞,例如大肠杆菌,以及众多真核宿主细胞,包括真菌(例如酵母)细胞、昆虫细胞和哺乳动物细胞(例如HEK293、CHO和VERO细胞)。表达载体为了促进复制和表达,核酸可以掺入载体内,例如原核或真核表达载体。尽管本文公开的核酸可以包括在多种载体(包括例如细菌质粒;噬菌体DNA;杆状病毒;酵母质粒;衍生自质粒和噬菌体DNA、病毒DNA组合的载体,所述病毒DNA例如牛痘、腺病毒、禽痘病毒、假狂犬病、腺病毒、腺相关病毒、逆转录病毒及许多其他)中的任何一种中,最通常地载体将是适合于生成多肽表达产物的表达载体。在表达载体中,编码蛋白质构建体的核酸一般以对于合适转录控制序列(启动子和任选地一个或多个增强子)的接近性和方向排列,以指导mRNA合成。即,目的多核苷酸序列与合适的转录控制序列可操作地连接。此类启动子的例子包括:CMV的立即早期启动子、LTR或SV40启动子、杆状病毒的多角体启动子、大肠杆菌lac或trp启动子、噬菌体T7和λxa0PL启动子、和已知控制原核或真核细胞或其病毒中基因的表达的其他启动子。表达载体一般还含有用于翻译起始的核糖体结合位点、和转录终止子。载体任选包括用于扩增表达的合适序列。此外,表达载体任选地包含一种或多种选择标记基因,以提供用于选择经转化的宿主细胞的表型性状,例如用于真核细胞培养的二氢叶酸还原酶或新霉素抗性,或例如在大肠杆菌中的四环素或氨苄青霉素抗性。足以指导本领域技术人员的通过重组CASB7439核酸产生的示例性程序可以在下述中发现:Sambrook等人,Molecularxa0Cloning:xa0Axa0Laboratoryxa0Manual,第2版,Coldxa0Springxa0Harborxa0Laboratoryxa0Press,1989;Sambrook等人,Molecularxa0Cloning:xa0Axa0Laboratoryxa0Manual,第3版,Coldxa0Springxa0Harborxa0Press,2001;Ausubel等人,Currentxa0Protocolsxa0inxa0Molecularxa0Biology,Greenexa0Publishingxa0Associates,1992(和对于2003年的增刊);和Ausubel等人,Shortxa0Protocolsxa0inxa0Molecularxa0Biology:xa0Axa0Compendiumxa0ofxa0Methodsxa0fromxa0Currentxa0Protocolsxa0inxa0Molecularxa0Biology,第4版,Wileyxa0&xa0Sons,1999。编码蛋白质构建体的示例性核酸分子由SEQxa0IDxa0NO:2、SEQxa0IDxa0NO:4、SEQxa0IDxa0NO:6、SEQxa0IDxa0NO:8、SEQxa0IDxa0NO:10和SEQxa0IDxa0NO:12表示。与示例性核酸分子共享序列同一性的另外序列变体可以由本领域技术人员产生。一般地,核酸变体将编码相差不超过1%、或2%、或5%、或10%、或15%、或20%氨基酸残基的多肽。即,所编码的多肽共享至少80%、或85%,更通常至少约90%或更多,例如95%、98%、99%、或99.5%序列同一性。本领域技术人员将立即理解,编码蛋白质构建体的多核苷酸序列自身可以共享更少的序列同一性,这是由于遗传编码的冗余。在某些情况下,相对于本文所示的示例性构建体的氨基酸序列(例如,除上述修饰外),修饰的CASB7439多肽或蛋白质构建体具有一个或多个氨基酸修饰。此类差异可以分别是一个或多个核苷酸或氨基酸的添加、缺失或置换。变体一般相差不超过约1%、或2%、或5%、或10%、或15%、或20%或25%或30%核苷酸残基。例如,与SEQxa0IDxa0NO:2、SEQxa0IDxa0NO:4、SEQxa0IDxa0NO:6、SEQxa0IDxa0NO:8、SEQxa0IDxa0NO:10和SEQxa0IDxa0NO:12的示例性CASB7439多肽或蛋白质构建体编码核酸比较,变体CASB7439多肽或蛋白质构建体编码核酸可以包括1或2、或直到5、或直到约10、或直到约15、或直到约50、或直到约100个核苷酸差异。因此,在CASB7439多肽或蛋白质构建体编码核酸背景中的变体,一般与参考序列共享至少70%、或75%、或80%、或85%、或90%、或95%、或98%、或99%、或99.5%序列同一性,例如由SEQxa0IDxa0NO:2、SEQxa0IDxa0NO:4、SEQxa0IDxa0NO:6、SEQxa0IDxa0NO:8、SEQxa0IDxa0NO:10和SEQxa0IDxa0NO:12举例说明的参考序列,或本文公开的其他示例性CASB7439多肽、蛋白质构建体编码核酸中的任何。另外变体可以通过遗传漂变出现,或可以使用定点或随机诱变、或通过2个或更多预先存在的变体的重组人工产生。此类另外变体还适合于本文公开的CASB7439多肽或蛋白质构建体背景中。除先前描述的变体核酸外,与由SEQxa0IDxa0NO:2、SEQxa0IDxa0NO:4、SEQxa0IDxa0NO:6、SEQxa0IDxa0NO:8、SEQxa0IDxa0NO:10和SEQxa0IDxa0NO:12表示的一种或多种示例性核酸杂交的核酸也可以用于编码本文公开的CASB7439多肽或蛋白质构建体。本领域技术人员应当理解除本文讨论的序列同一性百分比(%)测量外,2个核酸之间的序列相似性的另一个标记是杂交的能力。2个核酸的序列越相似,它们将在其下杂交的条件越严格。杂交条件的严格性是序列依赖性的,并且在不同环境参数下是不同的。因此,导致特定严格性程度的杂交条件将不同,这取决于杂交的性质、选择的方法、以及杂交核酸序列的组成和长度。一般地,杂交的温度和杂交缓冲液的离子强度(特别是Na⁺和/或Mg⁺⁺浓度)将决定杂交的严格性,尽管洗涤时间也影响严格性。一般地,严格条件选择为低于在限定离子强度和pH下关于特定序列的热解链温度(T_m)约5°Cxa0-xa020°C。T_m是在其下50%的靶序列与完全匹配的探针杂交的温度(在限定离子强度和pH下)。对于核酸杂交和严格性计算的条件可以例如在下述中找到:Sambrook等人,Molecularxa0Cloning:xa0Axa0Laboratoryxa0Manual,Coldxa0Springxa0Harborxa0Laboratoryxa0Press,Coldxa0Springxa0Harbor,NY,2001;Tijssen,Hybridizationxa0Withxa0Nucleicxa0Acidxa0Probes,Partxa0I:xa0Theoryxa0andxa0Nucleicxa0Acidxa0Preparation,Laboratoryxa0Techniquesxa0inxa0Biochemistryxa0andxa0Molecularxa0Biology,Elsevierxa0Sciencexa0Ltd.,NY,NY,1993和Ausubel等人Shortxa0Protocolsxa0inxa0Molecularxa0Biology,第4版,Johnxa0Wileyxa0&xa0Sons,Inc.,1999。为了本公开内容的目的,“严格条件”涵盖在其下杂交将仅在杂交分子和靶序列之间存在小于25%错配的情况下发生的条件。“严格条件”可以分解成特定严格水平用于更精确的定义。因此,如本文使用的,“适度严格”条件是在其下具有超过25%序列错配的分子将不杂交的那些;“中严格”的条件是在其下具有超过15%错配的分子将不杂交的那些;并且“高严格”的条件是在其下具有超过10%错配的序列将不杂交的那些。“极高严格”的条件是在其下具有超过6%错配的序列将不杂交的那些。相比之下,在“低严格条件”下杂交的核酸包括具有少得多的序列同一性,或仅在核酸的短子序列上具有序列同一性的那些。因此,应当理解由本公开内容涵盖的核酸的各种变体能够在严格条件下在基本上其整个长度上与SEQxa0IDxa0NO:2、SEQxa0IDxa0NO:4、SEQxa0IDxa0NO:6、SEQxa0IDxa0NO:8、SEQxa0IDxa0NO:10和SEQxa0IDxa0NO:12中的至少一个杂交。蛋白质构建体的产生本文公开的蛋白质构建体可以使用用于重组蛋白质表达和纯化的充分建立的程序来产生。足以指导本领域技术人员的程序可以在下述参考文献中找到:Sambrook等人,Molecularxa0Cloning:xa0Axa0Laboratoryxa0Manual,Coldxa0Springxa0Harborxa0Laboratoryxa0Press,Coldxa0Springxa0Harbor,NY,200;和Ausubel等人Shortxa0Protocolsxa0inxa0Molecularxa0Biology,第4版,Johnxa0Wileyxa0&xa0Sons,Inc.,999。另外和具体细节在下文中提供。编码蛋白质构建体的重组核酸可以通过多种众所周知程序中的任何引入宿主细胞内,例如电穿孔、脂质体介导的转染(例如使用商购可得的脂质体转染试剂,例如LIPOFECTAMINE?2000或TRANSFECTIN?)、磷酸钙沉淀、感染、转染等,这取决于载体和宿主细胞的选择。宿主细胞可以在适当修饰的常规营养培养基中进行培养,用于激活启动子、选择转化体或扩增插入的多核苷酸序列。培养条件例如温度、pH等一般是对于选择用于表达的宿主细胞先前使用的那些,并且对于本领域技术人员且在本文引用的参考文献中将是显而易见的,包括例如Freshney(1994)Culturexa0ofxa0Animalxa0Cells,axa0Manualxa0ofxa0Basicxa0Technique,第3版,Wiley-xa0Liss,Newxa0York和其中引用的参考文献。在某些实施方案中,合适的培养温度是16°C;在其他中37°C。对应于本发明的核酸的表达产物还可以在非动物细胞例如植物、酵母、真菌、细菌等中产生。除Sambrook、Berger和Ausubel外,关于细胞培养的细节可以在下述中找到:Payne等人(1992)Plantxa0Cellxa0andxa0Tissuexa0Culturexa0inxa0Liquidxa0Systemsxa0Johnxa0Wileyxa0&xa0Sons,Inc.xa0xa0Newxa0York,NY;Gamborg和Phillips(编辑)(1995)Plantxa0Cell,Tissuexa0andxa0Organxa0Culture;Fundamentalxa0Methodsxa0Springerxa0Labxa0Manual,Springer-Verlag(Berlinxa0Heidelbergxa0Newxa0York)以及Atlas和Parks(编辑)Thexa0Handbookxa0ofxa0Microbiologicalxa0Media(1993)CRCxa0Press,Bocaxa0Raton,FL。宿主细胞包括重组蛋白质构建体编码核酸的宿主细胞因此也是本公开内容的特征。有利的宿主细胞包括原核(即细菌)宿主细胞,例如大肠杆菌,以及众多真核宿主细胞,包括真菌(例如酵母,例如酿酒酵母(Saccharomycesxa0cerevisiae)和巴斯德毕赤酵母(Picchiaxa0pastoris))细胞、昆虫细胞、植物细胞和哺乳动物细胞(例如CHO细胞)。例如经由载体例如表达载体,将重组蛋白质构建体核酸引入(例如转导、转化或转染)宿主细胞内。如本文描述的,载体最一般是质粒,但此类载体还可以是例如病毒颗粒、噬菌体等。合适表达宿主的例子包括:细菌细胞例如大肠杆菌、链霉菌属(Streptomyces)和鼠伤寒沙门氏菌(Salmonellaxa0typhimurium);真菌细胞,例如酿酒酵母、巴斯德毕赤酵母和粗糙链孢霉(Neurosporaxa0crassa);昆虫细胞例如果蝇(Drosophila)和草地贪夜蛾(Spodopteraxa0frugiperda);哺乳动物细胞例如3T3、COS、CHO、BHK、HEK293或Bowesxa0melanoma;植物细胞包括藻类细胞等。宿主细胞任选就其调节插入序列表达或以所需方式加工表达蛋白质的能力加以选择。蛋白质的此类修饰包括但不限于糖基化(以及例如乙酰化、羧化、磷酸化、脂质化和酰化)。例如将前体形式切割成成熟形式的蛋白质的翻译后加工(例如通过弗林蛋白酶)任选在宿主细胞背景中执行。不同宿主细胞例如3T3、COS、CHO、HeLa、BHK、MDCK、HEK293、WI38等具有用于此类翻译后活性的特定细胞机制和特有机制,且可以选择以确保所引入的异种蛋白质的正确修饰和加工。对于本文公开的重组蛋白质构建体的长期、高收率生产,一般使用稳定表达系统。例如,使用含有病毒复制起点或内源表达元件和选择标记基因的表达载体,将稳定表达蛋白质构建体的核酸分子引入宿主细胞内。在引入载体后,在它们转到选择培养基之前,允许细胞在富集培养基中生长1-2天。选择标记的目的是赋予对于选择的抗性,并且它的存在允许成功表达所引入序列的细胞的生长和回收。例如,稳定转化细胞的抗性组或集落可以使用对于细胞类型合适的组织培养技术进行增殖。用编码蛋白质构建体的核酸转化的宿主细胞任选在适合于来自细胞培养的所编码蛋白质的表达和回收的条件下进行培养。表达的蛋白质构建体可以从重组细胞培养物中回收且纯化,其通过本领域众所周知的许多方法中的任何,包括硫酸铵或乙醇沉淀、酸萃取、过滤、超滤、离心、阴离子或阳离子交换层析、磷酸纤维素层析、疏水作用层析、亲和层析(例如使用本文指出的任何加标签系统)、羟磷灰石层析和凝集素层析。需要时,在成熟蛋白质的完成构型中,可以使用蛋白质重折叠步骤。最后,高效液相层析(HPLC)可以用于最后纯化步骤中。除本文指出的参考文献外,多种纯化法是本领域众所周知的,包括例如下述中阐述的那些:Sandana(1997)Bioseparationxa0ofxa0Proteins,Academicxa0Press,Inc.;和Bollag等人(1996)Proteinxa0Methods,第2版Wiley-Liss,NY;Walker(1996)Thexa0Proteinxa0Protocolsxa0Handbookxa0Humanaxa0Press,NJ,Harris和Angal(1990)Proteinxa0Purificationxa0Applications:xa0Axa0Practicalxa0Approachxa0IRLxa0Pressxa0atxa0Oxford,Oxford,U.K.;Scopes(1993)Proteinxa0Purification:xa0Principlesxa0andxa0Practicexa0第3版Springerxa0Verlag,NY;Janson和Ryden(1998)Proteinxa0Purification:xa0Principles,Highxa0Resolutionxa0Methodsxa0andxa0Applications,第2版Wiley-VCH,NY;和Walker(1998)Proteinxa0Protocolsxa0onxa0CD-ROMxa0Humanaxa0Press,NJ。在特定例子中,经由适合于在原核细胞例如大肠杆菌细胞中的引入和表达的载体将核酸引入细胞内。例如,包括编码蛋白质构建体的多核苷酸序列的核酸可以引入多种商购可得的或专有的(proprietary)载体中的任何内,例如表达载体的pET系列(例如pET9b和pET2d)。编码序列的表达可通过异丙基β-D-1-硫代半乳糖吡喃糖苷(IPTG)诱导,导致高水平的蛋白质表达。编码CASB7439蛋白质构建体的多核苷酸序列在噬菌体T7启动子下转录。包括热诱导型λpL启动子的可替代载体例如pURV22也是合适的。将表达载体引入(例如通过电穿孔)合适的细菌宿主内。大肠杆菌的众多合适菌株是可获得的,并且可以由本领域技术人员进行选择(例如BLRxa0DE3、BL21xa0DE3和Rosettaxa0DE3菌株已证明对于重组载体的表达是有利的,所述重组载体含有编码蛋白质构建体的多核苷酸序列)。任选地,将编码蛋白质构建体的多核苷酸掺入表达载体内,所述表达载体适合于在真核生物(例如昆虫或哺乳动物细胞)中引入和表达。有利地,此类核酸对于在所选载体/宿主细胞中的表达进行密码子最佳化。所选细胞可以是克隆扩增的且对于所需蛋白质构建体的表达进行表征。用于密码子最佳化的技术是本领域已知的。此外,在其他常规技术服务中,商业分子生物学服务供应商提供密码子最佳化。原核生物在细菌系统中,取决于对于表达产物预期的用途,可以选择许多表达载体。例如,当需要大量多肽或其片段用于抗体生产时,有利地采用指导容易纯化的融合蛋白的高水平表达的载体。此类载体包括但不限于多功能大肠杆菌克隆和表达载体,例如BLUEscript(Stratagene),其中目的编码序列例如如本文描述的本发明的多核苷酸可以与β-半乳糖苷酶的用于氨基末端翻译起始甲硫氨酸和后续7个残基的序列在框内一起连接到载体内,产生催化活性的β半乳糖苷酶融合蛋白;pIN载体(Vanxa0Heekexa0&xa0Schuster(1989)Jxa0Biolxa0Chemxa0264:5503-5509);pET载体(Novagen,Madisonxa0WI),其中氨基末端甲硫氨酸与组氨酸标签一起在框内连接;等。在某些实施方案中,合适的载体是pET19;在其他中是pET24;在其他中是pET26。真核生物类似地,在酵母例如酿酒酵母中,含有组成型或诱导型启动子例如α因子、醇氧化酶和PGH的许多载体可以用于所需表达产物的产生。关于综述,参见Berger、Ausubel和例如Grant等人(1987;Methodsxa0inxa0Enzymologyxa0153:516-544)。在哺乳动物宿主细胞中,可以利用许多表达系统,包括质粒和基于病毒的系统。免疫原性组合物药学可接受的载体或赋形剂药学可接受的载体和赋形剂是众所周知的,并且可以由本领域技术人员加以选择。例如,载体或赋形剂可以有利地包括缓冲剂。任选地,载体或赋形剂还含有稳定可溶性和/或稳定性的至少一种组分。增溶/稳定剂的例子包括去污剂例如月桂酰肌氨酸和/或吐温。可替代增溶/稳定剂包括精氨酸、和玻璃形成多元醇(例如蔗糖、海藻糖等)。众多药学可接受的载体和/或药学可接受的赋形剂是本领域已知的,并且例如在Remington’sxa0Pharmaceuticalxa0Sciences,E.xa0xa0W.xa0xa0Martin,Mackxa0Publishingxa0Co.,Easton,PA,第5版(975)中描述。相应地,合适的赋形剂和载体可以由本领域技术人员加以选择,以产生适合于通过所选施用途径递送给受试者的制剂。合适的赋形剂包括但不限于:甘油、聚乙二醇(PEG)、山梨糖醇、海藻糖、N-月桂酰肌氨酸钠盐、L-脯氨酸、非去污剂磺基甜菜碱、盐酸胍、尿素、氧化三甲胺、KCl、Ca²⁺、Mg²⁺xa0、Mn²⁺xa0、Zn²⁺和其他二价阳离子相关的盐、二硫苏糖醇、二硫赤藓醇和β-巯基乙醇。其他赋形剂可以是去污剂(包括:Tween80、Tween20、Tritonxa0X-00、NP-40、Empigenxa0BB、辛基葡糖苷、月桂酰麦芽糖苷、Zwittergentxa03-08、Zwittergentxa03-0、Zwittergentxa03-2、Zwittergentxa03-4、Zwittergentxa03-6、CHAPS、脱氧胆酸钠、十二烷基硫酸钠、溴化十六烷基三甲铵)。佐剂任选地,免疫原性组合物还包括佐剂。在适合于施用于受试者例如人受试者的免疫原性组合物背景中,用于引发针对CASB7439的免疫应答的目的,佐剂选择为引发偏于Th1(Th1xa0biased)的免疫应答。佐剂一般选择为增强组合物施用于其的受试者或受试者群体中偏于Th1的免疫应答。Th1免疫应答“Th1”型免疫应答的特征在于产生IL-2和IFN-γ的CD4+xa0T辅助细胞的诱导。相比之下,“Th2”型免疫应答的特征在于产生IL-4、IL-5和IL-13的CD4+xa0辅助细胞的诱导。TLR影响因子(affectors),包括但不限于3D-MPL用于与修饰的CASB7439多肽组合使用的一种合适的佐剂是TLR-4调节剂。一个例子是脂质A的无毒衍生物,例如单磷酰脂质A或更具体而言3-脱酰基单磷酰(monophoshoryl)脂质A(3D–MPL)。3D-MPL在名称MPL下由GlaxoSmithKlinexa0Biologicalsxa0S.A.销售,并且在文件中自始至终被称为MPL或3D-MPL。参见例如美国专利号4,436,727;4,877,611;4,866,034和4,912,094。3D-MPL主要促进具有IFN-γ(Th1)表型的CD4+xa0T细胞应答。3D-MPL可以根据GB2220211xa0A中公开的方法产生。在化学上,它是具有3、4、5或6条酰化链的3-脱酰基单磷酰脂质A的混合物。在本发明的组合物中,可以使用小颗粒3D-MPL。小颗粒3D-MPL具有这样的粒度,使得它可以通过0.22μm滤器进行无菌过滤。此类制剂在WO94/21292中描述。在其他实施方案中,脂多糖可以是β(1-6)葡糖胺二糖,如美国专利号6,005,099和EP专利号0xa0729xa0473xa0B1中描述的。基于这些参考文献的教导,本领域技术人员将容易地能够产生多种脂多糖,例如3D-MPL。除上述免疫刺激剂(其在结构中类似于LPS或MPL或3D-MPL的那种)外,为本文MPL结构的子部分的酰化单糖和二糖衍生物也是合适的佐剂。在其他实施方案中,佐剂是脂质A的合成衍生物,其中某些描述为TLR-4激动剂,并且包括但不限于:OM174(2-脱氧-6-o-[2-脱氧-2-[(R)-3-十二烷酰氧基十四烷酰基氨基]-4-o-膦酰基-β-D-吡喃葡萄糖基]-2-[(R)-3-羟基十四烷酰氨基]-α-D-吡喃葡萄糖基二氢磷酸酯),(WOxa095/xa014026);OMxa0294xa0DP(3S,9xa0R)–3--[(R)-xa0十二烷酰氧基十四烷酰氨基]-4-氧代-5-氮杂-9(R)-[(R)-3-羟基十四烷酰氨基]癸-1,10-二醇,1,10-双(二氢磷酸酯)(WOxa099/64301和WOxa000/0462);和OMxa0197xa0MP-Acxa0DP(3S-,9R)-3-[(R)-十二烷酰氧基十四烷酰基氨基]-4-氧代-5-氮杂-9-[(R)-3-羟基十四烷酰氨基]xa0癸-1,10-二醇,1xa0-二氢磷酸酯10-(6-氨基己酸酯)(WOxa001/46127)。可以使用的其他TLR-4配体是烷基氨基葡糖苷磷酸盐(AGPs),例如公开于WOxa098/50399或美国专利号6,303,347(还公开了用于制备AGPs的过程)中的那些,适当地RC527或RC529或AGPs的药学可接受的盐,例如公开于美国专利号6,764,840中。某些AGPs是TLR-4激动剂,并且某些是TLR-4拮抗剂。两者都认为作为佐剂是有用的。能够通过TLR-4引发信号应答的其他合适的TLR-4配体(Sabroe等人,JIxa02003第1630-5页)是例如来自革兰氏阴性菌的脂多糖及其衍生物,或其片段,特别是LPS的无毒衍生物(例如3D-MPL)。其他合适的TLR激动剂是:热休克蛋白(HSP)10、60、65、70、75或90;表面活性剂蛋白A、透明质酸寡糖、硫酸肝素片段、纤连蛋白片段、纤维蛋白原肽、b-防御素-2和胞壁酰二肽(MDP)。在一个实施方案中,TLR激动剂是HSPxa060、70或90。其他合适的TLR-4配体是如WOxa02003/011223和WOxa02003/099195中所述的,例如在WO2003/011223的第4-5页上或在WO2003/099195的第3-4页上公开的化合物I、化合物II和化合物III,且特别是在WO2003/011223中作为ER803022、ER803058、ER803732、ER804053、ER804057、ER804058、ER804059、ER804442、ER804680和ER804764公开的那些化合物。例如,一种合适的TLR-4配体是ER804057。皂苷佐剂可以在免疫原性组合物中例如单独或与3D-MPL或本文描述的另一种佐剂组合与CASB7439一起使用的其他佐剂是皂苷例如QS21。皂苷在Lacaille-Dubois,M和Wagnerxa0H.xa0(1996.xa0xa0Axa0reviewxa0ofxa0thexa0biologicalxa0andxa0pharmacologicalxa0activitiesxa0ofxa0saponins.xa0xa0Phytomedicine第2卷第363-386页)中教导。皂苷是广泛分布于植物和海洋动物界中的类固醇或三萜糖苷。皂苷因在水中形成胶体溶液而出名,所述胶体溶液在振荡后发泡,并且用于沉淀胆固醇。当皂苷接近细胞膜时,它们在膜中产生孔样结构,这引起膜爆裂。红细胞的溶血是这种现象的一个例子,这是某些但并非全部皂苷的性质。皂苷特别是免疫学活性的皂苷级分已知作为在用于全身施用的疫苗中的佐剂。个别皂苷的佐剂和溶血活性已在本领域中得到广泛研究(Lacaille-Dubois和Wagner,同上)。例如,Quilxa0A(衍生自南美洲树Quillajaxa0Saponariaxa0Molina的树皮)及其级分在USxa05,057,540和"Saponinsxa0asxa0vaccinexa0adjuvants",Kensil,C.xa0xa0R.,Critxa0Revxa0Therxa0Drugxa0Carrierxa0Syst,1996,12(1-2):1-55;和EPxa00xa0362xa0279xa0B1中描述。包含Quilxa0A级分的称为免疫刺激复合物(ISCOMS)的特定结构是溶血的,并且已用于疫苗制造中(Morein,B.,EPxa00xa0109xa0942xa0B1;WOxa096/11711;WOxa096/33739)。溶血皂苷QS21和QS17(Quilxa0A的HPLC纯化级分)已描述为有效的全身佐剂,并且其生产方法公开于美国专利号5,057,540和EPxa00xa0362xa0279xa0B1中。已用于全身疫苗接种研究中的其他皂苷包括衍生自其他植物物种例如石头花属(Gypsophila)和肥皂草属(Saponaria)的那些(Bomford等人,Vaccine,10(9):572-577,1992)。当连同抗原一起配制时,包含QS21和胆固醇的此类制剂已显示是成功的Th1刺激佐剂。因此,例如,CASB7439可以有利地与包含QS21和胆固醇的组合的佐剂一起用于免疫原性组合物中。免疫刺激性寡聚核酸用于与CASB7439组合使用的一种合适佐剂是能够通过TLR-9引起信号应答的细菌DNAxa0TLR激动剂,即TLR-9激动剂,更具体而言含有非甲基化CpG核苷酸的DNA,特别是称为CpG基序的序列背景。含CpG寡核苷酸诱导占优势地Th1应答。此类寡核苷酸是众所周知的,并且例如在WOxa096/02555,WOxa099/33488以及美国专利号6,008,200和5,856,462中描述。适当地,CpG核苷酸是CpG寡核苷酸。用于在本发明的免疫原性组合物中使用的合适寡核苷酸是含CpG寡核苷酸,任选含有由至少3个、适当地至少6个或更多核苷酸分开的2个或更多二核苷酸CpG基序。CpG基序是胞嘧啶核苷酸随后为鸟嘌呤核苷酸。本发明的CpG寡核苷酸一般是脱氧核苷酸。在一个特定实施方案中,寡核苷酸中的核苷间是二硫代磷酸酯或适当地硫代硫酸酯键,尽管磷酸二酯和其他核苷间键也在本发明的范围内。在某些实施方案中是具有混合的核苷间键合的寡核苷酸。用于产生硫代磷酸酯寡核苷酸或二硫代磷酸酯的方法在美国专利号5,666,153,5,278,302和WOxa095/26204中描述。在一个可替代实施方案中,使用能够通过TLR-9引起信号应答的TLR激动剂。在一个实施方案中,能够通过TLR-9引起信号应答的TLR激动剂是HSP90。不同佐剂例如本文提及那些的组合也可以用于具有CASB7439的组合物中。例如,如已指出的,QS21可以连同3D-MPL一起配制。QS21xa0:xa03D-MPL的比值一般将在1xa0:xa010至10xa0:xa01的级别中,例如1:5至5xa0:xa01,且通常基本上1xa0:xa01。一般地,比值在2.5xa0:xa01至1xa0:xa01xa03D-MPL:xa0QS21的范围中。另一种组合佐剂是在脂质体制剂中的3DMPL加上QS21,也与CpG组合。具有结肠直肠癌的受试者用于参与本文描述的方法中的具有结肠直肠癌的受试者的选择可以通过临床诊断、分子诊断或其组合。在某些实施方案中,受试者进行测试,以测定其癌细胞是否表达CASB7439(HASH2)。用于诊断结肠直肠癌的临床方法是本领域已知的。用于测定癌细胞或组织是否表达CASB7439(HASH2)的分子技术和方法公开于WO01/62778中。实验实施例实施例1在pET19b载体中生成编码包含CASB7439多肽的蛋白质构建体的2种核酸分子。His标签与CASB7439序列的N末端并列。这些克隆分别命名为LVL007xa0[SEQxa0IDxa0NO:15(aa);SEQxa0IDxa0NO:16(DNA)]和LVL010xa0[SEQxa0IDxa0NO:17(aa);SEQxa0IDxa0NO:18(DNA)]。观察到非故意突变已在LVL007克隆中出现,导致脯氨酸到亮氨酸的一个氨基置换(在就SEQxa0IDxa0NO:13而言的氨基酸残基17上)。核酸分子对于3种不同宿主细胞类型利用,即大肠杆菌菌株BLRxa0DE3、BL21xa0DE3和Rosettaxa0DE3。诱导以2个温度/诱导(16°C或37°C)且用1mMxa0IPTG执行。关于方案细节,参见下文材料与方法节段。对于每次诱导收获蛋白质,并且通过蛋白质印迹和通过SDS-PAGE用考马斯蓝染色进行分析。在这些实验中,蛋白质的检测仅在蛋白质印迹中可见。实施例2执行CASB7439基因的生物信息学分析,揭示下述结构特征:●xa0定位于SEQxa0IDxa0NO:14的核苷酸2xa0-xa027之间的发夹RNA结构元件●xa0核苷酸序列的62%GC含量●xa0富含精氨酸密码子的核苷酸序列(编码的26/193个氨基酸)●xa0具有高水平的碱性氨基酸残基的氨基酸序列●xa0具有高等电点(11.18)的氨基酸序列●xa0在氨基酸序列内的低复杂性区域(SEQxa0IDxa0NO:13的残基7-27●xa0在氨基酸序列内的螺旋-环-螺旋结构域(HLH)(IPR000014)(SEQxa0IDxa0NO:13的残基56-108)●xa0在氨基酸序列内的固有无序的第一个区域(SEQxa0IDxa0NO:13的残基118-164)●xa0在氨基酸序列内的固有无序的第二个区域(SEQxa0IDxa0NO:13的残基118-164)。申请人还鉴定了从氨基酸127到158的具有高脯氨酸周期性的区域。申请人将SEQxa0IDxa0NO:13(aa)的包括133和153在内的来自氨基酸133-153的区域指名为富含脯氨酸的区域。富含脯氨酸的区域连同这个实施例中提及的某些其他特征一起,连同在本文中其他地方提及的区域一起以示意方式在图1/35中描述。实施例3未修饰的CASB7439xa0DNA核苷酸序列(SEQxa0IDxa0NO:14)通过商业DNA合成服务供应商,Geneart(独特标识符0606597)进行密码子最佳化且克隆。Geneartxa0AG,BioPark,Josef-Engert-Str.xa0xa011D-93053xa0Regensburg,德国。CASB7439核苷酸序列通过PCR扩增得自克隆,且用于生成2种构建体。在第一种构建体LVL016xa0[SEQxa0IDxa0NO:29(aa),SEQxa0IDxa0NO:30(DNA)]中,将CASB7439序列插入pET21b(+)载体中与在CASB7439序列的N末端上的pD1/3蛋白质(来自流感嗜血杆菌)融合。在第二种构建体LVL018xa0[SEQxa0IDxa0NO:31(aa);SEQxa0IDxa0NO:32(DNA)]中,将CASB7439插入pET21b(+)载体中(不含任何蛋白质D组分)。这些构建体就在16°C和37°C用1mMxa0IPTG在BLRxa0DE3大肠杆菌中的生产进行评估。生产是可通过蛋白质印迹作为不溶性蛋白质检测的,主要在16°C产生。选择4个CASB7439结构域用于进一步研究,以改善蛋白质生产:核靶向结构域、富含脯氨酸的区域、DNA结合结构域和HLH结构域。实施例4选择CASB7439的核靶向结构域、DNA结合结构域、bHLH结构域和富含脯氨酸的区域,以研究来自包含编码CASB7439多肽的核苷酸序列的构建体的蛋白质生产。xa0CASB7439核苷酸序列的不同区段由本文描述的密码子最佳化的Geneart克隆进行PCR扩增且插入pET19b(+)载体中,导致具有不同CASB7439序列的5种构建体(以某些方式或完全截短);每种构建体在CASB7439序列的N末端具有多组氨酸尾部。参见图2/35。在图2/35上显示的这些构建体就在37°C和16°C用1mMxa0IPTG在BLRxa0DE3大肠杆菌菌株中的蛋白质表达进行评估。如图2/35中所述,这些构建体包含全长CASB7439xa0[LVL060,SEQxa0IDxa0NO:19(aa),SEQxa0IDxa0NO:20(DNA)];截短以去除核靶向结构域的CASB7439xa0[Const-1,SEQxa0IDxa0NO:21(aa),SEQxa0IDxa0NO:22(DNA)];截短以去除富含脯氨酸的区域的CASB7439xa0[LVL055,SEQxa0IDxa0NO:1(aa),SEQxa0IDxa0NO:2(DNA)];截短以去除DNA结合结构域的CASB7439[LVL056,SEQxa0IDxa0NO:23(aa),SEQxa0IDxa0NO:24(DNA)];截短以留下碱性螺旋-环-螺旋(bHLH)结构域的CASB7439xa0[LVL057,SEQxa0IDxa0NO:25(aa),SEQxa0IDxa0NO:26(DNA)]。由于实验误差,Const-1缺乏终止密码子,导致载体核苷酸序列的部分的翻译(导致在C末端区域中具有另外21个氨基酸,从LED...开始)。在16°C温育后LVL055的产生(C末端截短的)在考马斯蓝染色的SDS-PAGE凝胶上是可明确检测的。实施例5基于实施例4中所述的结果,设计新构建体,以(i)去除富含脯氨酸的区域,同时(ii)保留多肽的C末端部分的其他区域。参见图3/35和4/35的描述,这讨论了(i)在多肽内的各种鉴定或预测表位,和(ii)用于去除富含脯氨酸的区域的各种可替代方法。随后由Geneart(独特标识符0706840)定购编码修饰的CASB7439多肽的密码子最佳化的合成核酸基因序列,消化且平行插入2种不同载体中,以生成下述构建体:(i)LVL088,包含具有21氨基酸富含脯氨酸的区域缺失的CASB7439基因,在pET26b(+)载体中的C末端上与多组氨酸尾部融合(SEQxa0IDxa0NO:27(aa),SEQxa0IDxa0NO:28(DNA))和(ii)LVL111,包含具有21氨基酸富含脯氨酸的区域缺失,以及在pET19b(+)载体中的N末端和C末端的多组氨酸尾部的CASB7439基因(SEQxa0IDxa0NO:3(aa),SEQxa0IDxa0NO:4(DNA))。LVL111构建体(参见SEQxa0IDxa0NO:3)根据用于LVL055的相同策略进行克隆,即,使用包括由10个组氨酸组成的多组氨酸尾部随后为肠激酶位点的pET19(+)载体。这导致在N末端的23氨基酸融合配偶体(SEQxa0IDxa0NO:42)。生成具有实施例3(独特标识符0606597)中讨论的密码子最佳化的合成基因的其他构建体,包括下述:●xa0LVL090(包含(从N末端起)在pET21载体中的蛋白质D、全长最佳化的CASB7439和6-His的蛋白质构建体)(SEQxa0IDxa0NO:43(aa);SEQxa0IDxa0NO:44(DNA))●xa0LVL112(包含(从N末端起)在pSUMO载体中的SUMO蛋白质、全长最佳化的CASB7439的蛋白质构建体)(SEQxa0IDxa0NO:45(aa);SEQxa0IDxa0NO:46(DNA))●xa0LVL113(包含(从N末端起)在pSUMO载体中的SUMO蛋白质、pD1/3蛋白质、全长最佳化的CASB7439的蛋白质构建体)(SEQxa0IDxa0NO:47(aa);SEQxa0IDxa0NO:48(DNA))●xa0LVL114(包含(从N末端起)在pSUMO载体中的SUMO蛋白质、在氨基酸117上截短的CASB7439的蛋白质构建体)(SEQxa0IDxa0NO:49(aa);SEQxa0IDxa0NO:50(DNA))●xa0LVL115(包含(从N末端起)在pSUMO载体中的SUMO蛋白质、具有富含脯氨酸的区域去除的修饰的CASB7439的蛋白质构建体)(SEQxa0IDxa0NO:51(aa);SEQxa0IDxa0NO:52(DNA))未观察到生产改善,尽管执行仅一次重复(数据未显示)。LVL088的生产在37°C和在16°C用1mMxa0IPTG过夜温育后进行分析。当电泳分析时,LVL088生产仅通过蛋白质印迹进行显现。来自4个800xa0mL培养瓶的一个纯化批次导致0.4xa0mg蛋白质。另一方面,LVL111在考马斯蓝染色后是可容易检测的。产生重组蛋白质LVL111且经过8个批次进行纯化。估计LVL111的几个批次(各自来自4个800xa0mL培养瓶),以产生在3.3xa0mg/批次到10xa0mg/批次范围中的纯化蛋白质。因此,LVL088的生产低于对于LVL111可见的那种。纯化蛋白质也就其与几种抗CASB7439单克隆抗体的反应性进行测试,并且在所有情况下获得阳性反应性。实施例6研究了C末端多组氨酸尾部从LVL111构建体中的去除。编码polypro(-)CASB7439多肽而无编码C末端多组氨酸的部分的核酸分子通过PCR从LVL111构建体扩增,且克隆到pET19b载体内。将这种构建体指名为LVL137。LVL137构建体基本上是LVL111,而无编码C末端多组氨酸尾部的核苷酸序列。SEQxa0IDxa0NO:5(aa);SEQxa0IDxa0NO:6(DNA)。C末端多组氨酸尾部的去除对生产水平没有明显影响。如通过考马斯染色的SDS-PAGE凝胶分析的,LVL137产生与LVL111相同水平的蛋白质。编码polypro(-)CASB7439多肽的核酸分子随后通过PCR从Geneart(0706840)合成的CASB7439序列进行扩增,且克隆到在N末端具有6多组氨酸标签的pET26载体内(LVL138)。SEQxa0IDxa0NO:33(aa);SEQxa0IDxa0NO:34(DNA)。这种构建体显示出明显减少水平的蛋白质生产,且难以通过蛋白质印迹检测。在pET24卡那霉素抗性载体中生成编码在polypro(-)CASB7439多肽的N末端上的6多组氨酸标签的核酸分子。利用新接头设计,以去除在多组氨酸标签序列和CASB7439基因的5"末端之间产生的发夹结构。具体地,关于蛋白质构建体的前8个氨基酸残基的密码子改变为下述核苷酸序列:5’xa0ATGxa0CATxa0CATxa0CATxa0CATxa0CATxa0CATxa0GAC...xa03’(SEQxa0IDxa0NO:35)。(原始密码子是5’xa0ATGxa0xa0CACxa0CATxa0CACxa0xa0CATxa0xa0CACxa0CATxa0xa0GAT...xa03’(SEQxa0IDxa0NO:36)。)将这种构建体指名为LVL160。SEQxa0IDxa0NO:37(aa);SEQxa0IDxa0NO:38(DNA)。通过凝胶和蛋白质印迹分析,蛋白质生产看起来与用LVL138获得的那种一样弱。在pET24卡那霉素抗性载体中生成编码在polypro(-)CASB7439多肽的N末端上具有10多组氨酸标签的蛋白质构建体的核酸分子。将这种构建体鉴定为LVL168。SEQxa0IDxa0NO:11(aa);SEQxa0IDxa0NO:12(DNA)。生产水平与对于LVL111观察到的水平相当。这个实施例中讨论的几种构建体的比对在图5/35中发现。关于这个实施例和实施例1中讨论的构建体的结果在下表1中概括。xa0xa0# LVL描述载体生产LVL007长His-CASB7439pET19b(+)凝胶-/印迹+LVL010长His-CASB7439pET19b(+)凝胶-/印迹+LVL016pD1/3-CASB7439-OPT-6HispET21b(+)凝胶-/印迹 +LVL111长His-Del-多-Pro-结构域-His-OPTpET19b(+)凝胶+++/ 印迹 +++LVL137长His-Del-多-Pro-结构域-OPTpET19b(+)凝胶+++/印迹 +++LVL1386His-Del-多-Pro-结构域-OPTpET26b(+)凝胶-/ 印迹 +LVL160His基序--Del-多-pro-结构域-OPTpET24b(+)凝胶-/印迹 +LVL16810His-del-多-pro-结构域-OPTpET24b(+)凝胶+++/ 印迹 +++表1.xa0xa0关于实施例1、3和6中讨论的构建体的表达水平。当对全细胞裂解物实施SDS-PAGE时,导致“凝胶-/印迹+”生产的构建体一般仅通过蛋白质印迹可见。当对全细胞裂解物实施SDS-PAGE时,导致“凝胶+++/印迹+++”生产的构建体通过考马斯蓝染色是明确可见的。6His:xa0组氨酸标签=xa06个组氨酸残基长Hisxa0=xa023aa(MGHHHHHHHHHHSSGHIDDDDKH)(SEQxa0IDxa0NO:42)Del-多-Pro-结构域:xa0通过富含脯氨酸的区域的缺失修饰的CASB7439OPT:xa0密码子最佳化的His基序:xa0对于密码子选择修饰的组氨酸标签(参见本文,实施例6),1/3pD:xa0本文描述的蛋白质D构建体10His:xa0具有10个组氨酸残基的组氨酸标签。实施例7生成与来自流感嗜血杆菌的蛋白质D片段融合的另一种CASB7439构建体。如SEQxa0IDxa0NO:39(aa)(SEQxa0IDxa0NO:40(DNA))中所示,使氨基酸Met-Asp-Pro与经加工的蛋白质D的108个N末端氨基酸融合(经加工的蛋白质D的氨基酸残基2-109)。SEQxa0IDxa0NO:39在本文中被称为1/3pD或1/3蛋白质D。将得自Geneart(0706840)的合成CASB7439核苷酸序列(富含脯氨酸的区域缺失的)在pET26-1/3pD中进行亚克隆,所述pET26-1/3pD是含有1/3pD的卡那霉素抗性质粒,以获得LVL141。LVL141的序列在SEQxa0IDxa0NO:7(aa)和SEQxa0IDxa0NO:8(DNA)中阐述。生产与LVL111相当。该克隆随后通过PCR突变,以去除在1/3pD和CASB7439组分之间的4氨基酸接头(Ala-Ala-Ala-His)。指名为LVL144的所得到的构建体的序列在SEQxa0IDxa0NO:9(aa)和SEQxa0IDxa0NO:10(DNA)中阐述。生产与LVL111相当。图6/35显示CASB7439(SEQxa0IDxa0NO:13);LVL168(SEQxa0IDxa0NO:12)、PD1/3(SEQxa0IDxa0NO:39)和LVL144(SEQxa0IDxa0NO:9)的比对。实施例8LVL168的溶解测试一般地,将包含CASB7439的纯化蛋白质构建体在6M胍缓冲液中溶解,转移至8M尿素缓冲液,并且贮存于4M尿素、20mMxa0HEPES、1mMxa0TCEP、150mMxa0NaCl,pH7.0中。以小体积执行的初步结果暗示LVL168还可以溶解于不含尿素或任何还原剂例如EDTA或TCEP,且含或不含NaCl的磷酸盐缓冲液中。在这些缓冲液中透析后未观察到沉淀。执行溶解分析,以表征在表2中列出的16种缓冲液中的LVL168蛋白质。将在8M尿素缓冲液、20mMxa0HEPES、150mMxa0NaCl、1mMxa0TCEP,pH7.0中的100微升纯化的LVL168蛋白质样品放到先前通过2次冲洗用缓冲液条件化的小型透析单元10000xa0MWCO(Biolynx)内。透析在4°C搅拌下在各100mL表2中列出的16种缓冲液中执行过夜。随后从单元中收获样品,放到eppendorfs内且以20,000g离心5分钟。可溶蛋白质悬浮停留但不溶性蛋白质沉淀,并且在离心后导致团块。其中LVL168蛋白质是可溶的缓冲液在表2中列出。通过凝胶SDS-PAGE测试上清液,并且通过RCxa0DC法使用制造商的说明书测量其余可溶蛋白质的浓度。用于执行改良Lowry法的RCxa0DC法的试剂盒可从BioRadxa0Laboratories,1000xa0Alfredxa0Nobelxa0Drive,Hercules,CAxa094547)获得。样品维持于4°C用于稳定性测试。LVL168的稳定性测试来自可溶性测定的LVL168蛋白质维持于4°C,7天。将各20微升样品2、3、5、6、9xa0-xa016转移到其他管,并且就其在4°C、37°C或室温的稳定性测试另外2天。将样品以20,000g离心5分钟。通过SDS-PAGE分辨上清液,并且通过与原始纯化蛋白质比较,就降解、聚集或蛋白质丧失分析概况。蛋白质在测试的大多数缓冲液中是稳定的。xa0xa0样品 #缓冲液可溶性1PBS 1X pH7.3不可溶22M尿素、20mM Tris、150mM NaCl xa0+ 1mM TCEP,pH 8.0可溶的34M尿素、20 mM Tris、150mM NaCl xa0+ 1mM TCEP,pH 7.0可溶的4PBS 1X、1mMTCEP、1mM EDTA,pH7.3不可溶510mM NaAc 1mMxa0 EDTA.xa0 1mM、TCEP、5mM NaCl ,pH 5.01可溶的620mM咪唑(Imidazol)、150mM、NaCl 、1mMxa0 EDTA、1mM TCEP,pH 6.0可溶的720mM N-二(羟乙基)甘氨酸、138 mM NaCl、1mM EDTA、1 mM TCEP,pH 8.7不可溶850 mM Tris、250 mM NaCl、27 mM蔗糖、0.1%Tween80、1mMTCEP,pH 8.5不可溶950mM Tris、250mM NaCl 、270mM蔗糖、0.3ML-精氨酸、1mM TCEP、 pH 8.5可溶的1020mM Na₂HPO₄、150mM NaCl 、1mM EDTA + 1mM TCEP,pH 6.0可溶的1120mM N3₂HPO₄、5Mm NaCl 、1mM EDTA + 1Mm TCEP,pH 6.0可溶的1220mM Na₂HPO₄、5mM NaCl 、1mM EDTA pH 6.0可溶的13.20mM Na₂HPO₄、5mM NaCl xa0+ 1mM TCEP + pH 6.0可溶的1420mM Na₂HPO₄、5mM NaCl xa0pH 6.0可溶的1520mM Na₂HPO₄、5mM NaCl xa0pH 6.5可溶的1620mM Na₂HPO₄、150mM NaCl xa0pH 6.0可溶的表2.xa0LVL168的可溶性和稳定性测试。为了读者的方便,本文提及的构建体及其相对生产的概括在表3中提供。xa0xa0# LVL描述载体生产LVL007长His-CASB7439pET19b(+)凝胶-/印迹+LVL010长His-CASB7439pET19b(+)凝胶-:印迹+LVL016pD1/3-CASB7439-OPT-6HispET21b(+)凝胶-/印迹 +LVL018CASB7439-OPT-6HispET21b(+)凝胶-/印迹 +Const-1长His-CASB7439-OPT-Const-1(核靶向trunc.)pET19b(+)凝胶-/ 印迹 +LVL055长His-聚-Pro-结构域-trunc-OPTpET19b(+)凝胶+++/印迹 +++LVL056长His-DNA结合 trunc-OPTpET19b(+)凝胶-/印迹 -LVL057长His-单独的bHLH -OPTpET19b(+)凝胶-/印迹 -LVL060长His-C7439-OPTpET19b(+)凝胶-/印迹 +LVL088Del-聚-Pro-结构域-OPT-6HispET26b(+)凝胶-/印迹 +LVL111长His-Del-聚-Pro-结构域-His-OPTpET19b(+)凝胶+++/ 印迹 +++LVL137长His-Del-聚-Pro-结构域-OPTpET19b(+)凝胶+++/印迹 +++LVL1386His-Del-聚-Pro-结构域-OPTpET26b(+)凝胶-/ 印迹 +LVL1411/3pD-Del-聚-Pro-结构域-OPT-6HispET26b(+)凝胶+++/印迹 +++LVL1441/3pD-Del-聚-Pro-结构域-OPTHis mut接头pET26b(+)凝胶+++/ 印迹 +++LVL160His基序--Del-聚-pro-结构域-OPTpET24b(+)凝胶-/印迹 +LVL16810His-del-聚-pro-结构域-OPTpET24b(+)凝胶+++/ 印迹 +++表3.xa0xa0参见表1缩写。下述另外缩写在表3中利用:trunc:xa0截短的const:xa0构建体mut:xa0突变以去除在pD1/3和修饰的CASB7439多肽之间的无关氨基酸的序列接头:xa0在分子的2部分之间的无关氨基酸DNA结合:xa0DNA结合结构域单独的bHLH:xa0碱性螺旋-环-螺旋结构域。材料与方法表达–小规模诱导:用本文提及的构建转化大肠杆菌BLR(DE3)菌株,放到含合适抗生素(40xa0μg/ml卡那霉素或100xa0μg/ml羧苄青霉素)的Luriaxa0Broth(LB)琼脂板上,并且在37°C温育过夜。所得到的细菌菌苔用于接种含合适抗生素(40xa0μg/ml卡那霉素或100xa0μg/ml羧苄青霉素)的20mLxa0LBxa0Alternativexa0Proteinxa0Source(APS)培养基,并且放在37°C以达到0.5xa0-xa01.0的OD600。在16°C或37°C,通过1mMxa0IPTG的添加完成诱导。为了在16°C诱导,在诱导重组蛋白质表达前,使生长培养物在冰上冷却1小时。随后将培养物放回以在16°C生长,且在这些条件下维持16小时。为了在37°C诱导,通过将IPTG加入生长培养物中,立即诱导重组蛋白质的表达。诱导在37°C维持3小时。在诱导前和后获得1mL的小等分试样。随后将等分试样离心(10分钟,4°C,20000xa0×xa0g),并且将细菌团块维持在-20°C直至分析时。根据制造商的推荐在BugBuster蛋白质提取后执行分析。由Novagen制造的BugBuster从VWR商购可得。通过SDS-PAGE凝胶的考马斯蓝染色且通过蛋白质印迹测定表达水平。在检测来自BugBuster的提取的团块或上清液中的蛋白质后评估可溶性。表达–大规模诱导:用如本文描述的构建转化大肠杆菌BLR(DE3)菌株,放到含合适抗生素的LB琼脂板上,并且在37°C温育过夜。所得到的细菌菌苔用于接种含合适抗生素(40xa0μg/ml卡那霉素或100xa0μg/ml羧苄青霉素)的LBxa0APS培养基的所需数目800xa0mL烧瓶中,并且放在37°C以达到0.5xa0-xa01.0的OD₆₀₀。随后在通过加入1mMxa0IPTG诱导重组蛋白质表达前,使含有800ml生长培养物的2.5L烧瓶在冰上冷却1小时。为了在16°C诱导,在诱导前使生长培养物在冰上冷却1小时。随后将培养物放回以在16°C生长,且在这些条件下维持16小时。将培养物离心(15分钟,4°C,6000xa0×xa0g),并且将细菌团块维持在-80°C直至纯化过程时。还在诱导前和后获得1mL的小等分试样用于BugBuster且在纯化前通过SDS-PAGE和蛋白质印迹分析。纯化将细菌团块重悬浮于裂解缓冲液(含有500xa0mMxa0NaCl、10mMxa0TCEP的20xa0mMxa0Tris缓冲液(pHxa08.0))和蛋白酶抑制剂的混合物(完全无EDTA)中。通过超声处理使用13mm探针在Vibra细胞超声处理器上,通过Emulsiflexxa0C3(Avestin)或用恒定细胞破坏系统(Constantxa0System)裂解细菌。通过以20xa0000g在4°C离心20分钟分离可溶性(上清液)和不溶性(团块)组分。因为预期CASB7439重组蛋白质在团块中,所以弃去上清液。通常,将不溶性组分(团块)再溶解于含有6M胍HCl、500mMxa0NaCl、10mMxa0TCEP的50mMxa0N二羟乙基甘氨酸缓冲液pHxa08.0中,并且随后离心(20xa0000xa0×xa0g,20分钟)。将上清液装载到已在先前缓冲液中预平衡但具有低至1mM的TCEP浓度的5mlxa0Hisxa0Trap柱(GExa0Healthcare)上。在装载后,用相同缓冲液将柱洗涤1次。6Mxa0GnHCl离液剂替换为8M尿素(8M尿素、20mMxa0HEPES、500mMxa0NaCl、1mMxa0TCEP,pHxa08.0)。使用含有8M尿素、500mMxa0NaCl、1mMxa0TCEP和250xa0mM咪唑的20mMxa0HEPES缓冲液(pHxa08.0)执行洗脱。通过SDS-PAGE分析来自洗脱级分的样品,并且合并含有目的蛋白质的级分,需要时在离心装置上浓缩,并且用于第二步纯化。取决于需要的纯度,在最后一个脱盐步骤前,在8M尿素、20mMxa0HEPES、500xa0mMxa0NaCl、1mMxa0TCEP,pHxa08,0中,完成SEC(尺寸排阻层析)(Superdexxa0200,GExa0Healthcare)的一个或两个步骤。在用含有4M尿素、150mMxa0NaCl和1mMxa0TCEP的最终20mMxa0HEPES缓冲液(pHxa07.0)预平衡的G25脱盐柱上完成脱盐。蛋白质样品在管中1ml等分且贮存于-80°C。蛋白质分析—浓度测定使用RCxa0DC蛋白质测定(通过BioRad的改良Lowry法)测定蛋白质浓度。由于最终缓冲液的某些组分与常规Lowry或BCA测定(尿素和还原剂的高含量)的不相容性,使用该测定。也通过SDS-PAGE、蛋白质印迹并且对于LAL含量分析已知数量的最终蛋白质制剂,以评估聚集或降解、大肠杆菌蛋白质和LPS污染水平。实施例9在正常和结肠直肠癌(CRC)组织中的CASB7439表达验证申请人在得自Corixaxa0Corporation的83个CRC样品和12个正常结肠样品中执行CASB7439xa0mRNA表达的实时qPCR分析。与正常组织比较,与测试的63%xa0CRC样品中的正常结肠比较,CASB7439xa0mRNA在CRC中是至少10倍超表达的(数据报道为平均CASB7439/β-肌动蛋白表达比值)(图7/35)。此外,申请人使用兔抗CASB7439单克隆抗体(40-12)(本文其他地方讨论的抗体)通过免疫荧光(IF)在人CRC组织中检测CASB7439蛋白质;在正常相邻组织切片中未检测到CASB7439蛋白质。使用标准技术通过GeneLogic(Genexa0Microarray)分析,生成关于CASB7439的另外表达数据。发现CASB7439xa0mRNA在来自疾病的所有阶段的CRC样品中是高度表达的(数据未显示)。申请人在得自Corixaxa0Corporation的83个CRC样品和12个正常结肠样品中执行CASB7439xa0mRNA表达的实时qPCR分析。与正常组织比较,与测试的63%xa0CRC样品中的正常结肠比较,CASB7439xa0mRNA在CRC中是至少10倍超表达的(数据报道为平均CASB7439/β-肌动蛋白表达比值)(图7/35)。独立参考文献报道了CASB7439即HASH-2xa0mRNA通过原位杂交(ISH)以极低水平在结肠隐窝底部但不在除胎盘外的任何其他正常组织中的检测。Jubb等人(2006)Oncogenexa025:xa03445-3457。在结肠直肠癌(CRC)组织中,CASB7439xa0mRNA已显示在测试的70%人组织中是15倍超表达的。在CRC和正常相邻结肠组织中的CASB7439蛋白质表达为了通过免疫荧光在正常和CRC组织中分析CASB7439蛋白质表达,开发了特异性兔抗CASB7439单克隆抗体(40-12)。针对CASB7439产生的兔杂交瘤得自商业供应商Epitomicsxa0Inc.,并且由申请人筛选。使用重组蛋白质LVL111(SEQxa0IDxa0NO:3)通过ELISA,首先筛选通过杂交瘤产生的mAbs。使用LVL111和得自改造为表达CASB7439的重组细胞系的细胞裂解物,通过蛋白质印迹验证mAbs的特异性(参见下文,TC1/CASB7439)。通过免疫荧光用mAbs评价在TC1/CASB7439肿瘤(在小鼠中生长)、SW-620和SW-480细胞(CASB7439阳性人结肠直肠癌细胞系)中、和在HCT-116细胞(CASB7439阴性人结肠直肠癌细胞系)中的CASB7439蛋白质表达。选择mAbxa040-12用于CASB7439蛋白质表达验证。申请人从NDRI(Nationalxa0Diseasexa0Researchxa0Interchange,8xa0Pennxa0Center,8^thxa0Floor,1628xa0JFKxa0Boulevard,Philadelphia,PAxa019103)获得来自17个不同个体的CRC和正常相邻组织的OCT包埋的冷冻组织样品;对于这些个体中的5个,还获得转移性组织。申请人筛选了17个原发性肿瘤、17个正常相邻组织和5个转移灶。在分析的17个原发性CRC肿瘤中,13个对于CASB7439蛋白质表达是阳性的(76.5%)。所有这些CASB7439阳性样品是腺癌。正常相邻组织无一表达可检测水平的CASB7439蛋白质。在转移性组织中,5个中的3个对于CASB7439蛋白质表达是阳性的(60%)。通过使用常规技术在癌症和正常相邻结肠组织上执行的实时qPCR分析,在16个CRC组织中研究在CASB7439蛋白质和mRNA表达之间的关联。Ki67染色用作增殖标记。在CASB7439蛋白质和mRNA表达之间的关联在图xa08/35中呈现。通过免疫荧光显示出CASB7439蛋白质的组织样品也展示最高的CASB7439xa0mRNA水平。实施例10在小鼠中CASB7439的免疫原性:在近交小鼠中的CASB7439xa0T细胞免疫原性为了研究在小鼠中CASB7439的T细胞免疫原性,通过常规合成法生成肽库,以覆盖CASB7439蛋白质的整个序列(图xa09/35)。每种肽是15聚体,与下一个肽重叠11个氨基酸。为了研究免疫显性区域,根据矩阵排列14个肽库,从而使得任何2个肽库具有仅一个共同肽(图xa010/35)。对于在小鼠中的T细胞免疫原性研究,高达15只近交小鼠和高达10只远交小鼠/组已接受每2周的4次肌内免疫接种,用各种剂量(从0到30μg)的用AS01B或AS15配制的各种重组CASB7439蛋白质,这2者都是GSK专有的佐剂。一旦与抗原一起配制,AS01B就由在脂质体中的MPL(100μg/ml)和QS21(100μg/ml)组成。一旦与抗原一起配制,AS15就由在脂质体中的MPL(100μg/ml)、QS21(100μg/ml)和CpG7909(840xa0μg/ml)组成。每次免疫接种含有与25μlxa02X浓度佐剂混合的25μl重组CASB7439蛋白质。因此,在AS01B组中的每只小鼠接受5xa0μgxa0MPL和5xa0μgxa0QS21。在AS15组中的每只小鼠接受5xa0μgxa0MPL、5xa0μgxa0QS21和5xa0μgxa0CpG7909。在最后一次免疫接种后,从小鼠中获得脾脏或PBLs。对于在近交小鼠中的CASB7439免疫原性分析,脾脏或PBLs进行个别分析或合并。对于在CD1远交小鼠中的CASB7439免疫原性分析,每个脾脏个别进行加工。将PBLs或分离的脾细胞以10×10⁶细胞/ml的终浓度重悬浮于具有下述添加剂的RPMIxa01640培养基中:青霉素-链霉素(1X)、非必需氨基酸(1X)、2-巯基乙醇(55mM)、丙酮酸钠(100mM)、L-谷氨酰胺(200mM)。细胞已用来自CASB7439序列的肽进行刺激(在RPMIxa01640xa0+xa0添加剂xa0+xa05%热灭活的FBS中以1μg/ml/肽的终浓度使用)。根据常规程序,已执行用于CD4、CD8、IL-2、IL-5、IFNγ和TNFα的细胞内染色(ICS)。在刺激后,用布雷菲德菌素A处理细胞且固定。用CD4和CD8特异性单克隆抗体完成CD4和CD8的表面染色。随后,使细胞进行渗透化处理且用针对IL-2、IL-5、IFNγ和TNFα蛋白质产生的特异性单克隆抗体进行染色。细胞已通过流式细胞术使用BDxa0FACSCantoxa0II进行分析。数据以双重阳性IFNγ+和TNFα+xa0CD4或CD8xa0T细胞百分率表示。近交小鼠多品系T细胞免疫原性比较实验申请人在购自Charlesxa0River,Senneville,QC,加拿大的C57Bl/6、Balb/C、CB6f1(C57Bl/6与Balb/C小鼠杂交的第一代后代)和C3H近交小鼠中,比较了用AS01B或AS15配制的CASB7439蛋白质的免疫原性。用由AS01B或AS15配制的10xa0μg重组CASB7439蛋白质(LVL111)免疫接种5只小鼠/组。收集且合并脾脏(5只脾脏/组的一个库)。关于每个品系针对LVL111的CD4xa0T细胞应答(双重阳性IFNγ+和TNFα+)对于AS01B制剂呈现于图11/35中,并且对于AS15制剂呈现于图12/35中。在4个近交小鼠品系的任何中未观察到CD8xa0T细胞(双重阳性IFNγ+和TNFα+)应答。在用CASB7439+AS15免疫接种的近交小鼠中鉴定的CASB7439免疫显性肽呈现于图13/35中。免疫显性肽和SEQxa0IDxa0NO:13的相应区域是:●xa0C57Bl/6:xa0肽39(SEQxa0IDxa0NO:91)(SEQxa0IDxa0NO:13的aaxa0153xa0-xa0167)●xa0Balb/c:xa0肽24(SEQxa0IDxa0NO:13的aaxa093xa0-xa0107)●xa0CB6f1:xa0肽7-8(SEQxa0IDxa0NO:13的aaxa025xa0-xa043)和23-24(SEQxa0IDxa0NO:13的aaxa089xa0-xa0107)●xa0C3H:xa0肽9-11(SEQxa0IDxa0NO:13的aaxa033xa0-xa055)、16-19(SEQxa0IDxa0NO:13的aaxa061xa0-xa087)和41-43(SEQxa0IDxa0NO:13的aaxa0161-183)。LVL111、LVL168和LVL144的近交小鼠T细胞免疫原性研究LVL111、LVL168和LVL144的免疫原性在近交CB6f1小鼠中进行研究。在这个实验中,5只小鼠/组(Charlesxa0River,Senneville,QC,加拿大)已用由AS15配制的重组CASB7439蛋白质(LVL111、LVL168和LVL144)每2周免疫接种4次。每次免疫接种含有与如本文其他地方描述的25μlxa02X浓度佐剂混合的25μl重组CASB7439蛋白质。在用CASB7439肽矩阵再刺激脾细胞后,在个别近交CB6f1小鼠中通过细胞内染色和流式细胞术分析测量CD4和CD8xa0T细胞应答(双重阳性IFNγ和TNFα)。(数据未显示)。在CB6f1近交小鼠中用所有3种构建体的免疫接种触发针对相同免疫原性区域(SEQxa0IDxa0NO:13的aaxa025xa0-xa043和SEQxa0IDxa0NO:13的aaxa089xa0-xa0107)的CD4xa0T细胞免疫应答。在小鼠中CASB7439的免疫原性:在远交小鼠中的CASB7439xa0T细胞免疫原性CD1远交小鼠(Charlesxa0River,Senneville,QC,加拿大)用由AS01B或AS15配制的重组CASB7439蛋白质(LVL111)每2周免疫接种4次。每次免疫接种含有与如本文其他地方描述的25μlxa02X浓度佐剂混合的25μl重组CASB7439蛋白质。在用CASB7439肽矩阵再刺激脾细胞后,在个别CD1小鼠中通过细胞内染色和流式细胞术分析测量CD4和CD8xa0T细胞应答(双重阳性IFNγ和TNFα)。在用CASB7439+AS01B或CASB7439+AS15免疫接种的远交小鼠中鉴定的CASB7439xa0CD4-免疫原性肽的表分别呈现于图14/35的上和下中。在CD1远交小鼠中鉴定的CD4xa0T细胞免疫原性区域覆盖CASB7439的下述区域(就SEQxa0IDxa0NO:13的氨基酸位置而言表示):肽8-10(SEQxa0IDxa0NO:13的aaxa029xa0-xa051)、肽16-18(SEQxa0IDxa0NO:13的aaxa061xa0-xa083)和肽24-26(SEQxa0IDxa0NO:13的aaxa093xa0-xa0115)。在CD1远交小鼠中鉴定的CD8xa0T细胞免疫原性区域覆盖CASB7439(SEQxa0IDxa0NO:13)的下述区域:肽16-18(SEQxa0IDxa0NO:13的aaxa061xa0-xa083)、肽24-26(SEQxa0IDxa0NO:13的aaxa093xa0-xa0115)和肽32(SEQxa0IDxa0NO:13的aaxa0125xa0-xa0139)。(数据未显示)。LVL111、LVL168和LVL144的远交小鼠T细胞免疫原性研究在购自Charlesxa0River,Senneville,QC,加拿大的个别远交CD1小鼠中测试通过LVL111、LVL168和LVL144诱导的CASB7439+AS15介导的CD4和CD8-T细胞应答。5只小鼠/组接受由AS15配制的10xa0μgxa0CASB7439重组蛋白质(LVL111、LVL168或LVL144)组成的每2周的4次肌内免疫接种。(每次免疫接种含有与如本文其他地方描述的25μlxa02X浓度佐剂混合的25μl重组CASB7439蛋白质。对照组中的5只小鼠用盐水缓冲液进行免疫接种。在第4次免疫接种后2周,将小鼠处死。在用4个肽库(库1:肽8-9-10,库2:xa0肽16-17-18,库3:xa0肽24-25-26和库4:xa0肽30-31-32)的脾细胞再刺激后,通过细胞内染色和流式细胞术分析测量CD4和CD8xa0T细胞应答(双重阳性IFNγ和TNFα)。数据呈现于图15/35中。在用由AS15配制的3种CASB7439构建体各自免疫接种后激活SEQxa0IDxa0NO:13的相同CD4xa0T细胞免疫原性区域,具体地肽16-18(SEQxa0IDxa0NO:13的aaxa061xa0-xa083)和肽24-26(SEQxa0IDxa0NO:13的aaxa093xa0-xa0115)。LVL144和LVL168的HLAxa0A2.1/DR1转基因小鼠T细胞免疫原性研究在购自Pasteurxa0Institute,Paris,法国的合并HLAxa0A2.1/DR1转基因小鼠(3只小鼠的3个库)中测试通过2种构建体(LVL168或LVL144)诱导的CASB7439+AS15介导的CD4和CD8-T细胞应答。9只小鼠/组接受由AS15配制的6.25μgxa0LVL168或10μgxa0LVL144组成的每2周的4次肌内免疫接种。每次免疫接种含有与如本文其他地方描述的25μlxa02X浓度佐剂混合的25μl重组CASB7439蛋白质。对照组中的2只小鼠用单独的佐剂进行免疫接种。在第4次免疫接种后2周,将小鼠处死。在用覆盖整个CASB7439序列的7个肽库[库1:xa0肽1-7(SEQxa0IDxa0NOS:53-59),库2:xa0肽8-14(SEQxa0IDxa0NOS:60-66),库3:xa0肽15-21(SEQxa0IDxa0NOS:67-73),库4:xa0肽22-28(SEQxa0IDxa0NOS:74-80),库5:xa0肽29-35(SEQxa0IDxa0NOS81-87),库6:xa0肽36-42(SEQxa0IDxa0NOS:88-94)和库7:xa0肽43-46(SEQxa0IDxa0NOS:95-98)]的PBLs和脾细胞再刺激后,通过细胞内染色和流式细胞术分析测量CD4和CD8xa0T细胞应答(双重阳性IFNγ和TNFα)。此外,个别测试人HLAxa0DR免疫显性肽24(SEQxa0IDxa0NO:76)。图16-19中呈现的结果显示在用由AS15配制的2种CASB7439构建体各自免疫接种后激活相同CD4和CD8xa0T细胞免疫原性区域(肽22-28xa0+xa0肽24)。因此,肽24也是人HLAxa0A2.1免疫显性肽。这些结果在第二次实验中得到证实,其中相同CASB7439肽用于再刺激得自用由AS15配制的LVL168或LVL144免疫接种的5只个别小鼠/组的脾细胞。(数据未显示)。在小鼠中CASB7439的免疫原性:CASB7439介导的体液应答CB6f1小鼠研究在近交CB6f1小鼠(Charlesxa0River,Senneville,QC,加拿大)中评价针对以1/10人剂量使用的,由AS01B或AS15配制的10xa0μgxa0CASB7439(LVL111)的CASB7439介导的体液应答。19只小鼠/组接受每2周的4次肌内免疫接种。每次免疫接种含有与25μl佐剂(2X浓度)混合的25μl重组CASB7439蛋白质。小鼠仅在每次免疫接种前和第4次免疫接种后2周进行放血。在另一次实验中,在近交CB6f1小鼠(Charlesxa0River,Senneville,QC,加拿大)中评价针对LVL111、LVL168或LVL144的CASB7439介导的体液应答。50只小鼠/组接受由AS15配制的10xa0μgxa0CASB7439重组蛋白质(LVL111、LVL168或LVL144)或用单独的AS15作为对照组的每2周的4次肌内免疫接种。每次免疫接种含有与如本文其他地方描述的25μlxa02X浓度佐剂混合的25μl重组CASB7439蛋白质。小鼠在第4次免疫接种后2周进行放血。根据标准程序,抗CASB7439xa0IgG1和IgG2a血清抗体滴度已通过ELISA进行测定。简言之,CASB7439重组蛋白质在96孔板中在磷酸盐缓冲盐水(PBS)中进行包被。在用牛血清白蛋白1%的PBS-Tween(0.1%)溶液封闭后,来自免疫接种小鼠的血清在板中在37°C温育1小时。在板洗涤后,加入特异性山羊抗IgG1或IgG2a–HRP标记的小鼠抗体(Southernxa0Biotechxa0Associates,Birmingham,AL,USA)在37°C共1小时。在板洗涤后,加入TMB底物试剂(BDxa0Pharmingen,Mississauga,ON,加拿大)共15分钟。通过加入1M硫酸停止比色反应。OD已使用Spectramax分光光度计(Molecularxa0Device,Sunnyvale,CA,USA)在450nm进行测量。抗体滴度已用标准曲线进行测定,使用特异性总IgG、IgG1或IgG2a捕获抗体和内部CASB7439阳性小鼠血清。图20/35描述了在用由AS01B或AS15配制的CASB7439(LVL111)免疫接种的小鼠血清中的IgG1和IgG2a抗体滴度的时程分析。数据证实AS15触发更高的Th1(与AS01B比较,在4次免疫接种后约10倍高的IgG2a/IgG1比值(IgG2a是1型免疫应答的替代标记)。如图21/35中所示,由AS15配制的CASB7439蛋白质在近交CB6f1小鼠中触发极强的IgG1和IgG2a抗体应答,无论使用何种构建体(LVL111、LVL168或LVL144)。在小鼠中CASB7439的免疫原性:CASB7439介导的体液应答CD1小鼠研究在远交CD1小鼠(Charlesxa0River,Senneville,QC,加拿大)中评价在CASB7439免疫接种(LVL111、LVL168或LVL144)后CASB7439介导的体液应答。10只小鼠/组接受由AS15配制的10xa0μgxa0CASB7439重组蛋白质(LVL111、LVL168或LVL144)(或用单独的AS15作为对照组)的每2周的4次肌内免疫接种。每次免疫接种含有与如本文其他地方描述的25μlxa02X浓度佐剂混合的25μl重组CASB7439蛋白质。在第4次免疫接种后2周,小鼠进行放血,并且如已描述的,通过ELISA测定抗CASB7439总IgG血清抗体滴度。用各种CASB7439构建体(LVL111、LVL168或LVL144)免疫接种的CD1小鼠发生极强的CASB7439特异性体液免疫应答(图22/35)。数据指出与分别在CD1远交小鼠中的LVL168和LVL111比较,通过LVL144诱导8xa0–xa010倍高的抗CASB7439总IgG滴度。实施例11在小鼠中CASB7439xa0ASCI的抗瘤功效:鼠肿瘤模型开发开发了使用TC-1鼠肿瘤细胞或MC38鼠结肠直肠癌细胞的表达CASB7439蛋白质的鼠肿瘤模型,以研究在小鼠中CASB7439介导的体内肿瘤保护。TC-1肿瘤细胞由T.xa0xa0C.xa0xa0Wu(Johnsxa0Hopkinsxa0University,Baltimore,MD)友情提供。它们通过HPV16xa0E6和E7基因和激活的ras癌基因的相继转移由C57Bl/6小鼠的原发性肺细胞生成,如先前描述的(Lin等人(1996)Cancerxa0Res.xa0xa0Janxa01;56(1):21-6。MC38细胞,鼠结肠直肠腺癌细胞系,购自ATCC(Manassas,VA)。根据制造商的推荐,使用非脂质体转染试剂Fugene-6(Roche,Mississauga,ON,加拿大),用编码CASB7439的构建体稳定转染这些细胞。简言之,编码CASB7439蛋白质的整个序列且含有zeocine抗性基因的质粒(pcDNA3.1/Zeocine)已与Fugene-6混合,并且加入在无血清培养基中的TC-1或MC38肿瘤细胞上过夜。在转染后,允许细胞在培养基+xa010%热灭活的FBS中恢复24小时。随后将细胞收获且分布在96孔板(50xa0μl细胞悬液/孔)中用于有限稀释。在细胞种植后,将培养基用含有100μg/mlxa0zeocine(Invitrogen,Burlington,ON,加拿大)的培养基+xa010%热灭活的FBS替换。在选择后,收获每个克隆且允许在24孔板中生长且冷冻。使用CASB7439特异性TaqMan引物和探针,通过实时qPCR验证在TC1/CASB7439和MC38/CASB7439细胞中CASB7439xa0mRNA的表达。实时qPCR反应已使用TaqManxa07900仪(Appliedxa0Biosystem,Fosterxa0City,CA,USA)用TaqMan反应试剂盒执行。CASB7439蛋白质表达已通过蛋白质印迹和免疫荧光进行评价,其中使用特异性抗CASB7439单克隆抗体(40-12)。TC-1/CASB7439#14细胞群体不是完全克隆的,而是由至少2次不同亚克隆组成。因此,完成另一个有限稀释步骤,以便生成完全克隆的TC-1/CASB7439细胞群体:TC-1/CASB7439#14-2细胞。为了测定TC-1或MC38细胞用于小鼠中的肿瘤攻击的最佳剂量,将各种剂量的细胞(从1×10⁵到2xa0×xa010⁶细胞/小鼠)注射到CB6f1近交小鼠中。最佳剂量测定为对于TC-1/CASB7439#14和TC1/CASB7439#14-2攻击是2.5xa0×xa010⁵细胞/小鼠;并且对于用MC38/CASB7439#35细胞的攻击发现1xa0×xa010⁵细胞/小鼠是最佳的。在小鼠中的抗瘤功效:免疫接种和攻击实验设计一系列4个研究(1.1-1.4),以评估CASB7439介导的体内肿瘤保护。一般地,在这4个研究各自中,CB6f1小鼠组给予以2周间隔的4次肌内免疫接种,其应用以如本文其他地方描述的终浓度由AS01B或AS15配制的、各种剂量(0、1、10或30xa0μg)的选择用于研究的特异性重组CASB7439蛋白质,应用盐水缓冲液,应用单独的CASB7439蛋白质或用单独的佐剂。在第4次免疫接种后2周,通过皮下注射用250,000xa0TC-1/CASB7439xa0#14、100,000xa0MC38/CASB7439#35细胞或250,000xa0TC-1/CASB7439xa0#14-2肿瘤细胞攻击CB6f1小鼠。在攻击后,对于每只小鼠每周测量3次肿瘤大小。根据方案,具有大于200xa0mm²的肿瘤的小鼠被处死。随后绘制存活曲线。执行另外3个研究(2.1-2.4),以研究除0、1、10或30xa0μg重组CASB7439蛋白质外的剂量。研究2.4评价在雄性和雌性C57Bl/6小鼠中CASB7439的免疫原性和肿瘤保护之间的关联。平行评估CB6f1小鼠。研究1.1-2.4在下文更详细地描述。研究#1.1申请人研究了在CB6f1小鼠中针对TC1/CASB7439xa0#14攻击,通过用由AS01B或AS15配制的LVL111(1或10μg)的免疫接种赋予的肿瘤保护。10只小鼠/组用以如本文其他地方描述的终浓度由AS01B或AS15配制的重组CASB7439蛋白质(LVL111)以2周间隔肌内免疫接种4次。还测试了用盐水缓冲液或单独的CASB7439蛋白质免疫接种的2个对照组。在第4次免疫接种后2周,每只小鼠已用250,000xa0TC-1/CASB7439#14细胞进行皮下攻击。肿瘤生长跟踪42天,但未绘制存活曲线,因为在第42天太少的小鼠被处死。然而,对于每个组绘制了肿瘤生长曲线。图23/35的上和下图呈现了分别用AS01B和AS15制剂获得的肿瘤生长曲线。(注:AS15在该图中错标识为“AS015”。)曲线显示在接受由AS01B或AS15配制的CASB7439蛋白质的CB6f1小鼠中,TC1/CASB7439#14肿瘤生长减慢。研究#1.214只小鼠的组接受不同剂量的LVL111(1、10和30μg)或对照。小鼠用以如本文其他地方描述的终浓度由AS01B或AS15配制的不同剂量的LVL111以2周间隔肌内免疫接种4次。4个对照组也用仅AS01B、仅AS15、仅盐水缓冲液或仅30μgxa0LVL111进行免疫接种。在第4次免疫接种后2周,每只小鼠用250,000xa0TC-1/CASB7439#14细胞进行皮下攻击。在攻击后,对于每只小鼠每周测量3次肿瘤大小。根据方案,具有大于200xa0mm²的肿瘤的小鼠被处死。画出存活曲线。结果指示用由AS15配制的LVL111的免疫接种的小鼠针对TC1/CASB7439#14肿瘤攻击比用由AS01B配制的LVL111免疫接种的小鼠得到更佳保护。用由AS15配制的10μgxa0LVL111获得在CB6f1小鼠中的最佳结果。参见图24/35。研究#1.338只CB6f1小鼠/组用以如本文其他地方描述的终浓度由AS15配制的10xa0μgxa0LVL111、LVL168或LVL144以2周间隔肌内免疫接种4次。还测试了用单独的AS15免疫接种的对照组。在第4次免疫接种后2周,28只小鼠用250,000xa0TC-1/CASB7439#14细胞进行皮下攻击,并且其余10只小鼠已用100.000xa0MC38/CASB7439#35细胞进行皮下攻击。在攻击后,对于每只小鼠每周已测量3次肿瘤大小。根据方案,具有大于200xa0mm²的肿瘤的小鼠已被处死。结果指示用由AS15配制的LVL111、LVL168和LVL144针对TC1/CASB7439#14或MC38/CASB7439#35攻击都是保护性的。参见图25/35。研究#1.466只CB6f1小鼠/组用以如本文其他地方描述的终浓度由AS15配制的10xa0μgxa0LVL168或LVL144以2周间隔肌内免疫接种4次。还测试了用单独的AS15免疫接种的对照组。在第4次免疫接种后2周,22只小鼠/组用250,000xa0TC-1/CASB7439#14细胞(非克隆群体)、250,000xa0TC-1/CASB7439#14-2(克隆群体)细胞、或100,000xa0MC38/CASB7439#35细胞进行皮下攻击。在攻击后,对于每只小鼠每周测量3次肿瘤大小。根据方案,具有大于200xa0mm²的肿瘤的小鼠被处死。TC1/CASB7439#14-2攻击看起来比TC1/CASB7439#14攻击更有侵略性,如通过对照小鼠的更早死亡和在这个特定研究中可区分保护效应的不存在证明的。参见图26/35。后续试验用更有侵略性的TC-1/xa0CASB7439#14-2执行,如本文其他地方描述的。研究#2.115只CB6f1小鼠/组用以如本文其他地方描述的终浓度由AS15配制的各种等摩尔剂量的LVL168或LVL144肌内免疫接种4次。对于LVL168,使用下述抗原剂量:0.77、1.5、3.1和6.25xa0μg/小鼠。对于LVL144,使用下述抗原剂量:1.25、2.5、5和10xa0μg/小鼠。还测试了用单独的AS15免疫接种的对照组。在第4次免疫接种后2周,所有小鼠用250.000xa0TC-1/xa0CASB7439xa0#14-2(克隆群体)细胞进行皮下攻击。在攻击后,对于每只小鼠每周测量3次肿瘤大小。具有大于289xa0mm²(17mmxa0Xxa017mm)的肿瘤的小鼠被处死。画出关于每个组的存活曲线。参见图27/35,这描述了在TC1/xa0CASB7439xa0#14-2肿瘤攻击后,用由AS15配制的、等摩尔剂量的LVL168和LVL144获得的存活曲线。TF代表无肿瘤小鼠。与AS15对照组比较,等摩尔剂量的LVL144和LVL168的4个组看起来在CB6f1小鼠中类似地抑制肿瘤生长。研究#xa02.215只C57Bl/6小鼠/组用以如本文其他地方描述的终浓度由AS15配制的各种等摩尔剂量的LVL168或LVL144肌内免疫接种4次。对于LVL168,使用下述抗原剂量:0.77、1.5、3.1和6.25xa0μg/小鼠。对于LVL144,使用下述抗原剂量:1.25、2.5、5和10xa0μg/小鼠。作为对照组,小鼠还用单独的AS15或缓冲液进行免疫接种。在第4次免疫接种后2周,所有小鼠用250.000xa0TC-1/CASB7439xa0#14-2(克隆群体)细胞进行皮下攻击。在攻击后,对于每只小鼠每周测量3次肿瘤大小。具有大于289xa0mm²(17mmxa0Xxa017mm)的肿瘤的小鼠被处死。画出关于每个组的存活曲线。参见图28/35,这描述了在TC1/xa0CASB7439xa0#14-2肿瘤攻击后,用由AS15配制的、不同等摩尔剂量的LVL168和LVL144获得的存活曲线。TF代表无肿瘤小鼠。与用CB6f1小鼠进行的研究形成对比,在本研究中,未观察到在免疫接种组、AS15组或缓冲液组中的C57Bl/6小鼠存活之间的统计学显著差异。研究#xa02.315只CB6f1小鼠/组用以如本文其他地方描述的终浓度由AS15配制的各种等摩尔剂量的LVL168或LVL144肌内免疫接种4次。对于LVL168,使用下述剂量:0.04、0.19、0.77、1.5、3.1和6.25xa0μg/小鼠。对于LVL144,使用下述剂量:0.078、0.31、1.25、2.5、5和10xa0μg/小鼠。还测试了用单独的AS15免疫接种的对照组。首次用于实验的小鼠也用作第二个对照组。在第4次免疫接种后2周,所有小鼠用250,000xa0TC-1/xa0CASB7439xa0#14-2(克隆群体)细胞进行皮下攻击。在攻击后,对于每只小鼠每周测量3次肿瘤大小。具有大于289xa0mm²(17mmxa0Xxa017mm)的肿瘤的小鼠被处死。画出关于每个组的存活曲线。参见图29/35和30/35,这描述了在TC1/xa0CASB7439xa0#14-2肿瘤攻击后,用由AS15配制的、不同等摩尔剂量的LVL168和LVL144获得的存活曲线。TF代表无肿瘤小鼠。测试的2个最低等摩尔剂量看起来不显著抑制肿瘤生长。在4个最高剂量时,与LVL144加上AS15比较,在用LVL168加上AS15免疫接种的那些小鼠中观察到更多肿瘤保护。研究#xa02.4进一步研究如在研究#xa02.2中观察到的、针对TC1/CASB7439xa0#14-2肿瘤攻击用由AS15配制的CASB7439免疫接种的C57Bl/6小鼠中观察到的保护缺乏。15只CB6f1或C57Bl/6小鼠/组用以如本文其他地方描述的终浓度由AS15配制的1xa0μgxa0LVL168肌内免疫接种4次。分开研究用1xa0μgxa0LVL168xa0+xa0AS15免疫接种的雄性和雌性小鼠组。还测试了用单独的AS15免疫接种的分开对照雄性和雌性组。在第4次免疫接种后7天获得部分放血,并且通过ELISA测定抗CASB7439总IgG血清抗体滴度,如实施例10中描述的。在用LVL168xa0+xa0AS15免疫接种的雄性和雌性CB6f1小鼠中获得类似的CASB7439特异性CD4xa0T细胞应答(约1xa0×xa010^6xa0ng/ml总IgG);在C57Bl/6小鼠中未检测到抗体应答。参见图33/35。在第4次免疫接种后14天获得部分放血。在用覆盖整个CASB7439序列的肽库再刺激来自CB6f1或C57Bl/6小鼠(3只小鼠/组的5个库)的PBLs后,如实施例10中描述的,通过细胞内染色和流式细胞术分析测量CD4和CD8xa0T细胞应答(双重阳性IFNγ和TNFα)。此外,用来自C57Bl/6的PBLs测试肽39(SEQxa0IDxa0NO:91)。在用LVL168xa0+xa0AS15免疫接种的雄性和雌性CB6f1小鼠中获得类似的CASB7439特异性CD4xa0T细胞应答(约0.1xa0%频率);仅在雄性小鼠中获得CASB7439特异性CD8xa0T细胞应答(约0.05xa0%频率)。参见图34/35和35/35,上图。在用覆盖整个CASB7439序列的肽库或CASB7439肽39(SEQxa0IDxa0NO:91)(SEQxa0IDxa0NO:13的aaxa0153xa0-xa0167)的PBL再刺激后,在用1xa0μgxa0LVL168xa0+xa0AS15免疫接种的C57Bl/6小鼠中未检测到CASB7439特异性CD4或CD8xa0T细胞应答。参见图34/35和35/35(下图)。应当指出此处独立利用CASB7439肽39(SEQxa0IDxa0NO:91),因为它先前已鉴定为在用10xa0μgxa0LVL168xa0+xa0AS15免疫接种4次的C57Bl/6小鼠的脾细胞中的低CD4xa0T细胞免疫原性肽。参见实施例10中的图13。在第4次免疫接种后2周,所有小鼠用250,000xa0TC-1/xa0CASB7439#14-2细胞进行皮下攻击。在攻击后,对于每只小鼠每周测量3次肿瘤大小。具有大于289xa0mm²(17mmxa0Xxa017mm)的肿瘤的小鼠被处死。画出关于每个组的肿瘤生长和存活曲线。图31/35和32/35分别描绘了在TC1/CASB7439xa0#14-2肿瘤攻击后,用由AS15配制的、1xa0μgxa0LVL168或LVL144免疫接种的雄性或雌性CB6f1或C57Bl/6小鼠获得的肿瘤生长和存活曲线。结果指示与雌性CB6f1小鼠比较,CASB7439xa0+xa0AS15趋于在雄性CB6f1小鼠中获得更慢的肿瘤生长和更佳的存活,但对C57Bl/6小鼠中的肿瘤保护没有作用。在C57Bl/6小鼠中CASB7439肿瘤保护的缺乏对应于C57Bl/6小鼠中可检测的CASB7439特异性CD4和CD8xa0T细胞的不存在,以及可检测的CASB7439特异性抗体应答的不存在。这指示在使用的实验条件下,C57Bl/6小鼠不是研究通过CASB7439的免疫原性和肿瘤保护的理想小鼠模型。另一方面,在CB6f1小鼠中,所观察到的CASB7439肿瘤保护对应于显著的CASB7439特异性CD4xa0T细胞xa0[参见免疫原性肽7-8(SEQxa0IDxa0NO:13的aaxa025xa0-xa043)和23-24(SEQxa0IDxa0NO:13的aaxa089xa0-xa0107)图13/35,实施例10]和CASB7439特异性CD8xa0T细胞,以及CASB7439特异性抗体应答的存在。序列:SEQxa0IDxa0NO:1LVL055蛋白质ntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="576"/>SEQxa0IDxa0NO:2LVL055xa0DNAntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="576"/>SEQxa0IDxa0NO:3LVL111蛋白质ntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:4LVL111xa0DNAntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="576"/>SEQxa0IDxa0NO:5LVL137蛋白质ntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:6LVL137xa0DNAntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:7LVL141蛋白质ntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:8LVL141xa0DNAntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:9LVL144蛋白质ntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:10LVL144xa0DNAntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="576"/>SEQxa0IDxa0NO:11LVL168蛋白质ntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:12LVL168xa0DNAntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="576"/>SEQxa0IDxa0NO:13登记号AAB86993,HASH2蛋白质ntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:14HASH2xa0DNAntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="576"/>SEQxa0IDxa0NO:15LVL007蛋白质ntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="576"/>SEQxa0IDxa0NO:16LVL007xa0DNAntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:17LVL010蛋白质ntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:18LVL010xa0DNAntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:19LVL060蛋白质ntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="576"/>SEQxa0IDxa0NO:20LVL060xa0DNAntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="576"/>SEQxa0IDxa0NO:21Const-1蛋白质ntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:22Const-1xa0DNAntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:23LVL056蛋白质ntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:24LVL056xa0DNAntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:25LVL057蛋白质ntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:26LVL057xa0DNAntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:27LVL088蛋白质ntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:28LVL088xa0DNAntent="drawing" img-format="jpg" inline="no" orientation="portrait" wi="575"/>SEQxa0IDxa0NO:29LVL016蛋白质ntent="drawing" 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