CN115362260A - 用于高产重组微生物的系统和方法及其用途 - Google Patents
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Abstract
提供了用于在工程化微生物中高产地产生重组蛋白质的系统和方法。还提供了一种用于表达异源蛋白质的工程化宿主细胞,所述工程化宿主细胞可以包含至少三个不同表达盒,该至少三个不同表达盒被整合至该工程化宿主细胞的基因组中,其中;第一表达盒可以包含与编码异源蛋白质的异源基因序列可操作地连接的第一启动子;第二表达盒可以包含与编码异源蛋白质的异源基因序列可操作地连接的第二启动子;第三表达盒可以包含与辅助因子序列可操作地连接的第三启动子。
Description
相关申请的交叉引用
本申请要求2020年2月4日提交的美国临时专利申请序列号62/970,052的优先权。前述专利申请的全部内容通过引用并入本文。
序列表
本申请包含序列表,该序列表已通过EFS-Web以ASCII形式提交,并在此通过引用以其整体并入。所述ASCII副本创建于2021年2月3日,命名为49160-719.601_ST25.txt,并且大小为100,835字节。
背景技术
在工业蛋白质生产中,降低成本的目标是使蛋白质产物在重组生物中的表达最大化。甲基营养酵母诸如毕赤酵母属(Pichia sp.)是蛋白质的重要产生系统。尽管它们被广泛使用,但高产量的表达,特别是异源动物来源蛋白质的表达仍是挑战。该障碍在更大规模的发酵环境中尤为明显。虽然增加整合拷贝数可以导致蛋白质表达增加,但随着拷贝数的增加,产生的转录物数量似乎受到限制(Aw和Polizzi;Microb Cell Fact.2013;12:128)。
对于无动物蛋白质的需求(特别是在基于食品的成分中)不断增长。例如,近年来人们对注重健康的快餐食物的偏好趋势明显,蛋白质需求创下历史新高。除了越来越注重健康的消费者群体之外,对工业孵化场不人道方面的厌恶可能促使人们接受并最终偏爱无动物蛋白质替代品,而不是工厂化养殖的蛋类。因此,需要用于高产地工业化产生食物蛋白质(例如,备选的无动物蛋类蛋白质)的新方法。
发明内容
本发明解决了这种需要。该系统和方法在大规模生产中提供重组蛋白质的高滴度表达,并且特别适用于在微生物宿主中表达异源动物来源的蛋白质,诸如基于食物的蛋白质。
因此,本公开内容提供了用于表达异源蛋白质的工程化宿主细胞,所述工程化宿主细胞可以包含至少三个不同的表达盒(expression cassette),该至少三个不同表达盒被整合至该工程化宿主细胞的基因组中,其中;第一表达盒可以包含与编码异源蛋白质的异源基因序列可操作地连接的第一启动子;第二表达盒可以包含与编码异源蛋白质的异源基因序列可操作地连接的第二启动子;第三表达盒可以包含与辅助因子序列可操作地连接的第三启动子。在一些实施方案中,辅助因子编码序列与异源蛋白质编码序列的拷贝数比可以为至少1:10。
在一些方面,本文提供了用于表达异源蛋白质的工程化宿主细胞,其中所述工程化宿主细胞可以包含至少三个不同表达盒,该至少三个不同表达盒被整合至该工程化宿主细胞的基因组中。在一些情况下,第一表达盒可以包含与编码异源蛋白质的异源基因序列可操作地连接的第一启动子;第二表达盒可以包含与编码异源蛋白质的异源基因序列可操作地连接的第二启动子;第三表达盒可以包含与辅助因子序列可操作地连接的第三启动子;并且辅助因子编码序列与异源蛋白质编码序列的拷贝数比可以为至多1:2。
在一些方面,本文提供了在宿主细胞中产生重组异源蛋白质的方法。该方法可以包括:将多个质粒转化至宿主细胞中;其中该多个质粒可以包含至少三个质粒,该至少三个质粒中的每一个可以包含不同表达盒;其中不同表达盒中的每一个可以包含与异源基因序列可操作地连接的不同启动子。该方法包括将至少三个不同表达盒中的每一个的至少一个拷贝整合至宿主细胞中。在一些情况下,至少三个表达盒中的至少一个可以包含与辅助因子基因序列可操作地连接的启动子。在一些情况下,辅助因子基因与异源基因的拷贝数比可以为至少1:10。
在一些方面,本文提供了在宿主细胞中产生重组异源蛋白质的方法。在一些实施方案中,该方法可以包括:将多个质粒转化至宿主细胞中;其中该多个质粒可以包含至少三个质粒,该至少三个质粒中的每一个可以包含不同表达盒;其中不同表达盒中的每一个可以包含与异源基因序列可操作地连接的不同启动子;将至少三个不同表达盒中的每一个的至少一个拷贝整合至宿主细胞中;其中至少三个表达盒中的至少一个可以包含与辅助因子基因序列可操作地连接的启动子。在一些情况下,辅助因子基因与异源基因的拷贝数比可以为至多1:2。
在一些实施方案中,该方法可以进一步包括鉴定整合的表达盒。在一些实施方案中,鉴定可以包括对宿主细胞基因组进行测序。在一些实施方案中,鉴定可以包括确定是否存在与异源基因序列可操作地连接的启动子。在一些实施方案中,该方法进一步可以包括转化可以包含一个或多个表达盒的至少一个质粒,其中表达盒中的每一个包含与异源基因序列可操作地连接的启动子,其中该启动子被鉴定为存在于宿主细胞基因组中。在一些实施方案中,该方法可以进一步包括转化可以包含一个或多个表达盒的至少一个质粒,其中表达盒中的每一个包含与异源基因序列可操作地连接的启动子,其中该启动子被鉴定为不存在于宿主细胞基因组中。
在一些实施方案中,辅助因子编码序列与异源蛋白质编码序列的拷贝数比可以为至少1:10、1:9、1:8、1:7、1:6、1:5、1:4或1:3。在一些实施方案中,辅助因子编码序列与异源蛋白质编码序列的拷贝数比可以为至多1:9、1:8、1:7、1:6、1:5、1:4、1:3或1:2。
在一些实施方案中,至少一个启动子可以是诱导型启动子。在一些实施方案中,所有启动子均是诱导型启动子。在一些实施方案中,诱导型启动子可以是甲醇诱导型启动子。在一些实施方案中,每个甲醇诱导型启动子可以独立地选自AOX1、AOX2、DAK2、DAS2、FDH1、FGH1、FLD1和PEX11或其甲醇诱导型片段。
在一些实施方案中,至少一个启动子可以是组成型启动子。在一些实施方案中,组成型启动子可以独立地选自GAP和GCW14。
在一些实施方案中,宿主细胞可以包含第一表达盒的至少2个拷贝。在一些实施方案中,宿主细胞可以包含第二表达盒的至少2个拷贝。在一些实施方案中,宿主细胞可以包含第四表达盒的至少1个拷贝,该第四表达盒可以包含与异源基因序列可操作地连接的第四启动子。在一些实施方案中,第一盒和第二盒以相同的5’至3’方向被整合至基因组中。在一些实施方案中,第一盒和第二盒以相对的5’至3’方向被整合至基因组中。
在一些实施方案中,宿主细胞可以在1或2个表达盒中包含辅助因子编码序列的至少2个拷贝。在一些实施方案中,宿主细胞可以在1、2、3、4或5个表达盒中包含辅助因子编码序列的至少3、4或5个拷贝。在一些实施方案中,宿主细胞可以在1、2、3、4、5、6、7、8、9、10、11、12、13、14、15或16个表达盒中包含异源编码序列的至少3、4、5、6、7、8、9、10、11、12、13、14、15或16个拷贝。
在一些实施方案中,异源蛋白质可以是食物相关蛋白质。在一些实施方案中,食物相关蛋白质可以包括酶、营养蛋白质、食物成分或食物添加剂。在一些实施方案中,食物相关蛋白质可以是胃蛋白酶原蛋白质。在一些实施方案中,辅助因子编码序列与胃蛋白酶原编码序列的拷贝数比可以为1:2至1:5。
在一些实施方案中,食物相关蛋白质可以包括卵白蛋白质。在一些实施方案中,卵白蛋白质可以是卵类黏蛋白。在一些实施方案中,辅助因子编码序列与卵类黏蛋白编码序列的拷贝数比可以为1:3至1:6。在一些实施方案中,卵白蛋白质可以是卵清蛋白。在一些实施方案中,辅助因子编码序列与卵清蛋白编码序列的拷贝数比可以为1:3至1:8。
在一些实施方案中,在发酵条件下,工程化宿主细胞可以能够产生每升至少约5g的异源蛋白质。在一些实施方案中,在发酵条件下,工程化宿主细胞可以能够产生每升至少约10g的异源蛋白质。在一些实施方案中,在发酵条件下,工程化宿主细胞可以能够产生每升至少约20g的异源蛋白质。
在一些实施方案中,表达盒中的至少一个可以包含分泌信号。在一些实施方案中,表达盒中的至少一个可以包含终止序列。在一些实施方案中,辅助因子基因序列中的每一个编码独立地选自以下的蛋白质:HAC1、丝氨酸/苏氨酸蛋白激酶2(Kin2)、鲨烯合成酶(ERG9)、蛋白质二硫键异构酶1(PDI1)、SSA1、SSA4、SSB1、SSE1、BiP、ER膜蛋白复合物亚基1(EMC1)、YNL181W氧化还原酶、整合膜蛋白锌金属蛋白酶Ste24、14-3-3蛋白Bmh2和内质网氧化还原蛋白1(Ero1)。
在一些实施方案中,宿主细胞可以经工程化以有利于非同源整合而不是同源整合。在一些情况下,基于比同源整合更多的非同源整合对宿主细胞进行选择。在一些实施方案中,表达盒中的至少两个可以包含在不同整合位点处整合的异源基因序列。在一些实施方案中,宿主细胞可以是酵母细胞。在一些实施方案中,酵母细胞可以是毕赤酵母(Pichiapastoris)。在一些实施方案中,可以通过对宿主细胞基因组进行测序来测量拷贝数。
在一些方面,本文提供了在宿主细胞中产生重组异源蛋白质的方法,其中该方法可以包括:将第一媒介物转化至宿主细胞中;其中所述第一媒介物可以包含一个或多个第一表达盒;其中该第一表达盒中的每一个可以至少包含与编码异源蛋白质的异源基因序列可操作地连接的第一启动子;将一个或多个第一表达盒随机整合至宿主细胞中。在一些实施方案中,该方法包括鉴定一个或多个第一表达盒在宿主细胞中的整合;将第二媒介物转化至宿主细胞中;其中所述第二媒介物可以包含一个或多个第二表达盒;其中该第二表达盒中的每一个可以至少包含与异源基因序列可操作地连接的第二启动子;其中第二启动子可以与第一启动子不同。在一些实施方案中,该方法包括将一个或多个第二表达盒随机整合至宿主细胞中,并且其中宿主细胞可以是酵母或丝状真菌,并且其中在发酵条件下,工程化细胞可以能够产生每升至少5g的异源蛋白质。
在一些实施方案中,该方法可以包括转化除了第二媒介物之外的多个媒介物,其中该多个媒介物中的每一个包含一个或多个表达盒,该一个或多个表达盒各自可以包含驱动编码异源蛋白质的异源基因序列进行表达的一个或多个启动子。在一些实施方案中,一个或多个启动子包含第一启动子、第二启动子或其组合。在一些实施方案中,一个或多个启动子包含第一启动子、第二启动子、除了第一启动子或第二启动子之外的启动子或其组合。
在一些实施方案中,鉴定一个或多个第一表达盒的整合包括对获自宿主细胞的核酸进行测序。在一些实施方案中,鉴定一个或多个第一表达盒的整合可以包括鉴定是否存在抗性标志物;其中第一表达盒或第一质粒可以包含编码抗性标志物的序列。
在一些实施方案中,在发酵期间,异源蛋白质可以被分泌到培养基中,并且其中可以从发酵培养基中收获异源重组蛋白质。在一些实施方案中,第一表达盒和第二表达盒是线性分子,并且其中第一表达盒和第二表达盒在5’端有少于700bp与天然宿主细胞的基因组基因座同源。
在一些实施方案中,宿主细胞可以经工程化以有利于非同源整合而不是同源整合。在一些情况下,可以基于比同源整合更多的非同源整合对宿主细胞进行选择。在一些实施方案中,该方法进一步可以包括将辅助媒介物转化至宿主细胞中;其中所述辅助媒介物可以包含一个或多个辅助表达盒;其中辅助表达盒中的每一个可以包含与编码辅助因子蛋白质的基因序列可操作地连接的至少一个启动子。在一些实施方案中,一个或多个辅助表达盒中的启动子可以与第一启动子或第二启动子相同。在一些实施方案中,一个或多个辅助表达盒中的启动子可以与第一启动子或第二启动子不同。在一些实施方案中,该媒介物可以是质粒。在一些实施方案中,该媒介物可以是线性化质粒。
在一些方面,本文描述了用于通过发酵产生重组食物相关蛋白质的工程化细胞,其包含:至少一个第一盒,其包含与编码第一异源蛋白质的第一基因可操作地连接的第一启动子;和至少一个第二盒,其包含与编码第一异源蛋白质的第二基因可操作地连接的第二启动子;其中第一盒和第二盒在宿主细胞基因座的相同基因组基因座处或其附近被整合以产生工程化细胞;其中该基因组基因座不与第一启动子、第二启动子、第一基因或第二基因中的任何一个具有显著的序列同源性,并且其中宿主细胞是酵母或丝状真菌,并且其中在发酵条件下,工程化细胞能够产生每升至少5g的异源蛋白质。在一些实施方案中,第一启动子和第二启动子彼此不同。
在实施方案中,宿主细胞是甲基营养生物。在实施方案中,宿主细胞是法夫驹形氏酵母(Komagataella phaffii)或巴斯德驹形氏酵母(Komagataella pastoris)。在实施方案中,工程化细胞可以包含第一表达盒的2-5个拷贝。在其他实施方案中,工程化细胞可以包含第二表达盒的2-5个拷贝。在实施方案中,第一异源蛋白质包含动物来源的蛋白质序列。在一些实施方案中,动物来源的蛋白质序列编码卵白蛋白质。在实施方案中,卵白蛋白质选自卵黏蛋白(OVD)、卵清蛋白(OVA)、卵转铁蛋白和溶菌酶。在一个方面,第一异源蛋白质包含胃蛋白酶原。在实施方案中,第一盒和第二盒以相同的5’至3’方向被整合至工程化细胞的基因组中。在实施方案中,第一盒和第二盒以相对的5’至3’方向被整合至工程化细胞的基因组中。
在实施方案中,工程化细胞可以进一步包含整合至基因组中的至少一个第三盒。在实施方案中,第三盒包含与第三基因可操作地连接的第三启动子。在实施方案中,第三基因编码辅助因子。在实施方案中,第三基因编码第一异源蛋白质。在实施方案中,第三基因编码第二异源蛋白质。在实施方案中,第三盒在与第一盒和第二盒不同的整合位点处整合至工程化细胞的基因组中。在另一个方面,第三盒在与第一盒和第二盒相同的基因组基因座处整合。
在实施方案中,第一启动子是诱导型启动子。在实施方案中,第二启动子是诱导型启动子。在实施方案中,第一启动子是组成型启动子。在实施方案中,第二启动子是组成型启动子。在实施方案中,诱导型启动子是甲醇诱导型。在实施方案中,甲醇诱导型启动子选自AOX1、AOX2、FDH、FLD1、PEX11、DAS及其甲醇诱导型片段。在实施方案中,组成型启动子选自GAP、GCW14。在实施方案中,第一分泌信号与由第一基因编码的蛋白质可操作地连接。在实施方案中,第二分泌信号与由第二基因编码的蛋白质可操作地连接。
在实施方案中,本文提供了发酵高滴度异源重组蛋白质的方法,该方法包括在发酵培养物中提供工程化细胞;在发酵的2至12天内,使发酵培养物生长至50克细胞干重的最小密度以得到为每升至少2至10克蛋白质的蛋白质浓度;以及收获异源重组蛋白质,其中异源重组蛋白质由工程化细胞的第一基因和第二基因编码。在实施方案中,重组蛋白质的滴度在2-12天内达到每升每50g细胞干重至少4g蛋白质。在实施方案中,异源重组蛋白质在发酵期间被分泌到培养基中,并且从发酵培养基中收获异源重组蛋白质。
在实施方案中,异源重组蛋白质包含动物来源的蛋白质。在实施方案中,动物来源的蛋白质是食物相关蛋白质,诸如食物成分、食物组分或可用于食物加工和生产的酶。在实施方案中,动物来源的蛋白质包括卵白蛋白质,并且产生的卵白蛋白质表现出天然全卵或卵白的一种或多种功能特征。在实施方案中,产生的卵白蛋白质的至少一种功能特征等同于或优于天然全卵或卵白的功能特征。在实施方案中,一种或多种功能特征选自溶解度、透明度、质地、起泡、打发、渗出、胶凝、澄清、凝固、涂覆、结晶控制、干燥、食用包装膜、精加工、风味、强化、耐冻性、光泽、保湿、隔热、润湿、口感、pH稳定性、蛋白质富集、丰富度、保质期延长、结构、嫩化、质地、增稠、水结合、油结合、褐变、乳化、氮:碳比和/或抗微生物活性。
在一些实施方案中,使用本文的盒和方法表达的动物来源的蛋白质包括酶。在实施方案中,酶用于食物相关工艺,例如酶是胰蛋白酶、胰凝乳蛋白酶、溶菌酶、胃蛋白酶或其前体或前原体。
在实施方案中,本文提供了产生工程化细胞的方法,该方法包括:用包含第一盒和第二盒的核酸组合物转化宿主细胞,其中第一盒和第二盒在核酸组合物中未共价连接。在实施方案中,第一盒和第二盒是线性分子,其中第一盒和第二盒在5’端有少于700bp与天然宿主细胞的基因组基因座同源。在实施方案中,宿主细胞经工程化以有利于非同源整合而不是同源整合。
附图说明
本发明的新颖特征在所附权利要求中具体阐述。通过参考以下对其中利用本发明原理的说明性实施方案加以阐述的详细描述和附图,将获得对本发明的特征和优点的更好理解,在附图中:
图1显示了通过同源与异位整合产生的工程化OVD转化体。使用两个质粒(一个含有OVD的3个拷贝,一个含有OVD的6个拷贝,并且该质粒被设计用于将这些拷贝靶向特定基因座),用OVD的更多拷贝转化已经表达OVD的两个菌株。图1比较了通过同源表达与异位表达产生的工程化OVD菌株中的相对蛋白质表达。重复筛选来自菌株CF14和CF15的经PCR检查的转化体的5至6个单菌落。图1A和图1B显示了来自该实验的CF14和CF15重复筛选的总结。
具体实施方式
本文提供了用于使用调节控制而在工程化甲基营养酵母细胞(诸如毕赤酵母属,在本文中也称为且替代称为驹形氏酵母属(Komagataella sp.))中高产动物来源蛋白质(诸如动物来源的食物相关蛋白质)的生物系统和方法。本文所述的生物系统和方法采用异源基因序列的非同源整合,并且在一些情况下,使用这些整合位点来堆叠用于异源基因表达的表达盒。在一些实施方案中,整合的异源序列编码基于食物的蛋白质或食物相关蛋白质,诸如用作食物成分或在生产制造食品过程中使用的蛋白质。本文的系统和方法提供了高水平的基因表达,导致在发酵条件,特别是更大规模发酵条件下的高滴度蛋白质表达(大于5g/L)。
以下公开内容描述了通过组合以下项来驱动异源蛋白质在宿主细胞中高表达的系统和方法:(i)由一组不同的启动子驱动的多个表达盒稳定整合,每个整合位点携带一个或多个表达盒的多个拷贝;(ii)使用非同源重组方法,将多个表达盒共转化至宿主细胞(优选为毕赤酵母宿主细胞)的基因组中的单一位点中或单一位点附近;以及任选地,(iii)在宿主细胞基因组中整合表达盒后去除抗生素或其他选择标志物。表达盒与不同启动子的整合可以克服多拷贝整合的潜在问题,诸如盒的表达所需的同源转录因子的可能耗竭以及通过重组事件或其他宿主机制而缺失拷贝的可能性。
本文提供的系统和方法旨在促进宿主基因组中非同源位点的整合。与有利于同源重组的一些酵母不同,毕赤酵母属有利于异源序列的非同源整合。尽管具有这种有利的机制,但是毕赤酵母属的大多数表达系统却利用异源基因的同源整合。出乎意料地,在较小规模(诸如试管或摇瓶环境)中比较具有不同整合事件的工程化细胞显示出几乎等同的蛋白质产生水平,但是当在较大规模的发酵生产形式中进行比较时,在具有相应转基因的非同源整合事件的毕赤酵母细胞中发现了更高水平的期望异源蛋白质表达。
在一些实施方案中,在整合后,本文所述的工程化细胞不包含编码选择性标志物(例如营养缺陷型标志物或抗生素抗性基因)的序列,从而减少整合至宿主基因组中的外来异源DNA的量。另外,由于许多营养缺陷型标志物与宿主细胞中的内源基因高度同源,因此使用这样的标志物可能有利于经转化DNA的同源重组。
由于在大规模环境中的提高的高滴度表达能力以及在不使用抗生素或其他选择标志物的情况下的“更清洁”的生产系统,本文的系统和方法对于产生营养蛋白质(例如,用于食物成分和产品的植物或动物蛋白质、应用于食物和健康方面的蛋白质以及用于食物生产的动物来源的蛋白质)特别有用。
I.重组食物蛋白质的高滴度产生
本文的方法提供了从工程化宿主细胞以大体积生长形式(诸如在发酵罐中)以提高的高滴度产生重组蛋白质。
在一些实施方案中,本文的方法包括以大于约1、2、3、5、10、20、50、100、500、1000升的培养体积且在一段时间内(诸如1、2、3、4、5、6、7、8、9、10天或多于10天)在大规模生长环境中从工程化宿主细胞产生异源蛋白质。本文的系统和方法以大规模生长形式(例如,发酵罐)在发酵条件下提供至少4、5、6、7、8、9、10、11、12、13、14、15、16、17、18、19、20、21、22、23、24、25、26、27、28、29、30、32、34、36、38、40、42、44、46、48或50g蛋白质/升培养基的期望蛋白质的滴度。可以在一段时间内(诸如6小时、12小时、18小时、24小时、48小时或72小时)达到期望的异源蛋白质滴度。在一些情况下,可以在一段时间内(例如1、2、3、4、5、6、7、8、9、10天或多于10天)在发酵条件下达到期望的异源蛋白质滴度。在一些实施方案中,这样的滴度是从发酵培养物中分泌的期望蛋白质的量。在一些实施方案中,这样的滴度是发酵培养物中存在的总期望蛋白质(细胞内和细胞外)的量。在一些实施方案中,这样的滴度是来自发酵培养物的分泌蛋白质的量。
在一些实施方案中,本文的方法包括从工程化宿主细胞的异源重组蛋白质产生,其达到高达10克细胞每升培养基、30g/L、40g/L、50g/L、70g/L、100g/L或150g/L的培养密度。在一些实施方案中,本文的方法包括从工程化宿主细胞的异源重组蛋白质产生,其达到高达100g细胞干重/L、150g细胞干重/L或200g细胞干重/L的细胞密度。
发酵条件
本文的方法提供了发酵条件,该发酵条件提供了从工程化宿主细胞以大体积生长形式(诸如在发酵罐中)以提高的高滴度产生异源蛋白质。将酵母菌株甘油储备液解冻并以0.2%的接种比接种在含有BMDY培养基(BMDY培养基与BMGY培养基相似,其中甘油“G”已被葡萄糖/右旋糖“D”替代,毕赤酵母简易选择手册(Pichia Easy Select Manual),ThermoFisher)的具挡板摇瓶中。将摇瓶在30℃和250rpm下温育26小时。然后将摇瓶培养物以10%的比率转移到含有BSM(基础盐培养基)、葡萄糖和痕量金属(毕赤酵母发酵工艺指南(Pichia Fermentation Process Guidelines),Thermo Fisher)的生物反应器中。
生物反应器发酵分为三个阶段。在第1阶段期间,可以令培养物生长24小时直至所有葡萄糖均被消耗。在第2阶段期间,可以以葡萄糖限制速率向培养物补料葡萄糖12小时。在第3阶段期间,可以通过连续补料葡萄糖和诱导型启动子的激活剂(例如,用于AOX1启动子或PEX11启动子的甲醇)的共同补料96小时来诱导培养物。
在一个实施方案中,本发明提供了提高在发酵培养条件下从宿主细胞产生感兴趣重组蛋白质的体积产率的方法。在实施方案中,本发明提供了优化用于甲醇诱导型发酵系统(例如,在AOX1启动子的控制下)的细胞培养基,以用于使用补料分批发酵工艺在酵母宿主细胞中产生感兴趣重组蛋白质。在实施方案中,本发明提供了优化用于甲醇诱导型发酵系统(例如,在AOX1启动子的控制下)的细胞培养基,以用于使用连续发酵工艺在酵母宿主细胞中产生目的重组蛋白质。在一些情况下,宿主细胞是毕赤酵母细胞。
在实施方案中,该方法包括a)提供甘油补料酵母宿主细胞培养物,其包含如本文别处所述经工程化的毕赤酵母细胞,b)提供甲醇补料培养基,并且任选地提供渗透保护剂,以及c)在发酵条件下诱导酵母宿主细胞以使得重组蛋白质表达,其中感兴趣蛋白质的体积产率高于至少5g/L。如本文所用,术语“体积产率”意指每单位培养物体积的目标重组蛋白质的量(g/L)。在一些实施方案中,发酵条件的优化可用于将如本文所述经工程化的毕赤酵母菌株的体积产率提高20%、25%、30%、35%、40%、45%、50%、55%、60%、65%、70%、75%、80%、85%、90%、95%或大于100%。
在一些情况下,将如本文所述经工程化的宿主细胞的种子培养物接种到由合适培养基组成的起子培养物中。在一些情况下,培养基是BMGY培养基。在一些情况下,培养基是BMDY培养基。在一些情况下,起子培养基的体积为至多200ml、至多300ml或至多500ml。在一些情况下,起子培养物在24℃、25℃、26℃、27℃、28℃、29℃、30℃、31℃或32℃的温度下温育。在一些情况下,将起子培养物温育至多6小时、12小时、至多24小时、至多36小时或至多48小时。在一些情况下,在温育期间以100rpm、200rpm、300rpm、500rpm或600rpm的速度振荡起子培养物。在一些情况下,为培养宿主细胞提供发酵条件的生物反应器系统接种种子与初始发酵培养基的体积比至多3%、至多5%、至多10%、至多15%或至多20%。在一些情况下,初始发酵培养基是BMGY培养基。在一些情况下,初始发酵培养基是BSM培养基(基础盐培养基)。在一些情况下,初始发酵培养基含有葡萄糖和痕量金属。
在实施方案中,基于AOX1启动子的甲醇诱导型发酵系统可以使用甘油作为生物质生长的底物,然后使用甲醇补料来诱导异源蛋白质表达。在实施方案中,在发酵条件下培养毕赤酵母细胞涉及多阶段发酵工艺。在实施方案中,多阶段工艺是分批补料工艺。在实施方案中,初始阶段可以包括葡萄糖补料阶段,其中细胞在含葡萄糖培养基中培养以累积生物质。在一些情况下,初始阶段可以包括甘油补料阶段,其中细胞在含甘油培养基中培养以累积生物质。
在实施方案中,在下一阶段,可以以限速速率向细胞补料葡萄糖以准备诱导阶段。在实施方案中,葡萄糖的限速补料速率的范围可以为每小时至多0.005g/l、至多0.05g/l或至多0.5g/l的特定生长速率。在一些情况下,可以补料葡萄糖至多8小时、至多10小时、至多14小时、至多16小时、至多20小时、或至多24小时、至多30小时、至多36小时、至多40小时或至多48小时。在一些情况下,宿主细胞可以不在甲醇诱导之前补料甘油。
在一些情况下,甲醇诱导阶段之前可以是饥饿阶段。在一些情况下,诱导前的饥饿阶段可以持续30分钟、至多60分钟、至多90分钟、至多120分钟、至多150分钟、至多180分钟、至多4小时、至多6小时、至多8小时、至多9小时、至多10小时、至多15小时、至多18小时、至多20小时。
在一些情况下,可以优化甲醇补料速率以提高宿主细胞中重组蛋白质的产生。在一些情况下,甲醇补料方案(例如,保持固定的甲醇浓度(Damasceno等人,2004),通过甲醇补料速率控制溶解氧浓度(Charoenrat等人,2005),碳限制补料策略(Zhang等人,2000)以及混合碳源补料(Ramon等人,2007))可用于提高从工程化宿主细胞产生异源蛋白质的速率。在一些情况下,甲醇可以以恒定速率连续补料。在一些情况下,甲醇补料速率可以为至多0.5g/L/h,至多0.7g/L/h、0.8g/L/h、0.9g/L/h、1.1g/L/h、1.3g/L/h、1.5g/L/h、1.6g/L/h、1.8g/L/h、1.9g/L/h、2.1g/L/h、2.4g/L/h、2.6g/L/h、2.7g/L/h、2.9g/L/h、3.1g/L/h、3.3g/L/h、3.5g/L/h、3.7g/L/h、3.9g/L/h、4.5g/L/h或5.0g/L/h。在一些情况下,甲醇可以以指数速率补料。在一些情况下,甲醇可以作为定期推注添加。在一些情况下,对宿主细胞进行葡萄糖与甲醇共同补料。在一些情况下,葡萄糖补料速率可以为至多0.5g/L/h、至多0.7g/L/h、0.8g/L/h、0.9g/L/h、1.1g/L/h、1.3g/L/h、1.5g/L/h、1.6g/L/h、1.8g/L/h、1.9g/L/h、2.1g/L/h、2.4g/L/h、2.6g/L/h、2.7g/L/h、2.9g/L/h、3.1g/L/h、3.3g/L/h、3.5g/L/h、3.7g/L/h、3.9g/L/h、4.5g/L/h或5.0g/L/h。
在一些情况下,甲醇诱导阶段的长度可以为至多1天、至多2天、至多3天、至多4天、至多5天、至多6天、至多7天、至多8天、至多9天或至多10天。在一些情况下,甲醇诱导阶段的长度可以为至少1天、至少2天、至少3天、至少4天、至少5天、至少6天、至少7天、至少8天、至少9天或至少10天。
可以设计合适的培养基以提供纯碳源。在一些情况下,培养基可以任选地提供生物素、盐、痕量元素和水。在一些情况下,宿主细胞的碳源可以选自葡萄糖、岩藻糖、甘露糖、山梨糖或甘油、山梨糖醇。在一些情况下,培养基可以是BSGY、BMGY、BMMY、MD或YPD培养基。在一些情况下,培养基组成可以通过影响细胞生长和生存力或改变细胞外蛋白酶的分泌来影响宿主细胞中的异源蛋白质表达。在一些情况下,可以将山梨糖醇或甜菜碱添加到培养基中以增加异源重组蛋白质的产生。在实施方案中,向分批补料培养系统中添加有机氮源(例如,酵母提取物和蛋白质胨的混合物)可用于增加宿主酵母细胞中的异源蛋白质产生。
宿主细胞的细胞壁完整性可以影响异源蛋白质的产量。在实施方案中,可以设计利用优化的培养基和发酵条件的改进培养条件以改进工程化毕赤酵母菌株的细胞壁完整性。例如,在实施方案中,发酵培养基可以包含补充有不可发酵糖或不可发酵糖醇作为渗透保护剂的基础培养基。在特定实施方案中,渗透保护剂可以选自麦芽糖、山梨糖、核糖、麦芽糖醇、肌醇、蜜二糖和奎尼酸。在一些情况下,甘油、阿糖醇、甘氨酸甜菜碱、山梨糖醇或海藻糖可用于在渗透胁迫条件下调节细胞渗透压。可以将渗透保护剂添加到任何合适的基础培养基中。在特定实施方案中,除了其他培养基补充剂(包括但不限于包含氨基酸、维生素、痕量金属或基础盐的混合物)之外,还可以添加渗透保护剂。在实施方案中,可以维持包含渗透保护剂通过甘油补料阶段、甲醇诱导阶段或这两个阶段。
在实施方案中,渗透保护剂以约15g/L、约25g/L、约35g/L、约50g/L、约75g/L或约100g/L的浓度存在。在实施方案中,分批培养基中渗透保护剂的存在增加并维持分批培养基的渗透压浓度为大于约50mOsm/kg、大于约100mOsm/kg、大于约200mOsm/kg、大于约500mOsm/kg、大于约700mOsm/kg、大于1000mOsm/kg或大于约1500mOsm/kg。在实施方案中,使增加的渗透压维持约24小时至约48小时、约80小时至约110小时或直到甲醇诱导阶段完成(例如,约24至约150小时)。在一些情况下,维持增加的渗透压度过甲醇补料阶段。
在一些情况下,可以优化培养参数(例如pH、温度或溶解氧)以提高宿主细胞中重组蛋白质的产生。在一些情况下,培养温度条件可以为至少24℃、24.1℃、24.2℃、24.5℃、24.8℃、26.0℃、26.3℃、26.5℃、26.8℃、27.0℃、27.2℃、27.5℃、27.8℃、29.0℃、29.3℃、29.5℃、29.8℃、30.0℃、30.3℃、30.5℃、30.7℃、31℃、31.3℃、31.5℃、31.7℃、31.9℃、32.3℃、32.6℃、32.8℃、33.0℃、33.1℃、33.5℃、33.6℃或34.0℃。在一些情况下,发酵培养条件的pH可以为至多5、5.2、5.4、5.6、5.8、6.0、6.2、至多6.4、至多6.6、至多6.7、至多6.8、至多6.9、至多7.0、至多7.1、至多7.3、至多7.5、至多7.8、至多7.9或至多8.0。在一些情况下,发酵培养条件的pH可以为至少4、4.4、4.6、4.8、5、5.2、5.4、5.6、5.8、6.0、6.2、6.4、6.6、6.7、6.8、6.9、7.0、7.1、7.3、7.5、7.8或7.9。在一些情况下,溶解氧水平可以保持在至多15%、至多17%、至多20%、至多22%、至多25%、至多27%、至多30%、至多32%或至多35%的饱和度。
食物蛋白质
在一些实施方案中,本文提供的方法可用于在大规模发酵环境中产生动物来源的食物相关蛋白质。在一些情况下,动物来源的蛋白质是酶,诸如用于食物和/或饮料成分和产品的制造、加工和/或产生。动物来源的酶的一些示例包括胰蛋白酶、胰凝乳蛋白酶、胃蛋白酶以及这样的酶的前体和前原体;例如,胃蛋白酶原是胃蛋白酶的前体/前原体。在一些情况下,动物蛋白质是营养蛋白质,诸如保持或结合维生素或矿物质的蛋白质(例如,铁结合蛋白或血红素结合蛋白)或提供蛋白质源和/或特定氨基酸的蛋白质。
在一些实施方案中,本文提供的方法可用于在大规模发酵环境中产生食物蛋白质。在一些情况下,食物蛋白质可以是动物蛋白质。在一些实施方案中,动物蛋白质可以是卵相关蛋白质。这样的卵白蛋白质的示例性示例可以是卵清蛋白(OVA)、卵类黏蛋白(OVD)、卵转铁蛋白和溶菌酶蛋白质。卵相关蛋白质的其他示例包括卵黏蛋白、卵球蛋白G2、卵球蛋白G3及其任何组合。卵相关蛋白质的其他示例包括卵抑制剂、卵糖蛋白、黄素蛋白、卵巨球蛋白、卵固蛋白(ovostatin)、半胱氨酸蛋白酶抑制剂、抗生物素蛋白、卵清蛋白相关蛋白X、卵清蛋白相关蛋白Y及其任何组合。
在一些情况下,使用本文提供的系统和方法产生的蛋白质是经翻译后修饰的。这样的修饰包括糖基化和磷酸化。在一些情况下,产生的蛋白质的翻译后修饰与天然产生的蛋白质相同或基本相似。在一些情况下,与蛋白质的天然来源相比,产生的蛋白质的翻译后修饰发生改变。
在一些实施方案中,使用本文提供的系统和方法收获的重组蛋白质可以提供天然蛋白质的至少一种或多种功能特征。例如,重组卵白卵清蛋白可以表现出天然卵白蛋白质的至少一种或多种功能特征,其选自胶凝、起泡、打发、疏松、结合、弹性、充气、乳脂状和对组合物的黏合性。在其他情况下,一种或多种功能特征可以选自溶解度、透明度、质地、起泡、打发、渗出、胶凝、氮:碳比、水结合、油结合、褐变、乳化、澄清、凝固、涂覆、结晶控制、干燥、可食用包装膜、精加工、风味、强化、耐冻性、光泽、保湿、隔热、润湿、口感、pH稳定性、蛋白质富集、丰富度、保质期延长、结构、嫩化、质地、增稠或抗微生物活性。在一些情况下,使用本文提供的系统和方法收获的重组动物蛋白质可以提供与天然蛋白质的相同特征基本相同或比其更好的至少一种或多种功能特征。在一个示例中,用本文的系统和方法生产的重组卵清蛋白的特征可以与天然蛋白质提供的相同特征基本上相同或比其更好。在一些实施方案中,本文提供了用作卵白替代物的重组蛋白质组合物。
使用本文的系统和方法产生的蛋白质可以用于食物成分和食物产品。例如,使用本文所述的方法产生的重组卵清蛋白可以为食物成分和食物产品提供一种或多种功能特征。在一些情况下,使用本文的方法产生的重组动物蛋白质可以为食物成分或食物产品提供营养特征,诸如蛋白质含量、蛋白质强化和氨基酸含量。例如,由使用本文的方法产生的重组卵清蛋白提供的营养特征可以与卵、卵白或天然卵清蛋白相当或基本相似。在其他情况下,由使用本文的方法产生的重组卵清蛋白提供的营养特征可以优于由天然卵或天然卵白提供的营养特征。
食物组合物可以包括0.1%至50%的量(基于重量/重量(w/w)或重量/体积(w/v))的重组食物蛋白质,例如重组卵黏蛋白。使用本文的系统和方法产生的重组蛋白质可以以或至少以0.1%、0.2%、0.25%、0.3%、0.4%、0.5%、0.6%、0.7%、0.8%、0.9%、1%、2%、3%、4%、5%、6%、7%、8%、9%、10%、11%、12%、13%、14%、15%、16%、17%、18%、19%、20%、25%、30%、35%、40%、45%或50%(基于重量/重量(w/w)或重量/体积(w/v))存在于食物组合物中。附加地或备选地,使用本文的系统和方法产生的重组蛋白质可存在于这样的食物组合物中的浓度为至多70%、60%、50%、40%、30%、20%、15%、10%、5%、4%、3%、2%或1%(基于w/w或w/v)。在一些实施方案中,食物成分或食物产品中的重组蛋白质可以在0.1%-50%、1%-30%、0.1%-20%、1%-10%、0.1%-5%、1%-5%、0.1%-2%、1%-2%或0.1-1%w/w的浓度范围内。
II.用于高产量食物蛋白质产生的工程化细胞的生成
本文提供的系统和方法被设计用于通过将包含在一个或多个表达盒中的用于重组蛋白质表达的异源序列引入宿主细胞来工程化宿主细胞。
一个或多个表达盒可以被整合至宿主细胞中。宿主细胞可以包含第一表达盒。第一表达盒可以具有与编码第一异源蛋白质的第一基因可操作地连接的第一启动子。宿主细胞可以包含第二表达盒。在一些情况下,第一表达盒和第二表达盒编码相同的蛋白质。例如,第一表达盒和第二表达盒可以驱动重组卵类黏蛋白的表达。在一些情况下,在第一表达盒和第二表达盒中表达的重组异源蛋白质由相同的基因序列编码。在一些情况下,在第一表达盒和第二表达盒中表达的重组蛋白质可以由不同的基因序列编码。例如,表达盒可以包含编码相同蛋白质的一种或多种基因序列,诸如,这些基因序列中的一种可以经密码子优化。在一些情况下,编码在第一表达盒和第二表达盒中表达的重组蛋白质的基因序列可以具有至少80%、至少85%、至少90%、至少95%或至少99%的序列相似性。
在一些情况下,在第一表达盒中表达的重组蛋白质可以是与第二表达盒中的重组蛋白质同源的蛋白质。例如,第一表达盒中的重组蛋白质可以来自第一物种的卵相关蛋白质,并且第二表达盒中的重组蛋白质可以是来自相关物种的同源卵相关蛋白质。例如,第一表达盒中的重组蛋白质可以是由家鸡(Gallus gallus domesticus)编码的卵类黏蛋白,并且第二表达盒中的重组蛋白质可以是由绿头鸭(Anas platyrhynchos)物种编码的卵类黏蛋白。在一些情况下,编码在第一表达盒和第二表达盒中表达的重组蛋白质的同源基因序列可以具有至少80%、至少85%、至少90%、至少95%或至少99%的序列相似性。
在一些情况下,第一表达盒和第二表达盒可以编码不同的蛋白质。例如,第一表达盒和第二表达盒可以分别驱动卵类黏蛋白和卵清蛋白的表达。在一些情况下,任选地,第三表达盒可以与第三基因可操作地连接。在一些情况下,第三基因可以编码第一重组蛋白质。在一些情况下,第三基因可以编码第二重组蛋白质。在一些情况下,任选地,第三基因编码第三重组蛋白质。在一些情况下,第三重组异源蛋白质可以编码辅助蛋白质,即辅助第一异源蛋白质或第二异源蛋白质表达的蛋白质。
在一些情况下,任选地,第四表达盒可以与第四基因可操作地连接。在一些情况下,第四基因可以编码第一重组蛋白质。在一些情况下,第四基因可以编码第二重组蛋白质。在一些情况下,任选地,第四基因编码第三重组蛋白质。在一些情况下,任选地,第五表达盒可以与第五基因可操作地连接。在一些情况下,第五基因可以编码第一重组蛋白质。在一些情况下,第五基因可以编码第二重组蛋白质。在一些情况下,任选地,第五基因编码第三重组蛋白质。在一些情况下,任选地,第五基因编码第四重组蛋白质。在一些情况下,任选地,第五基因编码第五重组蛋白质。
在一些情况下,由第一表达盒或第二表达盒编码的重组异源蛋白质可以是动物来源的蛋白质。在一些情况下,动物来源的蛋白质是食物相关蛋白质。在一些情况下,动物来源的蛋白质可以是卵相关蛋白质。卵相关蛋白质或卵白蛋白质的示例包括例如,卵类黏蛋白、卵清蛋白、溶菌酶、卵转铁蛋白、卵黏蛋白、卵球蛋白G2、卵球蛋白G3及其任何组合。在一些情况下,信号肽的序列同一性可以是与表4中列出的SEQ ID NO:13-16具有至少80%、90%、95%、96%、97%、98%、99%或99.5%序列同一性的序列。用于生产的附加的卵相关蛋白质包括卵抑制剂、卵糖蛋白、黄素蛋白、卵巨球蛋白、卵固蛋白、半胱氨酸蛋白酶抑制剂、抗生物素蛋白、卵清蛋白相关蛋白X、卵清蛋白相关蛋白Y及其任何组合。
在一些情况下,由第一表达盒或第二表达盒编码的重组异源蛋白质可以是基于植物的食物蛋白质。一些情况下,一种或多种基于植物的蛋白质可以包括但不限于:豌豆蛋白质分离物和/或浓缩物;鹰嘴豆(鸡心豆)蛋白质分离物和/或浓缩物;蚕豆蛋白质分离物和/或浓缩物;大豆蛋白质分离物和/或浓缩物;稻蛋白质分离物和/或浓缩物;绿豆蛋白质分离物和/或浓缩物;土豆蛋白质分离物和/或浓缩物;大麻蛋白质分离物和/或浓缩物;或其任何组合。基于植物的蛋白质可以包括,例如,大豆蛋白质(例如,所有形式,包括浓缩物和分离物)、豌豆蛋白质(例如,所有形式,包括浓缩物和分离物)、菜籽蛋白质(例如,所有形式,包括浓缩物和分离物)、其市售为小麦的其他植物蛋白质和分级的小麦蛋白质、玉米及其级分(包括玉米醇溶蛋白)、稻、燕麦、土豆、花生、绿豌豆粉、绿豆粉以及衍生自豆类、扁豆和干豆的任何蛋白质。在特定实施方案中,豌豆蛋白质可以衍生自黄豌豆,诸如加拿大黄豌豆。
表达盒整合拷贝数
在一些实施方案中,用于整合至宿主细胞中的媒介物或质粒可以包含第一表达盒的一个或多个拷贝。在一些实施方案中,用于整合至宿主细胞中的质粒可以包含第一表达盒的一个或多个拷贝和第二表达盒的一个或多个拷贝。在一些情况下,工程化宿主细胞可以整合一个或多个质粒,每个质粒包含第一表达盒的至少1个、至少2个、至少3个、至少4个、至少5个、至少6个、至少7个、至少8个、至少9个、至少10个、至少11个、至少12个、至少13个、至少14个、至少15个、至少16个、至少17个、至少18个、至少19个或至少20个拷贝。在一些情况下,工程化宿主细胞可以整合一个或多个质粒,每个质粒包含第一表达盒的至多1个、至多2个、至多3个、至多4个、至多5个、至多6个、至多7个、至多8个、至多9个、至多10个、至多11个、至多12个、至多13个、至多14个、至多15个、至多16个、至多17个、至多18个、至多19个或至多20个拷贝。在一些情况下,工程化宿主细胞可以整合一个或多个质粒,每个质粒包含第二表达盒的至少1个、至少2个、至少3个、至少4个、至少5个、至少6个、至少7个、至少8个、至少9个、至少10个、至少11个、至少12个、至少13个、至少14个、至少15个、至少16个、至少17个、至少18个、至少19个或至少20个拷贝。在一些情况下,工程化宿主细胞可以整合一个或多个质粒,每个质粒包含第二表达盒的至多1个、至多2个、至多3个、至多4个、至多5个、至多6个、至多7个、至多8个、至多9个、至多10个、至多11个、至多12个、至多13个、至多14个、至多15个、至多16个、至多17个、至多18个、至多19个或至多20个拷贝。
在一些情况下,工程化宿主细胞可以整合第一表达盒的一个或多个拷贝、第二表达盒的一个或多个拷贝以及任选的第三表达盒的一个或多个拷贝。在一些情况下,宿主细胞整合可以包括第一表达盒的至少1个、至少2个、至少3个、至少4个、至少5个、至少6个、至少7个、至少8个、至少9个、至少10个、至少11个、至少12个、至少13个、至少14个、至少15个、至少16个、至少17个、至少18个、至少19个或至少20个拷贝以及第二表达盒的至少1个、至少2个、至少3个、至少4个、至少5个、至少6个、至少7个、至少8个、至少9个、至少10个、至少11个、至少12个、至少13个、至少14个、至少15个、至少16个、至少17个、至少18个、至少19个或至少20个拷贝。附加地,宿主细胞可以包括第三表达盒的至多1个、至多2个、至多3个、至多4个、至多5个、至多6个、至多7个、至多8个、至多9个、至多10个、至多11个、至多12个、至多13个、至多14个、至多15个、至多16个、至多17个、至多18个、至多19个或至多20个拷贝。在一些情况下,整合可以包括第一表达盒的至少1个、至少2个、至少3个、至少4个、至少5个、至少6个、至少7个、至少8个、至少9个、至少10个、至少11个、至少12个、至少13个、至少14个、至少15个、至少16个、至少17个、至少18个、至少19个或至少20个拷贝以及第二表达盒的至多1个、至多2个、至多3个、至多4个、至多5个、至多6个、至多7个、至多8个、至多9个、至多10个、至多11个、至多12个、至多13个、至多14个、至多15个、至多16个、至多17个、至多18个、至多19个或至多20个拷贝。附加地,宿主细胞可以包括第三表达盒的至多1个、至多2个、至多3个、至多4个、至多5个、至多6个、至多7个、至多8个、至多9个、至多10个、至多11个、至多12个、至多13个、至多14个、至多15个、至多16个、至多17个、至多18个、至多19个或至多20个拷贝。
在一些情况下,工程化宿主细胞可以整合编码第一重组蛋白质的基因序列的一个或多个拷贝、编码第二重组蛋白质的基因序列的一个或多个拷贝以及任选的编码第三重组蛋白质的转基因的一个或多个拷贝。在一些情况下,宿主细胞整合可以包括编码第一重组蛋白质的转基因的至少1个、至少2个、至少3个、至少4个、至少5个、至少6个、至少7个、至少8个、至少9个、至少10个、至少11个、至少12个、至少13个、至少14个、至少15个、至少16个、至少17个、至少18个、至少19个或至少20个拷贝以及编码第二重组蛋白质的转基因的至少1个、至少2个、至少3个、至少4个、至少5个、至少6个、至少7个、至少8个、至少9个、至少10个、至少11个、至少12个、至少13个、至少14个、至少15个、至少16个、至少17个、至少18个、至少19个或至少20个拷贝。附加地,宿主细胞可以包括编码第三重组蛋白质的转基因的至多1个、至多2个、至多3个、至多4个、至多5个、至多6个、至多7个、至多8个、至多9个、至多10个、至多11个至多12个、至多13个、至多14个、至多15个、至多16个、至多17个、至多18个、至多19个或至多20个拷贝。附加地,宿主细胞可以包括编码第四重组蛋白质的转基因的至多1个、至多2个、至多3个、至多4个、至多5个、至多6个、至多7个、至多8个、至多9个、至多10个、至多11个、至多12个、至多13个、至多14个、至多15个、至多16个、至多17个、至多18个、至多19个或至多20个拷贝。附加地,宿主细胞可以包括编码第五重组蛋白质的转基因的至多1个、至多2个、至多3个、至多4个、至多5个、至多6个、至多7个、至多8个、至多9个、至多10个、至多11个、至多12个、至多13个、至多14个、至多15个、至多16个、至多17个、至多18个、至多19个或至多20个拷贝。
工程化宿主细胞可以包含编码异源蛋白质(诸如重组产生的动物蛋白质)的异源基因的多于一个拷贝。可以使用标准技术(诸如定量PCR或测序)来确定整合至宿主细胞基因组中的异源基因的拷贝数。诸如宿主细胞基因组测序的技术可以在拷贝数计算中提供最小变异量,因此可以提供更可靠的拷贝数计数。在一些情况下,工程化宿主细胞包含每个细胞2至20个异源基因拷贝。在一些情况下,工程化宿主细胞包含每个细胞至少2个异源基因拷贝。在一些情况下,工程化宿主细胞包含每个细胞至多20个异源基因拷贝。在一些情况下,工程化宿主细胞包含每个细胞2至4、2至5、2至6、2至8、2至10、2至12、2至14、2至16、2至18、2至20、4至5、4至6、4至8、4至10、4至12、4至14、4至16、4至18、4至20、5至6、5至8、5至10、5至12、5至14、5至16、5至18、5至20、6至8、6至10、6至12、6至14、6至16、6至18、6至20、8至10、8至12、8至14、8至16、8至18、8至20、10至12、10至14、10至16、10至18、10至20、12至14、12至16、12至18、12至20、14至16、14至18、14至20、16至18、16至20或18至20个异源基因拷贝。在一些情况下,工程化宿主细胞包含每个细胞约2、4、5、6、8、10、12、14、16、18或20个异源基因拷贝。在一些情况下,工程化宿主细胞包含每个细胞至少2、4、5、6、8、10、12、14、16或18个异源基因拷贝。在一些情况下,工程化宿主细胞包含每个细胞至多4、5、6、8、10、12、14、16、18或20个异源基因拷贝。
工程化宿主细胞可以包含一个或多个拷贝的编码辅助因子蛋白质的辅助因子基因。可以使用标准技术(例如定量PCR或测序)来确定整合至宿主细胞基因组中的辅助因子基因的拷贝数。诸如宿主细胞基因组测序的技术可以在拷贝数计算中提供最小变异量,因此可以提供更可靠的拷贝数计数。在一些情况下,工程化宿主细胞包含每个细胞1至8个辅助因子基因拷贝。在一些情况下,工程化宿主细胞包含每个细胞至少1个辅助因子基因拷贝。在一些情况下,工程化宿主细胞包含每个细胞至多8个辅助因子基因拷贝。在一些情况下,工程化宿主细胞包含每个细胞1至2、1至3、1至4、1至5、1至6、1至7、1至8、2至3、2至4、2至5、2至6、2至7、2至8、3至4、3至5、3至6、3至7、3至8、4至5、4至6、4至7、4至8、5至6、5至7、5至8、6至7、6至8或7至8个辅助因子基因拷贝。在一些情况下,工程化宿主细胞包含每个细胞约1、2、3、4、5、6、7或8个辅助因子基因拷贝。在一些情况下,工程化宿主细胞包含每个细胞至少1、2、3、4、5、6或7个辅助因子基因拷贝。在一些情况下,工程化宿主细胞包含每个细胞至多2、3、4、5、6、7或8个辅助因子基因拷贝。
在一些情况下,辅助因子基因与异源基因的拷贝数的平衡比率导致异源蛋白质产生增加。在缺乏辅助因子蛋白质的情况下,异源基因的过表达可能使宿主细胞产生的蛋白质的量饱和,但在一些情况下,如果存在一种或多种辅助因子蛋白质,工程化宿主细胞可能能够克服饱和并进一步提供更高滴度。在一些情况下,过表达的辅助因子蛋白质也可能导致蛋白质产生降低。在一些情况下,宿主细胞可以包含每个辅助因子基因拷贝1.1、1.2、1.3、1.5、1.7、1.9、2、2.2、2.4、2.5、2.6、2.8、3、3.2、3.4、3.6、3.8、4、4.2、4.4、4.6、4.8、5、5.4、5.8、6、6.4、6.8、7、7.4、7.8、8、8.4、8.8、9、9.4、9.8、10或12个异源基因拷贝。在各种实施方案中,辅助因子编码序列与异源蛋白质编码序列的拷贝数比为至少约1:10、1:9、1:8、1:7、1:6、1:5、1:4或1:3。在一些实施方案中,辅助因子编码序列与异源蛋白质编码序列的拷贝数比为至多约1:9、1:8、1:7、1:6、1:5、1:4、1:3或1:2。
辅助因子基因与异源基因的平衡拷贝数比可以根据异源蛋白质而变化,并且不希望受理论束缚,特定比率可能提供出乎意料的优异蛋白质表达,而另一个比率(高于或低于特定比率)可能提供非期望的蛋白质表达。
在一个示例中,辅助因子基因与卵类黏蛋白(OVD)基因的拷贝数比可以为1:2至1:8。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含2至8个OVD基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含至少2个OVD基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含至多8个OVD基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含2至2.25、2至2.5、2至2.75、2至3、2至3.5、2至4、2至4.5、2至5、2至5.5、2至6、2至8、2.25至2.5、2.25至2.75、2.25至3、2.25至3.5、2.25至4、2.25至4.5、2.25至5、2.25至5.5、2.25至6、2.25至8、2.5至2.75、2.5至3、2.5至3.5、2.5至4、2.5至4.5、2.5至5、2.5至5.5、2.5至6、2.5至8、2.75至3、2.75至3.5、2.75至4、2.75至4.5、2.75至5、2.75至5.5、2.75至6、2.75至8、3至3.5、3至4、3至4.5、3至5、3至5.5、3至6、3至8、3.5至4、3.5至4.5、3.5至5、3.5至5.5、3.5至6、3.5至8、4至4.5、4至5、4至5.5、4至6、4至8、4.5至5、4.5至5.5、4.5至6、4.5至8、5至5.5、5至6、5至8、5.5至6、5.5至8或6至8个OVD基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含约2、2.25、2.5、2.75、3、3.5、4、4.5、5、5.5、6或8个OVD基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含至少2、2.25、2.5、2.75、3、3.5、4、4.5、5、5.5、6或7个OVD基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含至多2.25、2.5、2.75、3、3.5、4、4.5、5、5.5、6或8个OVD基因拷贝。
在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含2至5个卵清蛋白(OVA)基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含至少2个OVA基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含至多5个OVA基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含2至2.5、2至3、2至3.2、2至3.4、2至3.6、2至3.8、2至4、2至4.5、2至5、2.5至3、2.5至3.2、2.5至3.4、2.5至3.6、2.5至3.8、2.5至4、2.5至4.5、2.5至5、3至3.2、3至3.4、3至3.6、3至3.8、3至4、3至4.5、3至5、3.2至3.4、3.2至3.6、3.2至3.8、3.2至4、3.2至4.5、3.2至5、3.4至3.6、3.4至3.8、3.4至4、3.4至4.5、3.4至5、3.6至3.8、3.6至4、3.6至4.5、3.6至5、3.8至4、3.8至4.5、3.8至5、4至4.5、4至5或4.5至5个OVA基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含约2、2.5、3、3.2、3.4、3.6、3.8、4、4.5或5个OVA基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含至少2、2.5、3、3.2、3.4、3.6、3.8、4或4.5个OVA基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含至多2.5、3、3.2、3.4、3.6、3.8、4、4.5或5个OVA基因拷贝。
在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含1.5至5个胃蛋白酶原(PGA)基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含至少1.5个PGA基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含至多5个PGA基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含1.5至1.75、1.5至2、1.5至2.25、1.5至2.5、1.5至2.75、1.5至3、1.5至3.5、1.5至4、1.5至5、1.75至2、1.75至2.25、1.75至2.5、1.75至2.75、1.75至3、1.75至3.5、1.75至4、1.75至5、2至2.25、2至2.5、2至2.75、2至3、2至3.5、2至4、2至5、2.25至2.5、2.25至2.75、2.25至3、2.25至3.5、2.25至4、2.25至5、2.5至2.75、2.5至3、2.5至3.5、2.5至4、2.5至5、2.75至3、2.75至3.5、2.75至4、2.75至5、3至3.5、3至4、3至5、3.5至4、3.5至5或4至5个PGA基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含约1.5、1.75、2、2.25、2.5、2.75、3、3.5、4或5个PGA基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含至少1.5、1.75、2、2.25、2.5、2.75、3、3.5或4个PGA基因拷贝。在一些示例中,对于每个辅助因子基因拷贝,宿主细胞可以包含至多1.75、2、2.25、2.5、2.75、3、3.5、4或5个PGA基因拷贝。
增加的蛋白质产生
在一些情况下,本公开内容的工程化细胞及其使用方法提供了相对于对照细胞或对照方法增加的蛋白质产生。
在实施方案中,工程化细胞及其使用方法提供了相对于对照细胞或对照方法约1.1倍、1.2倍、1.3倍、1.4倍、1.5倍、1.6倍、1.7倍、1.8倍、1.9倍、2倍、2.1倍、2.2倍、2.3倍、2.4倍、2.5倍、2.6倍、2.7倍、2.8倍、2.9倍、3倍、3.1倍、3.2倍、3.3倍、3.4倍、3.5倍、3.6倍、3.7倍、3.8倍、3.9倍、约4倍或其间的任何倍数的增加的蛋白质产生。在一些实施方案中,工程化细胞及其使用方法提供了相对于对照细胞或对照方法约4.2倍、4.4倍、4.6倍、4.8倍、5倍、5.2倍、5.4倍、5.6倍、5.8倍、6倍、6.2倍、6.4倍、6.6倍、6.8倍、7倍、7.2倍、7.4倍、7.6倍、7.8倍、8倍、8.2倍、8.4倍、8.6倍、8.8倍、9倍、9.2倍、9.4倍、9.6倍、9.8倍、约10倍或其间的任何倍数的增加的蛋白质产生。在各种实施方案中,工程化细胞及其使用方法提供了相对于对照细胞或对照方法约10倍、15倍、20倍、25倍、约30倍或其间的任何倍数的增加的蛋白质产生。
在一些情况下,工程化细胞及其使用方法提供了相对于对照细胞或对照方法约1倍至约2倍、2倍至3倍、3倍至4倍、4倍至5倍、5倍至6倍、6倍至7倍、7倍至8倍、8倍至9倍、9倍至10倍、10倍至15倍、15倍至20倍、20倍至25倍或约25倍至约30倍的增加的蛋白质产生。
对照细胞可以是缺少如本文公开的第一表达盒、第二表达盒和/或第三表达盒的细胞。对照细胞可以包含小于或大于本文公开的拷贝数的异源蛋白质编码序列拷贝数。对照细胞可以包含小于或大于本文公开的拷贝数的辅助因子编码序列拷贝数。对照细胞可以包含在本文公开的比率之外(即,大于或低于)的辅助因子编码序列与异源蛋白质编码序列的拷贝数比。在一些情况下,对照可以包括上述与本文公开的工程化细胞的差异的任何组合。作为示例,辅助因子编码序列的拷贝数可以小于本文公开的拷贝数并且拷贝数比可以低于本文公开的比率,或者对照细胞可以缺少如本文公开的第二表达盒并且可以包含大于本文公开的拷贝数的辅助因子编码序列拷贝数。
启动子多样性
转录瓶颈可能是由于那些可用于介导一个或多个表达盒中的整合启动子的活性的同源转录因子库的耗竭而产生的。在一些实施方案中,引入多种表达盒,这些表达盒携带不同启动子以驱动感兴趣转基因,从而使对可用转录因子的需求多样化以驱动表达。在一些情况下,每个表达盒携带独特的启动子,该启动子不同于另一个表达盒携带的启动子。附加地,多个启动子的使用降低了盒之间的同源性,这可能增加整合的稳定性和拷贝数,特别是当多个拷贝在基因组内的位点整合在一起时。在一些情况下,当包含特定启动子的表达盒被整合至细胞的基因组中时,如果用另一个仍包含特定启动子的表达盒转化细胞,则整合的特定启动子和转化的特定启动子的同源性可能导致整合的表达盒的同源重组和切除;在这种情况下,整合表达盒的拷贝数不会在后续转化后增加,而是由于新盒的整合和旧盒的切除,拷贝数保持不变。
在本文的一些实施方案中,第一表达盒和第二表达盒含有不同的启动子序列。启动子可以衍生自不同的来源(例如,不同的调节区)。启动子可以衍生自相同或基本上类似的来源,但序列的总长度和/或调控元件的排列不同。在一些情况下,启动子可以是合成启动子。
工程化宿主细胞可以包含与整合至基因组中的异源基因的序列可操作地连接的多于一个启动子。在一些情况下,工程化宿主细胞可以包含与一个或多个异源基因的序列可操作地连接的至少2、3、4、5、6、7或8个不同启动子。在一些情况下,工程化宿主细胞可以包含与异源基因的单个序列可操作地连接的至少2、3、4、5、6、7或8个不同启动子。可以使用一个质粒或媒介物将与基因连接的每个启动子转化至宿主细胞中。备选地,可以使用多于一个质粒或媒介物将与基因连接的启动子转化至宿主细胞中。
第一表达盒的启动子可以是诱导型启动子。诱导型启动子包括这样的启动子,其在存在诱导物(诸如小分子、蛋白质、肽、温度、光或其他环境条件)时转录基因的编码序列;另一方面,在不存在诱导物时转录很少或没有转录,因此,蛋白质表达很少或没有蛋白质表达。在一些实施方案中,表达盒包括醇诱导型启动子,诸如甲醇诱导型启动子。在一些实施方案中,诸如在本文的系统和方法中采用两个或更多个不同表达盒时,每个表达盒可以采用不同的诱导型启动子。在一些实施方案中,诸如在本文的系统和方法中采用两个或更多个不同表达盒时,每个表达盒可以采用相同的诱导型启动子。在一些实施方案中,第一表达盒和第二表达盒的启动子是不同启动子序列,但均可以被相同诱导物诱导(例如,所有甲醇诱导型启动子)。用于毕赤酵母的示例性甲醇诱导型启动子包括AOX1、AOX2、FDH、PEX11,以及糖诱导型启动子,诸如葡萄糖诱导的和鼠李糖调节的启动子。表达盒中可以包括的诱导型启动子的其他示例在本公开内容的其他地方进行了描述。
第一表达盒可以包括组成型启动子,其在不需要诱导物的情况下表达。用于本文的组成型启动子可以包括从提供高表达到提供更中等和更低表达水平的表达水平谱的那些组成型启动子。在一些实施方案中,诸如在本文的系统和方法中采用两个或更多个不同表达盒时,第一和第二类型的表达盒采用不同的组成型启动子。在本文的系统和方法中采用两个或更多个不同表达盒的一些实施方案中,第一表达盒采用诱导型启动子,并且第二表达盒采用组成型启动子。
在一些情况下,启动子序列的序列同一性可以是与表1中列出的SEQ ID NO:1-8具有至少80%、90%、95%、96%、97%、98%、99%或99.5%序列同一性的序列。在一些实施方案中,一个或多个启动子选自adh1+、醇脱氢酶(ADH1、ADH2、ADH4)、AHSB4m、AINV、醇氧化酶I(AOX1)、醇氧化酶2(AOX2)、二羟基丙酮合酶(DAS)、烯醇化酶(ENO、ENO1)、甲醛脱氢酶(FLD1)、FMD、甲酸脱氢酶(FMDH)、G1、G6、GAA、GCW14、gdhA、3-磷酸甘油醛脱氢酶(gpdA、GAP、GAPDH)、磷酸甘油酸变位酶(GPM1)、甘油激酶(GUT1)、HSP82、invl+、异柠檬酸裂解酶(ICL1)、乙酰羟酸异构还原酶(ILV5)、KAR2、β-半乳糖苷酶(lac4)、LEU2、melO、MET3、nmt1、NSP、pcbC、PET9、过氧化物酶体生成蛋白8(PEX8)、磷酸甘油酸激酶(PGK,PGK1)、pho1、PHO5、PHO89、磷脂酰肌醇合酶(PIS1)、PYK1、丙酮酸激酶(pki1)、RPS7、山梨醇脱氢酶(SDH)、3-磷酸丝氨酸氨基转移酶(SER1)、SSA4、TEF、翻译延伸因子1α(TEF1)、THI11、高丝氨酸激酶(THR1)、tpi、TPS1、磷酸丙糖异构酶(TPI1)、XRP2和YPT1。
终止子
表达盒可以在蛋白质编码序列的3’端包括终止子。在一些实施方案中,终止子和启动子序列来自相同的基因来源(例如,DAS启动子和DAS终止子)。在其他实施方案中,表达盒的启动子和终止子衍生自不同的基因来源。在一些实施方案中,诸如在本文的系统和方法中采用两个或更多个不同表达盒时,每个表达盒可以采用不同的终止序列。在一些实施方案中,诸如在本文的系统和方法中采用两个或更多个不同表达盒时,每个表达盒可以采用相同的终止子。
在一些情况下,终止序列的序列同一性可以是与表2中列出的SEQ ID NO:9-10具有至少80%、90%、95%、96%、97%、98%、99%或99.5%序列同一性的序列。在一些实施方案中,表达盒的终止子选自adh1+、醇脱氢酶(ADH1、ADH2、ADH4)、AHSB4m、AINV、醇氧化酶I(AOX1)、醇氧化酶2(AOX2)、二羟基丙酮合酶(DAS)、烯醇化酶(ENO、ENO1)、甲醛脱氢酶(FLD1)、FMD、甲酸脱氢酶(FMDH)、G1、G6、GAA、GCW14、gdhA、3-磷酸甘油醛脱氢酶(gpdA、GAP、GAPDH)、磷酸甘油酸变位酶(GPM1)、甘油激酶(GUT1)、HSP82、invl+、异柠檬酸裂解酶(ICL1)、乙酰羟酸异构还原酶(ILV5)、KAR2、β-半乳糖苷酶(lac4)、LEU2、melO、MET3、nmt1、NSP、pcbC、PET9、过氧化物酶体生成蛋白8(PEX8)、磷酸甘油酸激酶(PGK、PGK1)、pho1、PHO5、PHO89、磷脂酰肌醇合酶(PIS1)、PYK1、丙酮酸激酶(pki1)、RPS7、山梨醇脱氢酶(SDH)、3-磷酸丝氨酸氨基转移酶(SER1)、SSA4、TEF、翻译延伸因子1α(TEF1)、THI11、高丝氨酸激酶(THR1)、tpi、TPS1、磷酸丙糖异构酶(TPI1)、XRP2和YPT1。
信号分泌序列
在实施方案中,本文提供的系统和方法被设计用于分泌期望的重组异源蛋白质。在一些情况下,这通过将分泌信号框内(in-frame)融合到整合至宿主细胞基因组中的多个表达盒中的重组异源蛋白质的编码区来实现。在一些实施方案中,多个表达盒可以包括异源分泌信号(例如,不是从待表达的异源蛋白质中天然衍生的)。在一些实施方案中,在本文的系统和方法中采用的多个表达盒可以包括异源分泌信号并且缺乏任何天然存在的分泌信号。
在一些实施方案中,诸如在本文的系统和方法中采用两个或更多个不同表达盒时,每个表达盒可以采用不同的分泌信号肽序列。在一些实施方案中,诸如在本文的系统和方法中采用两个或更多个不同表达盒时,每个表达盒可以采用相同的分泌信号肽序列。示例性分泌信号包括但不限于来自酿酒酵母(Saccharomyces cerevisiae)的交配因子α-因子原序列、Ostl信号序列、杂合Ost1-α-因子原序列和合成的信号序列。
在一些情况下,信号肽的序列同一性可以是与表3中列出的SEQ ID NO:11-12具有至少80%、90%、95%、96%、97%、98%、99%或99.5%序列同一性的序列。在本文公开的任一实施方案中,信号肽可以选自酸性磷酸酶、白蛋白、碱性胞外蛋白酶、α-交配因子、淀粉酶、β-酪蛋白、碳水化合物结合模块家族21-淀粉结合结构域、羧肽酶Y、纤维二糖水解酶I、二肽基蛋白酶、葡糖淀粉酶、热休克蛋白质(例如,细菌Hsp70)、疏水蛋白、菊粉酶、转化酶、杀伤蛋白质或杀伤毒素(例如,128kDa pGKL杀伤蛋白质、K1杀伤毒素的α-亚基(例如,乳酸克鲁维酵母(Kluyveromyces lactis)、K1毒素KILM1、K28前原毒素、金合欢毕赤酵母(Pichia acaciae))、富含亮氨酸人工信号肽CLY-L8、溶菌酶、植物血凝素、麦芽糖结合蛋白、P因子、毕赤酵母Dse、毕赤酵母Exg、毕赤酵母Pir1、毕赤酵母Scw、Pir4及其任何组合。
选择标志物
在本文提供的系统和方法中,用于整合至宿主细胞中的表达盒可以被设计成缺少选择标志物。在一些其他情况下,用于整合至宿主细胞中的表达盒可以被设计用于使用一种或多种选择标志物来鉴定阳性整合体。在一些情况下,用于整合至宿主细胞中的表达盒可以包括一种或多种抗生素抗性基因、营养缺陷型标志物或其组合。在一些实施方案中,诸如在本文的系统和方法中采用两个或更多个不同表达盒的情况下,每个表达盒可以采用选择标志物的不同组合。在一些实施方案中,诸如在本文的系统和方法中采用两个或更多个不同表达盒时,每个表达盒可以采用相同的选择标志物组合。示例性的选择标志物可以包括:抗生素抗性基因(例如博来霉素(zeocin)、氨苄青霉素(ampicillin)、杀稻瘟素(blasticidin)、卡那霉素(kanamycin)、诺尔丝菌素(nurseothricin)、氯霉素(chloroamphenicol)、四环素(tetracycline)、三氯生(triclosan)、更昔洛韦(ganciclovir))或其任何组合。选择标志物的其他示例可以包括营养缺陷型标志物(例如ade1、arg4、his4、ura3、met2)或其任何组合。在一些情况下,营养缺陷型标志物可以是有缺陷的营养缺陷型标志物,例如leu2-d或参与亮氨酸代谢的leu2-d变体(Betancur等人,2017)。在一些情况下,选择标志物的序列同一性可以是与表5中列出的SEQ ID NO:17-25具有至少80%、90%、95%、96%、97%、98%、99%或99.5%序列同一性的序列。
辅助因子蛋白质
工程化宿主细胞可以包编码辅助因子蛋白质的辅助因子基因的含一个或多个拷贝。在一些情况下,本文的方法可以包括使用用于表达辅助因子(诸如促进蛋白质折叠、蛋白质稳定性、蛋白质翻译和/或增加从启动子的转录的辅助因子)的表达盒进行转化。
包含一种或多种辅助因子基因的表达盒可以包含在用于表达异源基因的表达盒中使用的启动子。备选地,包含辅助因子基因的表达盒可以包含与整合至宿主基因组中用于表达异源基因的任何启动子不同的启动子。
示例性的辅助因子蛋白质包括诸如丝氨酸/苏氨酸蛋白激酶2(Kin2)、鲨烯合成酶(ERG9)、蛋白质二硫键异构酶1(PDI1)、热休克蛋白质(诸如SSA1、SSA4)、伴侣蛋白质(诸如SSB1、SSE1、BiP)、转录激活因子(诸如HAC1)、ER膜蛋白复合物亚基1(EMC1)、YNL181W氧化还原酶、整合膜蛋白锌金属蛋白酶Ste24、14-3-3蛋白Bmh2、内质网氧化还原蛋白1(Ero1)等蛋白质。在一些情况下,辅助因子蛋白质的序列同一性可以是与表6中列出的SEQ ID NO:26-39具有至少80%、90%、95%、96%、97%、98%、99%或99.5%序列同一性的序列。
用于表达盒的遗传元件的示例性组合
表达盒的遗传元件可以设计成适合在预期的宿主细胞生物中表达。例如,可以针对多个表达盒中的遗传元件进行密码子优化以在预期的宿主细胞生物中有效表达。
可以构建表达盒以包含遗传元件(例如,启动子、终止子、信号序列、选择标志物、转基因编码序列等)的任何组合。在一些情况下,可以通过转化含有pAOX1启动子、α交配因子分泌信号、tAOX1终止子以及Ura3选择标志物的表达盒来生成用于表达OVD编码序列的宿主菌株。在一些情况下,可以将pDAS2启动子与α交配因子分泌信号和tAOX1终止子组合(无选择标志物)以生成用于表达OVD编码序列的盒。在一些情况下,表达盒可以包括pPEX11启动子和tAOX1终止子。在一些情况下,表达盒可以包括驱动辅助因子蛋白质(诸如HAC1)的pPEX11启动子和tAOX1终止子。在一些情况下,用于表达OVD的表达盒可以包括pAOX1启动子、α交配因子分泌信号和tAOX1终止子以及选择标志物。
在一些情况下,可以通过转化含有pAOX1启动子、α交配因子分泌信号、tAOX1终止子以及选择标志物的表达盒来生成用于表达OVD编码序列的宿主菌株。在一些情况下,可以通过转化含有pAOX1启动子、α交配因子分泌信号、tAOX1终止子以及选择标志物的表达盒来生成用于表达OVD编码序列的宿主菌株。在一些情况下,可以通过转化含有pDAS2启动子、α交配因子分泌信号、tAOX1终止子以及选择标志物的表达盒来生成用于表达OVD编码序列的宿主菌株。在一些情况下,可以通过转化含有pFLD1启动子、α交配因子分泌信号、tAOX1终止子以及选择标志物的表达盒来生成用于表达OVD编码序列的宿主菌株。
在一些情况下,可以通过转化含有pAOX1启动子、α交配因子分泌信号、tAOX1终止子以及选择标志物的表达盒来生成用于表达PGA编码序列的宿主菌株。在一些情况下,可以通过转化含有pFDH1启动子、α交配因子分泌信号、tAOX1终止子以及选择标志物的表达盒来生成用于表达PGA编码序列的宿主菌株。在一些情况下,可以通过转化含有pFLD1启动子、α交配因子分泌信号、tAOX1终止子以及选择标志物的表达盒来生成用于表达PGA编码序列的宿主菌株。
表达盒共转化的方法
本文的方法采用共转化以生成多个表达盒进入基因组中。将作为DNA的表达盒(例如,1、2、3个或更多个不同的盒)混合在一起并转化至宿主细胞中。备选的方法可以采用预连接的盒,由此针对单个盒的多个拷贝的DNA序列,或针对不同表达盒的DNA序列在转化之前在体外(例如,在单个质粒中)连接。在一些情况下,包含设计的拷贝数的异源蛋白质(例如,重组卵清蛋白)的一个或多个质粒可以经线性化并组合在核酸的起始混合物中,以用于单一转化反应进入宿主细胞(例如,毕赤酵母)中。例如,质粒1可以含有盒的2个头对尾拷贝,该盒具有pAOX1启动子、与卵清蛋白(OVA)cDNA框内融合的α交配因子分泌信号和随后的tAOX2终止子,而质粒2可以用盒的四个头对尾拷贝构建,该盒含有pFLD1启动子、与PGAcDNA框内融合的α交配因子分泌信号和随后的tAOX1终止子。两种质粒均可以包括loxZeo选择盒。在组合转化中,质粒1和2均经线性化并组合在核酸的起始混合物中,以用于单一转化反应进入毕赤酵母中,并回收转化菌株A。
在其他情况下,可以将包含一个或多个拷贝的表达盒的一个或多个质粒顺序转化至宿主细胞中。例如,先前从组合转化获得的菌株A可以用作起始材料。然后可以用两个质粒(质粒3和4)顺序转化菌株A,每个质粒均含有与编码cDNA的卵清蛋白框内融合的PGK1信号序列。每个质粒可以含有启动子和终止子的独特组合。例如,质粒3可以含有pDAS2和tAOX2,而质粒4可以含有pFLD1和tAOX1。质粒3中的骨架可以包括LoxZeo抗性基因。质粒4中的骨架可以包括潮霉素抗性。用质粒3转化第一菌株A,并通过选择回收转化菌株B。然后用质粒4转化菌株B,并通过选择回收最终的转化菌株C。在一些情况下,质粒可以被整合至相同的基因组基因座中,或在相同的基因组基因座附近。在其他情况下,质粒可以被整合至不同的基因组基因座中。
在一些情况下,引入表达盒骨架的选择标志物可以在顺序转化之间被切除,这在本公开内容的其他地方进行了描述。在一些情况下,可以使用带有不同选择标志物的质粒进行顺序转化。
将表达盒整合至宿主细胞基因组中
在一些实施方案中,多个表达盒被整合至宿主细胞(诸如甲基营养酵母细胞,例如毕赤酵母细胞)的基因组中的单个位点中。在一些实施方案中,多个表达盒被整合在宿主细胞(诸如甲基营养酵母细胞,例如毕赤酵母细胞)的基因组中的另一个位点附近。在一些情况下,当在本文的系统和方法中采用两个或更多个不同表达盒时,第一表达盒和第二表达盒的整合位点可以位于相同的染色体上。在一些情况下,附加地,第三表达盒可以在与第一盒和第二盒不同的整合位点被整合至工程化细胞的基因组中。在一些情况下,附加地,第三表达盒可以在与第一盒和第二盒的整合位点相同的整合位点被整合至工程化细胞的基因组中。在一些情况下,当在本文的系统和方法中采用两个或更多个不同表达盒时,多个表达盒的整合位点可以位于宿主细胞基因组的不同染色体中的同源位点上。
在一些实施方案中,多个表达盒在宿主细胞的基因组位点串联整合,其中所有表达盒处于单一方向(例如,参考盒的5’至3’方向)。在一些实施方案中,多个表达盒以其中一个或多个盒与其他盒相比处于不同方向的布置被整合至宿主细胞(诸如甲基营养酵母细胞,例如毕赤酵母细胞)的基因组中。在一些情况下,在本文的系统和方法中采用两个或更多个不同表达盒时,第一表达盒和第二表达盒以相对的5’至3’方向被整合至基因组中。在一些情况下,在本文的系统和方法中采用两个或更多个不同表达盒时,第一表达盒和第二表达盒以相同的5’至3’方向被整合至基因组中。在一些情况下,附加地,第三表达盒可以以与第一盒、第二盒或第一盒和第二盒不同的5’至3’方向在整合位点处整合至工程化细胞的基因组中。在一些情况下,附加地,第三表达盒可以以与第一盒、第二盒或第一盒和第二盒相同的5’至3’方向被整合至工程化细胞的基因组中。
在一些实施方案中,可以通过非同源重组将多个表达盒异位整合至宿主细胞基因组的单个基因组基因座中。在一些实施方案中,可以通过非同源重组将多个表达盒异位整合在宿主细胞基因组中的相同基因组基因座附近或相同基因组基因座处。在一些实施方案中,可以通过在宿主细胞基因组中的相同染色体上的非同源重组将多个表达盒异位整合。在一些实施方案中,可以通过在宿主细胞基因组中的不同染色体上的非同源重组将多个表达盒异位整合。
在一些情况下,可以通过非同源重组方法将多个表达盒整合至宿主细胞(例如,毕赤酵母细胞)的基因组中。在一些情况下,当在本文的系统和方法中采用两个或更多个不同表达盒时,可以通过非同源重组整合多个表达盒中的每个表达盒。在一些情况下,当在本文的系统和方法中采用两个或更多个不同表达盒时,可以通过非同源重组整合多个表达盒中的至少一个表达盒。
在一些情况下,当在本文的系统和方法中采用两个不同表达盒时,可以通过非同源重组整合第一表达盒和第二表达盒。在一些情况下,可以通过同源重组将多个表达盒整合至宿主细胞基因组中。在一些情况下,当在本文的系统和方法中采用两个不同表达盒时,可以通过非同源重组整合第一表达盒,并且可以通过同源重组整合第二表达盒。在一些情况下,附加地,可以通过与第一盒、第二盒或第一盒和第二盒不同的重组方法将第三表达盒整合至工程化细胞的基因组中。在一些情况下,附加地,可以通过与第一盒、第二盒或第一表达盒和第二表达盒相同的重组方法将第三表达盒整合至工程化细胞的基因组中。
在一些情况下,表达盒中的序列与宿主细胞基因组中的相应序列之间存在非实质的序列同源性。例如,当在本文的系统和方法中采用两个或更多个不同表达盒时,宿主细胞中整合的基因组基因座与第一启动子、第二启动子、第一基因、第二基因、第一信号序列、第二信号序列、第一选择性标志物或第二选择标志物不具有序列同源性。
在一些情况下,宿主细胞基因组中的序列与具有表达盒的一个或多个序列之间存在序列同源性。在一些情况下,序列同源性位于或部分位于线性化表达盒的5’和3’端的序列处。在一些情况下,在本文的系统和方法中采用两个不同表达盒,并且第一表达盒和第二表达盒是线性分子的情况下,第一表达盒或第二表达盒可以在5’端包含与宿主细胞基因组基因座的同源性。例如,整合的基因组基因座中的序列与表达盒的5’序列或3’序列处的序列之间的序列同源性可以为至少5bp、至少10bp、至少20bp、至少30bp、至少40bp、至少60bp、至少80bp、至少100bp、至少120bp、至少150bp、至少180bp、至少200bp、至少250bp、至少300bp、至少350bp、至少400bp、至少450bp、至少500bp、至少600bp、至少700bp长、至少800bp长、至少900bp长或至少1000bp长。在一些情况下,整合的基因组基因座中的序列与表达盒的5’序列或3’序列处的序列之间的序列同源性可以为至多10bp、至多20bp、至多30bp、至多40bp、至多60bp、至多80bp、至多100bp、至多120bp、至多150bp、至多180bp、至多200bp、至多250bp、至多300bp、至多350bp、至多400bp、至多450bp、至多500bp、至多600bp、至多700bp长、至多800bp长、至多900bp长或至多1000bp长。
在一些情况下,可以通过依赖于表达盒中的序列与宿主细胞基因组中的相应序列之间的序列同源性的同源重组来整合表达盒。在一些情况下,同源重组可以依赖于第一表达盒中的启动子序列与基因组启动子序列之间的序列同源性。例如,同源重组可以依赖于表达盒中的AOX1启动子与基因组AOX1序列之间的序列同源性。在一些情况下,同源重组可以依赖于第一表达盒中的分泌信号序列与宿主细胞基因组细胞中的分泌信号序列之间的序列同源性。在一些情况下,同源重组可以依赖于第一表达盒中的选择标志物序列与基因组序列之间的序列同源性。例如,同源重组可以依赖于表达盒中的URA3选择标志物与基因组URA3序列之间的序列同源性。
选择标志物的切除和转化体筛选
在本文提供的方法中,将含有遗传信息的表达盒插入宿主细胞中。在一些实施方案中,可以通过本领域已知的任何方式分离成功转化体的克隆种群。在一些情况下,增加浓度的抗生素(诸如(G418)和ZeocinTM)的使用,以及它们相应的抗生素抗性基因可用于筛选多拷贝整合。可以通过本领域经培训的人员已知的标准分子生物学方法(即菌落PCR、基因组测序)挑取和验证将表达盒整合至宿主细胞基因组中的单个菌落。可以通过标准分子生物学方法(例如,Western印迹、使用已知标准蛋白质的SDS-PAGE)来确定单个蛋白质的表达。
在一些实施方案中,本文采用的方法包括整合包含选择标志物的表达盒,然后使用位点特异性基因组编辑系统切除选择标志物。在一些情况下,表达盒中的选择标志物序列,例如,抗生素抗性基因或营养缺陷型标志物可以与一对lox位点(例如,lox71和lox66;表5中提供的示例性序列;SEQ ID NO:23或24)邻接。工程化细胞中的Cre重组酶表达可用于从loxP位点切除选择标志物基因。在一些情况下,(使用诸如表5中例示的序列,SEQ ID NO:22)可以将Cre重组酶和选择标志物序列在表达盒中组合。在一些情况下,表达盒还可以含有Cre基因内含子序列,以防止Cre蛋白质表达中的遗漏。在一些情况下,Cre重组酶可以使用附加体质粒单独表达。在一些情况下,其他重组酶系统(诸如FLP/FRT位点特异性重组系统)可用于在整合至基因组后切除选择标志物。在一些实施方案中,切除lox(或其他重组酶位点)之间的序列,也切除附加的序列,诸如载体骨架、细菌复制起点、细菌选择标志物和其他序列(其中一些示例在表5中提供)。在一些实施方案中,重组酶表达盒被包括在通过在宿主细胞中表达重组酶而切除的序列中。
有多种方法可用于在不使用选择标志物的情况下鉴定具有改变的基因组的那些细胞。在一些实施方案中,这样的方法包括但不限于PCR方法(包括定量PCR)、测序方法、核酸酶消化(例如,限制酶图谱)、Southern印迹及其任何组合。表型读数,例如预测的功能增益或损失,也可以用作影响预期基因组修饰的指标。
使用本文提供的方法,在单个基因座处包含成功整合的表达盒的转化细胞的无标志物恢复(包括载体骨架和其他切除序列的丧失)可以在至少10%、20%、30%、50%、60%、70%、80%、90%或100%频率的筛选的接触宿主细胞或其克隆群内发生。在某些实施方案中,在两个、三个、四个或五个基因座处包含成功整合表达的转化细胞的无标志物恢复可以在至少10%、20%、30%、40%、50%、60%、70%、80%、90%或100%的筛选的接触宿主细胞或其克隆群中发生。
在一些情况下,第一线性表达盒可以与宿主细胞中的第二线性表达盒重组以在宿主细胞中形成两种或更多种不同的环状染色体外核酸。例如,宿主细胞可以与包含第一或第二表达盒的一个或多个拷贝的两个或更多个第二线性化质粒接触,第一和第二线性表达盒经历同源重组以形成包含选择标志物的编码序列的环状游离或染色体外核酸。一旦被环化,染色体外核酸包括选择标志物的编码序列和合适的调控序列,诸如能够在宿主细胞中表达标志物的启动子和/或终止子。
在一些实施方案中,本文所述的方法可以进一步包括从宿主细胞中消除环化的染色体外载体的步骤,例如,当选择的宿主细胞已被鉴定为包含期望的基因组整合时。在一些实施方案中,可以通过使选择的细胞经历足够的有丝分裂以使质粒从群体有效稀释来实现从选择的细胞中消除编码选择标志物的质粒。备选地,可以通过选择质粒的不存在来选择不含质粒的细胞,例如通过针对反选择标志物(例如URA3)进行选择或通过在选择性培养基和非选择性培养基上铺板相同的菌落,然后选择在选择性培养基上不生长但在非选择性培养基上生长的菌落。
宿主细胞工程化
除了整合表达盒之外,还可以单独修饰宿主细胞。这样的修饰可以在用表达盒转化之前或之后进行。在一些情况下,修饰有助于宿主细胞的生长特征和/或表达特征,从而有助于在发酵条件下产生高蛋白质滴度。
在一些实施方案中,修饰改变宿主细胞对诱导物的反应。例如,一种这样的修饰可以是将宿主细胞(例如,毕赤酵母)的生长特性改变为甲醇型生长特性的修饰。在一些实施方案中,使用突变宿主作为宿主细胞以进一步转化和整合表达盒,其中一个或多个盒包括可由甲醇诱导的启动子。在一些实施方案中,修饰包括增加由表达盒编码的蛋白质的活性形式的量、累积或产生的一种或多种因子的表达。这样的修饰可以包括一种或多种辅助因子(诸如转录因子、伴侣蛋白质和参与蛋白质折叠的其他蛋白质)、转录后修饰酶(例如,磷酸化酶、磷酸酶、糖基化酶和去糖基化酶)的表达。
在一些实施方案中,宿主细胞(例如,毕赤酵母细胞)可以经工程化以显示与同源重组相比增加的非同源重组(NHEJ)。例如,在一些情况下,宿主细胞(例如,毕赤酵母细胞)可以经工程化以过表达参与细胞的非同源重组活动的基因(即编码驱动NHEJ途径或有助于NHEJ的蛋白质的一个或多个基因)。毕赤酵母的NHEJ途径基因的示例包括但不限于YKU70、YKU 80、DNL4、Rad50、Rad 27、MRE1 1和POL4。不同宿主细胞的基因名称可能不同。NHEJ活动的增加可以是与在细胞中不过表达控制NHEJ的基因(例如毕赤酵母细胞的YKU70基因座)的宿主细胞相比,同源重组减少至少20%、30%、40%、50%、60%、70%、80%、90%、100%或减少这些百分比之间的任何百分比。
为了减轻可能由于高重组蛋白质产生而导致的细胞内氨基酸浓度的耗竭,宿主细胞可以经工程化以改善巴斯德毕赤酵母中氨基酸的供应,从而改善蛋白质产生。在一些实施方案中,编码氨基酸生物合成的通用转录激活因子的GCN4的过表达,丝氨酸、异亮氨酸、丙氨酸和芳香族氨基酸合成代谢中代谢酶的直接过表达,或真菌羧酸酯酶的直接过表达,可用于通过调整酶丰度或其动力学来优化氨基酸的合成途径。
为了克服由于高重组蛋白质产生而可能发生的能量低效的限制,可以优化宿主细胞以改善参与细胞氧化还原和能量效率的前体供应。在一些实施方案中,策略可以包括使碳转向发酵途径的基因的删除、苹果酸脱氢酶的过表达(这可以增加线粒体NADH的供应)或PPP的氧化部分中的酶(例如,NADH氧化酶)的过表达,其导致增加的NADPH和前体的供应,从而产生更高滴度的蛋白质。
巴斯德毕赤酵母中表达的异源蛋白质发生非期望的蛋白质水解不仅降低产品产量或生物活性,而且还可能使完整产品的下游加工复杂化,因为降解产物将具有相似的物理化学和亲和力性质。为了缓解蛋白质水解问题,可以使用缺乏蛋白酶的蛋白酶缺陷型宿主细胞株。蛋白酶的示例包括PEP4、羧肽酶Y(PRC1)和蛋白酶B(PRB1)。这样的巴斯德毕赤酵母蛋白酶缺陷型菌株的示例包括SMD1163(Δhis4 Δpep4 Δprb1)、SMD1165(Δhis4 Δprb1)和SMD1168(Δhis4 Δpep4)。
高重组蛋白质产生以不合适的mRNA结构、到ER的不完全蛋白质折叠或蛋白质易位的形式诱导分泌瓶颈。宿主细胞可以经工程化以通过折叠辅助蛋白质(诸如iP/Kar2p、DnaJ、PDI、PPI和Ero1p)的过表达或HAC1(UPR途径基因的转录调节因子)的过表达来克服潜在的分泌瓶颈。
在一些情况下,宿主细胞中异源蛋白质的产生可能伴随高甘露糖聚糖结构,影响血清半衰期或引发人体过敏反应。为了缓解这个问题,宿主细胞可以经进一步工程化以包括敲除蛋白质-O-甘露糖基转移酶(PMT)或由OCH1编码的酵母高尔基体蛋白质α-1,6-甘露糖基转移酶。在其他情况下,宿主细胞可以经工程化以表达里氏木霉(Trichodermareesei)α-1,2-甘露糖苷酶,或者可以使用携带适当靶向信号的几种糖基转移酶和糖苷酶中的一种(例如,β-1,2-N-乙酰葡萄糖胺转移酶1、尿苷5’-二磷酸(UDP)-GlcNAc转运蛋白、与酿酒酵母ER蛋白质Sec12的N端定位肽融合的小鼠甘露糖苷酶MnsIA催化结构域、与来自酿酒酵母高尔基体蛋白质Mnn9的前导序列融合的人GlcNAc转移酶GnTI、黑腹果蝇(Drosophila melanogaster)甘露糖苷酶II(ManII)或大鼠GlcNAc转移酶GnTII的过表达、粟酒裂殖酵母(Schizosaccharomyces pombe)半乳糖差向异构酶或人β-1,4半乳糖基转移酶的过表达)。在一些情况下,参与唾液酸合成、转运和转移的基因(例如,人UDP-N-乙酰葡萄糖胺-2-差向异构酶/N-乙酰甘露糖胺激酶(GNE)、人N-乙酰神经氨酸-9-磷酸合成酶(SPS)、人CMP-唾液酸合成酶(CSS)、小鼠CMP-唾液酸转运蛋白(CST))可以共表达,以获得最佳的唾液酸化N-聚糖。
在一些情况下,重组宿主细胞可以是甲烷氧化菌。在甲烷氧化菌中,巴斯德驹形氏酵母和法夫驹形氏酵母是优选的(也称为毕赤酵母)。毕赤酵母属菌株的示例包括毕赤酵母菌株。示例可以包括NRRL Y-11430、BG08、BG10、NRRL Y-11430GS115(NRRL Y-15851)、GS190(NRRL Y-18014)、PPF1(NRRL Y 18017)、PPY120OH、YGC4和衍生自其的菌株。可用作宿主细胞的巴斯德毕赤酵母菌株的其他示例包括但不限于CBS7435(NRRL Y-11430)、CBS704(DSMZ70382)或其衍生物。利用甲醇的酵母的其他示例包括属于Ogataea属(Ogataea morpha)、假丝酵母属(博伊丁假丝酵母(Candida boidinii))、球拟酵母属(球拟酵母(Torulopsis))或驹形氏酵母属(Komagataella)的酵母。
合适的宿主细胞生物的其他示例包括但不限于:阿克氏酵母属(Arxula spp.);食腺嘌呤阿克氏酵母(Arxula adeninivorans);克鲁维酵母属(Kluyveromyces spp.),乳酸克鲁维酵母(Kluyveromyces lactis);毕赤酵母属(Pichia spp.),安格斯毕赤酵母(Pichia angusta)、巴斯德毕赤酵母;酵母属(Saccharomyces spp.),酿酒酵母;裂殖酵母属(Schizosaccharomyces spp.),粟酒裂殖酵母;耶氏酵母属(Yarrowia spp.),解脂耶氏酵母(Yarrowia lipolytica);蘑菇属(Agaricus spp.),二孢蘑菇(Agaricus bisporus);曲霉属(Aspergillus spp.),泡盛曲霉(Aspergillus awamori)、烟曲霉(Aspergillusfumigatus)、构巢曲霉(Aspergillus nidulans)、黑曲霉(Aspergillus niger)、米曲霉(Aspergillus oryzae);炭疽菌属(Colletotrichum spp.),胶孢炭疽菌(Colletotrichumgloeosporiodes);内座壳属(Endothia spp.),寄生内座壳(Endothia parasitica);镰孢属(Fusarium spp.),禾本科镰孢(Fusarium graminearum)、腐皮镰孢(Fusarium solani);毛霉属(Mucor spp.),米黑毛霉(Mucor miehei)、微小毛霉(Mucor pusillus);毁丝霉属(Myceliophthora spp.),嗜热毁丝霉(Myceliophthora thermophila);脉胞菌属(Neurospora spp.),粗糙脉胞菌(Neurospora crassa);青霉属(Penicillium spp.),沙门柏干酪青霉(Penicillium camemberti)、变灰青霉(Penicillium canescens)、产黄青霉(Penicillium chrysogenum)、埃默森青霉(Penicillium emersonii(埃默森蓝状菌,Talaromyces emersonii))、绳状青霉(Penicillium funiculosum)、产紫青霉(Penicillium purpurogenum)、娄地青霉(Penicillium roqueforti);侧耳属(Pleurotusspp.),糙皮侧耳(Pleurotus ostreatus);根毛霉属(Rhizomucor spp.),米黑根毛霉(Rhizomucor miehei)、微小根毛霉(Rhizomucor pusillus);根霉属(Rhizopus spp.)、少根根霉(Rhizopus arrhizus)、少孢根霉(Rhizopus oligosporus)、米根霉(Rhizopusoryzae);木霉属(Trichoderma spp.),深绿木霉(Trichoderma altroviride)、里氏木霉、绿木霉(Trichoderma vireus);米曲霉(Aspergillus oryzae)、枯草芽孢杆菌(Bacillussubtilis)、大肠杆菌(Escherichia coli)、嗜热毁丝霉、粗糙脉胞菌、毕赤酵母、毕赤酵母“MutS”菌株(Graz University of Technology(CBS7435MutS)或Biogrammatics(BG11))、法夫驹形氏酵母和巴斯德驹形氏酵母。
III.定义
除非另有定义,否则本文使用的所有技术术语、符号和其他技术和科学术语或专用语旨在具有与要求保护的主题所属领域的普通技术人员通常理解的相同的含义。在一些情况下,为了清楚和/或为了便于参考,本文定义了具有普遍理解含义的术语,并且本文中包括这样的定义不一定被解释为表示与本领域通常理解的内容具有实质性差异。
在整个本申请中,可以以范围形式呈现各种实施方案。应当理解,范围形式的描述仅是为了方便和简洁,并且不应理解为对本公开内容范围的硬性限制。因此,范围的描述应该被认为已经具体公开了所有可能的子范围以及该范围内的各个数值。例如,对诸如1至6的范围的描述应该被认为具有具体公开的子范围,诸如1至3、1至4、1至5、2至4、2至6、3至6等,以及该范围内的各个数字,例如1、2、3、4、5和6。无论范围的宽度如何,这均适用。
作为示例的短语“辅助因子编码序列与异源蛋白质编码序列的比率为至少1:10”中的术语“至少”意指覆盖的比率可以相对于异源蛋白质编码序列的拷贝数具有辅助因子编码序列的更多个拷贝。换言之,“至少1:10”的条件,意指每有异源蛋白质编码序列的10个拷贝必须有辅助因子编码序列的“至少1个”拷贝,例如,可以有1个拷贝、2个拷贝、3个拷贝、4个拷贝或更多个拷贝。另一方面,作为示例的短语“辅助因子编码序列与异源蛋白质编码序列的比率为至多1:2”中的术语“至多”意指覆盖的比率可以相对于异源蛋白质编码序列的拷贝数具有辅助因子编码序列的更少个拷贝。换言之,“至多1:2”的条件,意指每有异源蛋白质编码序列的2个拷贝必须有辅助因子编码序列的“至多1”个拷贝。注意1:2的比率等同于5:10的比率;因此,“至多5:10”的等同术语将涵盖每有异源蛋白质编码序列的10个拷贝有辅助因子序列的5个拷贝,每有异源蛋白质编码序列的10个拷贝有辅助因子序列的4个拷贝,每有异源蛋白质编码序列的10个拷贝有辅助因子序列的3个拷贝,以此类推。
在本文中,术语“约”或“大约”是指在由本领域普通技术人员确定的特定值的可接受误差范围内,这将部分取决于如何测量或确定该值,例如,测量系统的局限性。例如,根据本领域的实践,“约”可以指在1个或大于1个标准偏差内。备选地,“约”可以指给定值的至多20%、至多15%、至多10%、至多5%或至多1%的范围。备选地,特别是关于生物系统或工艺,该术语可以指在值的数量级内,优选地在5倍内,更优选地在2倍内。在本申请和权利要求中描述了特定值的情况下,除非另有说明,否则应假定术语“约”的含义在特定值的可接受误差范围内。
在本文中,术语“序列同一性”,诸如为了评估互补性百分比的目的,可以通过任何合适的比对算法来测量。一般来讲,“序列同一性”是指两个多核苷酸或多肽序列分别精确的核苷酸-核苷酸或氨基酸-氨基酸对应。通常,用于确定序列同一性的技术包括确定多核苷酸的核苷酸序列和/或确定由其编码的氨基酸序列并将这些序列与第二核苷酸或氨基酸序列进行比较。可以通过确定它们的“同一性百分比”来比较两个或更多个序列(多核苷酸或氨基酸)。与可能是较长分子(例如,多核苷酸或多肽)内的序列的参考序列(例如,核酸或氨基酸序列)的同一性百分比可以计算为两个最佳比对序列之间的精确匹配数除以参考序列的长度并乘以100。还可以例如通过使用先进的BLAST计算机程序(包括2.2.9版,可获自美国国立卫生研究院)比较序列信息来确定同一性百分比。在本文中,序列同一性百分比可以指序列和它们在查询序列的跨度上的比对。如果一个序列比另一个序列短,则可以在较短序列的跨度上考虑同一性百分比。在本文中,“覆盖率百分比”可以指与两个序列中较长序列比对相同的核苷酸或氨基酸的数量占较长序列中核苷酸或氨基酸数量的百分比。
在本文中,如果一个多核苷酸与另一个多核苷酸具有100%的序列同一性并且长度相同,则将它称为另一个多核苷酸的“拷贝”。在一些情况下,如果一个多核苷酸与另一个多核苷酸具有不同的序列,但由这两个多核苷酸编码的蛋白质具有相同的氨基酸序列,则将它称为另一个多核苷酸的“拷贝”。在本文中,如果多核苷酸不是一组多核苷酸中的任何元素的拷贝,或者对于一组中所有那些元素它是一个拷贝但是除了它的基因或氨基酸序列之外还包含将它与该元素区分开的化学差异,则它与该组多核苷酸“不同”。
在本文中,“表达盒”是任何多核苷酸,其含有编码转基因的子序列并且当包含在宿主细胞中时可以赋予该子序列表达并且对于该宿主生物是异源的。
本文使用的章节标题仅用于组织目的,不应被解释为限制所描述的主题。
表1:启动子序列
表2:终止序列
表3:信号肽序列
表4:与分泌信号融合的蛋白质
表5:选择标志物和其他标志物
表6:辅助蛋白质序列
IV.实施例
以下实施例仅用于说明目的,并不旨在限制本发明的范围。
实施例1:通过顺序转化构建OVD表达菌株
使用如下的启动子、信号序列和终止子的文库构建OVD的表达盒。
用pAOX1启动子、与编码OVD(seq 1;SEQ ID NO:13)的cDNA框内融合的α交配因子分泌信号(seq 1;SEQ ID NO:13)和随后的tAOX1终止子来构建质粒1。质粒1在质粒骨架上还含有Ura3选择盒以用于选择。
用pDAS2(1)启动子、与编码OVD(seq 1;SEQ ID NO:13)的cDNA框内融合的α交配因子分泌信号(seq 1;SEQ ID NO:13)和随后的tAOX1终止子来构建质粒2。质粒2的骨架不含有选择表达盒。
通过用质粒1和质粒2的混合物转化毕赤酵母来构建菌株CF1,鉴定含有质粒1和质粒2二者的拷贝的菌落。
然后用质粒3转化所选择的菌株CF1以产生菌株CF2。质粒3包括用于同源整合至AOX1基因组位点以产生AOX1缺失表型的序列。在选择具有AOX1缺失并保留整合的质粒1和2的菌落后,然后用Cre重组酶瞬时转化该菌株以去除包含质粒骨架的floxed序列以产生菌株CF3。
对于转化,将至少1微克质粒DNA用限制酶SmiI线性化。在消化后将线性化的DNA用乙醇沉淀,然后重悬于水中。
使用Harvard Apparatus BTX ECM 630电穿孔器装置将于1M冰冷的山梨糖醇中的大约75uL的制备的感受态毕赤酵母细胞在2mm电穿孔比色皿(Bulldog Bio)中以1500V 200欧姆电穿孔,其中电容器设置为25μF。电穿孔后立即将1mL 1M山梨糖醇添加到比色皿中,然后将细胞在30℃下静置1小时,然后平板接种到具有适当抗生素(取决于所选择的与诸如博来霉素、G418、潮霉素或诺尔丝菌素等抗生素选择标志物匹配的载体)的YPD琼脂平板上,然后在30℃下温育3天,然后鉴定并挑取菌落进行试验。
如本文所用,术语“floxed”是指从基因组中去除DNA序列,其中序列的任一侧侧接有lox位点。重组酶的表达切除2个loxP位点之间的DNA序列,因此产生的菌株不再携带质粒骨架。在本文的示例中,采用两种重组酶表达方法。在第一种方法中,Cre重组酶从没有整合至毕赤酵母基因组中的复制质粒上的组成型启动子表达。当保留抗生素选择时,保留质粒。在通过重组酶去除质粒骨架后,所得菌株的抗生素选择去除,重组酶质粒不再保留。鉴定缺失质粒骨架和重组酶表达质粒的菌株。在第二种方法中,Cre重组酶从甲醇诱导型启动子表达,该启动子被整合为包含表达盒的一个或多个质粒的质粒骨架的一部分,其中具有重组酶盒的骨架侧接于loxP侧的任一侧。在甲醇诱导后,表达重组酶,然后重组酶切除该质粒骨架,从而使所得菌株缺失质粒骨架和重组酶盒。
以菌株CF3作为起始材料产生菌株CF4,然后用质粒4转化。质粒4包括上游的pPEX11启动子、编码辅助因子的序列和随后的tAOX1终止序列。质粒4的骨架包括loxZeoSynUra选择盒。
将OVD的附加拷贝添加到菌株CF4以通过用质粒5转化产生CF5。质粒5含有上游的pAOX1启动子、与OVD(seq 2;SEQ ID NO:14)cDNA框内融合的α交配因子分泌信号(seq 1;SEQ ID NO:13)和随后的tAOX1终止子。骨架还包括CLPH选择盒。
实施例2:通过组合转化构建OVD表达株
构建一系列四种质粒(质粒7-10),其各自含有与OVD(seq 2;SEQ ID NO:14)编码cDNA框内融合的α交配因子分泌信号(seq1;SEQ ID NO:13)和随后的tAOX1终止子。每个质粒在OVD融合物上游含有独特的启动子:质粒7含有pAOX1,质粒8含有pDAS2(2),质粒9含有pFLD1,并且质粒10含有pFDH1。质粒7-10各自包括上述OVD表达盒的3个拷贝,并且骨架包含loxZeo选择盒。质粒7-10经线性化,然后作为所有四种质粒的混合物被转化至毕赤酵母中。所得选定菌株被命名为CF6。
实施例3:针对表达构建体的基因组堆叠进行菌株比较
使用前述实施例中描述的构建体和方法,构建了许多菌株,如下表7所示。
表7:菌株中的整合
实施例4:蛋白质表达分析
使用Qpix菌落挑取器将来自转化的菌落挑取到96孔深孔板的YPD中。将挑取的菌落在平板振荡器中于30℃下生长24小时,然后离心,去除旧培养基,并添加含有葡萄糖和甲醇的新诱导培养基。诱导阶段持续96小时,每天补料葡萄糖/甲醇混合物。
为了测定分泌的蛋白质表达,将细胞和培养基离心,并测定所得上清液的等分试样的蛋白质含量。在一些情况下,将上清液直接添加到蛋白质测定试剂(来自ThermoScientific的Coomassie Plus蛋白质测定试剂)中,将上清液于100mM磷酸钾缓冲液中稀释,然后将其添加到蛋白质测定试剂中。将样品与蛋白质测定试剂一起温育10分钟,然后使用Spectra Max M2读板器(Molecular Devices)在595nm波长下读数。数据以每升的蛋白质克数计算。
为了测定蛋白质量并确认蛋白质测定的结果,通过SDS PAGE分析上清液并用简单蓝色安全染料(Simply Blue Safe Stain,Life Technologies)染色。使用Protein Simple成像仪记录所得凝胶图像。
实施例5:OVD菌株的蛋白质表达水平
对四种基因组堆叠的OVD菌株CF3、CF4、CF10和CF6的蛋白质表达进行相互比较,在使用深孔板生长形式的高通量筛选(HTS)(如实施例4中所述)中并且在2升生物反应器中在高细胞密度生长条件下(DASGIP)比较总蛋白质(如实施例7中进一步解释)。在HTS深孔板生长形式下,使用CF6产生的蛋白质滴度作为基线(100%),菌株CF10(105.3%)和CF6(100%)比CF3(74.9%)和CF4(76.5%)菌株的总蛋白质表达更高。在DASGIP条件下,使用CF6产生的蛋白质滴度作为基线(100%),与CF3(约135%)和CF6菌株相比,CF4和CF10的大规模总蛋白质产量分别为大约164%和200%
实施例6:在大体积发酵条件下的表达
使菌株CF3、CF5和CF10在40升发酵罐中生长。将酵母菌株甘油储备液解冻并以0.2%的接种率接种在含有BMDY培养基(BMDY培养基与BMGY培养基相似,其中甘油“G”已被葡萄糖/右旋糖“D”替代,毕赤酵母简易选择手册,Thermo Fisher)的具挡板摇瓶中。将摇瓶在30℃和250rpm下温育26小时。然后将摇瓶培养物以10%的比率转移到含有BSM(基础盐培养基)、葡萄糖和痕量金属的生物反应器中(毕赤酵母发酵工艺指南,Thermo Fisher)。
生物反应器发酵分为三个阶段。在第1阶段,使培养物生长24小时,直至所有葡萄糖均被消耗。在第2阶段,以葡萄糖限制速率向培养物补料葡萄糖12小时。最后,在第3阶段,通过连续补料葡萄糖和诱导型启动子的激活剂(即甲醇)的共同补料来诱导培养物96小时。
上清液中OVD的表达水平以克/升培养基测量。表8显示了在生物反应器中生长的不同菌株的上清液中OVD的相对蛋白质表达。滴度以g/L测量并用于计算倍数提高,或以表8中的相对水平呈现。菌株CF10是分泌型OVD的最高表达者。
表8:相对表达水平
菌株 | 相对表达水平 |
CF3 | +++ |
CF5 | ++ |
CF10 | ++++ |
实施例7:具有同源整合位点与非同源整合位点的OVD工程化菌株的比较
通过在紧邻AOX1基因上游经由同源重组(即,依赖于盒中的AOX1启动子与基因组AOX1序列之间的序列同源性)将盒整合而产生一系列包含AOX1表达盒的转化体。通过测序确定的每个菌株中OVD的拷贝数在CF11菌株中为大约5,在CF12菌株中为1,并且在CF13菌株中为7-8。这些菌株中OVD的拷贝数与OVD的表达水平相关。将这3个工程化菌株与在非同源位点仅整合OVD的4-5个拷贝的CF1(实施例3)进行比较。出乎意料的是,没有一个同源整合的工程化OVD菌株的表达水平与CF1相当;CF1菌株的OVD表达显著高于具有相似OVD拷贝数的CF11,并且显著高于具有较高OVD拷贝数的CF13。
在单独的实验中,使用质粒进一步用附加的OVD拷贝对已经表达OVD的两个毕赤酵母菌株CF14和CF15进行转化。CF14和CF15均衍生自CF16,CF16是实施例2中描述的CF6的衍生菌株并且包含由pPEX11驱动的添加的Hac1辅助因子基因。用以下2个质粒转化CF14和CF15:含有3个OVD拷贝的质粒3X,含有6个OVD拷贝的质粒6X。3X和6X质粒中的OVD拷贝由AOX1、DAS和FLD启动子驱动。AOX1终止子用于两个质粒。每组选择80-320个转化体(如表9所示)。从每组中选择高表达者。使用PCR确认OVD质粒的整合位点。使用CF6产生的蛋白质滴度作为基线(100%),CF14和CF15的DASGIP滴度分别为176%和164%。
将CF15重转化组中的六个和CF14重转化组中的三个(质粒3X和6X转化体)划线用于单菌落,挑取5或6个单菌落并测定高蛋白质表达。表9指示了针对每个转化筛选的转化体的数量。表10指示了在期望位点呈插入阳性的转化体的数量与通过PCR检测时筛选的转化体总数的比较。
图1A-B显示了来自该实验的CF14和CF15重复筛选的总结,该实验通过质粒3X和6X的同源和非同源(异位)整合位点分离重复转化体组。
异位整合(即在非同源基因组位点整合)的转化体在每个重复转化体组中产生最高表达(在该数据中未区分来自3X和6X质粒的重复转化体)。
表9:转化体
CF14 | CF15 | |
3x | 240 | 160 |
6x | 320 | 80 |
表10:在期望位点呈插入阳性的转化子
CF14 | CF15 | |
3x | 3/8 | 4/6 |
6x | 4/8 | 2/3 |
实施例8:OVD菌株的比较
使用与实施例1至7中所述相似的方法制备毕赤酵母菌株D1-D10。一些菌株包含辅助因子HAC1。HAC1表达的表达盒在所有情况下均使用PEX11启动子和AOX1终止序列进行表达,但D10除外,D10中除了PEX11外,还使用DAS启动子用于HAC1表达。下表11显示了每个菌株的序列中存在的启动子、OVD的拷贝数和辅助因子的拷贝数。结果在下表11中提供。表11表明使用辅助拷贝时滴度明显提高,即使在减少异源基因拷贝数时也是如此。如所示,将异源基因(OVD)拷贝数从15个减少到12个,同时添加2个辅助拷贝,增加了深孔滴度(平均约10%)和DASGIP滴度(平均约50%)。然而,将辅助拷贝数进一步增加到4产生不同的结果(降低了深孔滴度,增加了DASGIP滴度)。
表11:OVD菌株的结果
带有星号的菌株经进一步修饰以降低甲醇利用能力,从而简化发酵条件。
实施例9:通过组合转化来构建胃蛋白酶原表达菌株
如下构建一系列含有胃蛋白酶原表达盒的质粒。所有质粒在其骨架中均含有loxZeo选择标志物盒,且所有质粒在转化至毕赤酵母之前均经线性化。质粒11包含盒的3个头对尾拷贝,该盒具有pAOX1启动子、与胃蛋白酶原(PGA)cDNA(SEQ ID NO:15)框内融合的α交配因子分泌信号、和随后的tAOX1终止子。
质粒12由具有pAOX1启动子、与PGA cDNA框内融合的α交配因子分泌信号和随后的tAOX1终止子的盒的2个头对尾拷贝以及具有pFDH1启动子、与PGA cDNA框内融合的α交配因子分泌信号和随后的tAOX1终止子的盒的1个拷贝来构建。
质粒13由具有pAOX1启动子、与PGA cDNA框内融合的α交配因子分泌信号和随后的tAOX1终止子的盒的2个头对尾拷贝以及具有pFLD1启动子、与PGA cDNA框内融合的α交配因子分泌信号和随后的tAOX1终止子的盒的1个拷贝来构建。
质粒14包含具有pAOX1启动子、与PGA cDNA框内融合的α交配因子分泌信号和随后的tAOX1终止子的盒的2个头对尾拷贝以及具有pDAS2(3)启动子、与PGA cDNA框内融合的α交配因子分泌信号和随后的tAOX1终止子的盒的1个拷贝。质粒14被构建成具有盒的4个头对尾拷贝,该盒具有pAOX1启动子、与PGA cDNA框内融合的α交配因子分泌信号和随后的tAOX1终止子。
质粒15包含具有pAOX1启动子、与PGA cDNA框内融合的α交配因子分泌信号和随后的tAOX1终止子的盒的2个头对尾拷贝以及具有pFLD1启动子、与PGA cDNA框内融合的α交配因子分泌信号和随后的tAOX1终止子的盒的2个拷贝。
将全部经线性化的质粒11-15组合在核酸的起始混合物中,用于单一转化反应进入毕赤酵母中。从转化中分离菌株CF9。
实施例10:通过顺序转化来构建胃蛋白酶原表达菌株
使用菌株CF9作为起始材料。然后用质粒6和质粒16转化,其含有pAOX1启动子、与PGA cDNA框内融合的α交配因子分泌信号和随后的tAOX1终止子,其中骨架含有CLPH标志物盒。去除转化的floxed骨架。从这些顺序转化中分离菌株CF7和CF8。
实施例11:用胃蛋白酶原表达盒进行基因组堆叠的毕赤酵母的转化
巴斯德毕赤酵母菌株BG08(BioGrammatics Inc.,Carlsbad;CA,USA)是从农业研究服务培养物保藏中心(Agriculture Research Service culture collection)获得的Phillips Petroleum菌株NRRL Y-11430的单菌落分离物(Sturmberger等人,2016)。使用Hoechst染料选择来去除细胞质杀伤质粒(Sturmberger等人,2016),从BG08衍生巴斯德毕赤酵母BG10(BioGrammatics Inc,Carlsbad,CA,USA)。然后将得到的BG10菌株进一步修饰,使其缺失醇氧化酶1基因(AOX1)。这种缺失产生甲醇利用缓慢的表型,该表型降低菌株消耗甲醇的能力。该基础菌株称为DFB-001,用于转化胃蛋白酶原构建体。
将胃蛋白酶原构建体连同用于在强甲醇诱导型启动子控制下表达巴斯德毕赤酵母转录因子HAC1的构建体一起转化至毕赤酵母中,并选择表达和分泌胃蛋白酶原的分离物。选择作为高产者的转化体用于后续步骤。高产菌株的繁殖证实,引入菌株的所有变化均稳定地整合至基因组中,并证实在非选择性生长培养基上生长>45代后存在。
对选择的转化体(所得菌株)进行DNA测序;它包含HAC1表达盒的三个拷贝和胃蛋白酶原表达盒的五个拷贝。测序也证实该菌株不含任何抗生素标志物或原核载体复制起点序列。测序显示胃蛋白酶原盒均位于所得菌株的1号染色体上的基因座上(见下表12)。
表12:菌株中的整合
实施例12:胃蛋白酶原菌株的蛋白质表达水平
在两种生长条件下,将两个胃蛋白酶原基因组堆叠菌株CF7和CF8的蛋白质表达相互比较。第一个条件是在高通量筛选(HTS)中表达,使用深孔板生长形式,如实施例3所述。CF8菌株显示出比CF7菌株更高的蛋白质表达。还在高细胞密度生长条件下的2升生物反应器中比较这些菌株(DASGIP,参见实施例7)。简而言之,将酵母菌株甘油储备液解冻并以0.2%的接种率接种在含有BMDY培养基(BMDY培养基与BMGY培养基相似,其中甘油“G”已被葡萄糖/右旋糖“D”替代,毕赤酵母简易选择手册,Thermo Fisher)的具挡板摇瓶中。将摇瓶在30℃和250rpm下温育26小时。然后将摇瓶培养物以10%的比率转移到含有BSM(基础盐培养基)、葡萄糖和痕量金属的生物反应器中(毕赤酵母发酵工艺指南,Thermo Fisher)。生物反应器发酵分为三个阶段。在第1阶段,使培养物生长24小时,直到所有葡萄糖均被消耗。在第2阶段,以葡萄糖限制速率向培养物补料葡萄糖12小时。最后,在第3阶段,通过连续补料葡萄糖和诱导型启动子的激活剂(即甲醇)的共同补料来诱导培养96小时。
测定菌株的总分泌蛋白质,然后测定感兴趣的总分泌蛋白质(测定为存在于上清液中)。在两次测量中,CF8菌株均优于CF7菌株。使用来自以下实施例13的P5小规模滴度,CF7的小规模HTS滴度为22%并且CF8为45%。使用来自以下实施例13的P5大规模滴度,CF7的大规模DASGIP滴度为108%并且CF8为117.5%。
实施例13:胃蛋白酶原菌株的比较
使用与实施例9至12中所述相似的方法制备毕赤酵母菌株P1-P5,其中所有表达盒均使用AOX1终止序列。一些菌株包含辅助因子HAC1。HAC1表达的表达盒在所有情况下均使用PEX11启动子和AOX1终止序列进行表达。下表13显示了每个菌株的序列中存在的启动子、PGA的拷贝数和辅助因子的拷贝数。结果在下表13中提供。
表13:PGA菌株的结果
实施例14:卵清蛋白菌株的比较
使用与针对OVD和PGA中所述的方法类似地制备表达毕赤酵母卵清蛋白(OVA)的菌株V1-V8,其中所有表达盒均使用AOX1终止序列。SEQ ID NO:16与下表14中描述的启动子可操作地连接。菌株V1是基础菌株,用具有驱动OVA表达的启动子FLD和DAS1的表达盒转化菌株V2。用具有驱动OVA表达的AOX1启动子的附加表达盒转化菌株V2,从而产生菌株V7。一些菌株(诸如V7)包含辅助因子HAC1。HAC1表达的表达盒在所有情况下均使用Pex11启动子和AOX1终止序列进行表达。下表14显示了每个菌株的序列中存在的启动子、OVA的拷贝数和辅助因子的拷贝数。
表14展示了在使用辅助拷贝时,特别是在某些比率下显著提高的滴度。如所示,使用HAC1拷贝显著提高了深孔和DASGIP滴度二者。可以看出,增加异源基因(OVA)拷贝数对提高滴度几乎没有作用(比较3个OVA拷贝与9个OVA拷贝),但添加HAC1拷贝显示滴度显著提高,其中深孔滴度提高超过5倍,而DASGIP滴度提高至3倍或更多。另外,随着异源基因拷贝数增加而观察到收益递减,当HAC1拷贝数从2增加到5时观察到收益递减(或减少),表明异源基因拷贝与辅助拷贝的最佳工作比率。
表14:OVA菌株的结果
带有星号的菌株经进一步修饰以降低甲醇利用能力,这简化了发酵条件
虽然本文已经示出和描述了本发明的优选实施方案,但是对于本领域技术人员而言显而易见的是,这些实施方案仅作为示例提供。在不脱离本发明的情况下,本领域技术人员现在将想到许多变化、改变和替换。应当理解,在实施本发明时可以使用本文所述的本发明实施方案的各种替代方案。所附权利要求旨在限定本发明的范围,并且由此涵盖这些权利要求范围内的方法和结构及其等同物。
序列表
<110> 克莱拉食品公司
<120> 用于高产重组微生物的系统和方法及其用途
<130> 49160-719.601
<150> US 62/970,052
<151> 2020-02-04
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<400> 3
gatctctgag acaacgatga acctcccatg tagattccac cgccccaatt actgttttgg 60
gcaatcctgt tgataagacg cattctagag ttgtttcatg aaagggttac gggtgttgat 120
tggtttgaga tatgccagag gacagatcaa tctgtggttt gctaaactgg aagtctggta 180
aggactctag caagtccgtt actcaaaaag tcataccaag taagattacg taacacctgg 240
gcatgacttt ctaagttagc aagtcaccaa gagggtccta tttaacgttt ggcggtatct 300
gaaacacaag acttgcctat cccatagtac atcatattac ctgtcaagct atgctacccc 360
acagaaatac cccaaaagtt gaagtgaaaa aatgaaaatt actggtaact tcaccccata 420
acaaacttaa taatttctgt agccaatgaa agtaaacccc attcaatgtt ccgagattta 480
gtatacttgc ccctataaga aacgaaggat ttcagcttcc ttaccccatg aacagaaatc 540
ttccatttac cccccactgg agagatccgc ccaaacgaac agataataga aaaaagaaat 600
tcggacaaat agaacacttt ctcagccaat taaagtcatt ccatgcactc cctttagctg 660
ccgttccatc cctttgttga gcaacaccat cgttagccag tacgaaagag gaaacttaac 720
cgataccttg gagaaatcta aggcgcgaat gagtttagcc tagatatcct tagtgaaggg 780
ttgttccgat acttctccac attcagtcat agatgggcag ctttgttatc atgaagagac 840
ggaaacgggc attaagggtt aaccgccaaa ttatataaag acaacatgtc cccagtttaa 900
agtttttctt tcctattctt gtatcctgag tgaccgttgt gtttaatata acaagttcgt 960
tttaacttaa gaccaaaacc agttacaaca aattataacc cctctaaaca ctaaagttca 1020
ctcttatcaa actatcaaac atcaaagg 1048
<210> 4
<211> 564
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 4
tgctcctata aggaacgaag ggttccagct tccttacccc atcaatggaa atctcctatt 60
taccccccac tggaaagatc cgtccgaacg aacggataat agaaaaaaga aattcggaca 120
aaatagaaca cttatttagc caatgaaatc catttccagc atctccttca actgccgttc 180
catccccttt gttgagctac accatcgtca gccagtaccg aataggaaac ttaaccgata 240
tcttggagac ttctaatgcg cgaatgagtt tagcctagat atccttagtg aagggttgtt 300
ccgatacttc tccacattca gtcatttcag atgggcagca ttgttatcat gaagaaacgg 360
aaacgggcag taagggttaa ccgccaaatt atataaagac aacatgtccc cagtttaaag 420
tttttctttc ctattcttgt atcctgagtg accgttgtgt ttaaaataac aagttcgttt 480
taacttaaga ccaaaaccag ttacaacaaa ttattcccca actaaacact aaagttcact 540
cttatcaaac tatcaaacat caaa 564
<210> 5
<211> 750
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 5
cttccccatt tcactgacag tttgtagaaa tagggcaaca attgatgcaa atcgattttc 60
aacgcattgg ttttgatagc attgatgatc ttggagctgt aaaagtccgg ctggataagc 120
tcaatgaaat aggttggttg atctggatct tcttttgggt cattttgttc gctctgtatt 180
tcacaaattg ccagaatctc tgccaaccac agtggtaggt ccaacttggt gttctgaatc 240
acaggcttcc ccgggttgtt ctctaaataa ccgaggcccg gcacagaaat cgtaaaccga 300
cacggtatct tttgtccgtc cgccagtatc tcatcaaggt cgtagtagcc catgatgagt 360
atcaaagggg atttggttat gcgatgcaac gagagattgt ttatcccaga tgctgatgta 420
aaaaccttaa ccagcgtgac agtagaaata agacacgtta aaattacccg cgcttcccta 480
acaattggct ctgcctttcg gcaagtttct aactgccctc ccctctcaca tgcaccacga 540
acttaccgtt cgctcctagc agaaccaccc caaagtttaa tcaggaccgc attttagcct 600
attgctgtag aaccccacaa cataacctgg tccagagcca gccctttata tatggtaaat 660
cccgtttgaa cttcgaagtg gaatcggaat ttttacatca aagaaactga tactgaaact 720
tttggcttcg acttggactt tctcttaatc 750
<210> 6
<211> 1005
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 6
aaataaatgg cagaaggatc agcctggacg aagcaaccag ttccaactgc taagtaaaga 60
agatgctaga cgaaggagac ttcagaggtg aaaagtttgc aagaagagag ctgcgggaaa 120
taaattttca atttaaggac ttgagtgcgt ccatattcgt gtacgtgtcc aactgttttc 180
cattacctaa gaaaaacata aagattaaaa agataaaccc aatcgggaaa ctttagcgtg 240
ccgtttcgga ttccgaaaaa cttttggagc gccagatgac tatggaaaga ggagtgtacc 300
aaaatggcaa gtcgggggct actcaccgga tagccaatac attctctagg aaccagggat 360
gaatccaggt ttttgttgtc acggtaggtc aagcattcac ttcttaggaa tatctcgttg 420
aaagctactt gaaatcccat tgggtgcgga accagcttct aattaaatag ttcgatgatg 480
ttctctaagt gggactctac ggctcaaact tctacacagc atcatcttag tagtcccttc 540
ccaaaacacc attctaggtt tcggaacgta acgaaacaat gttcctctct tcacattggg 600
ccgttactct agccttccga agaaccaata aaagggaccg gctgaaacgg gtgtggaaac 660
tcctgtccag tttatggcaa aggctacaga aatcccaatc ttgtcgggat gttgctcctc 720
ccaaacgcca tattgtactg cagttggtgc gcattttagg gaaaatttac cccagatgtc 780
ctgattttcg agggctaccc ccaactccct gtgcttatac ttagtctaat tctattcagt 840
gtgctgacct acacgtaatg atgtcgtaac ccagttaaat ggccgaaaaa ctatttaagt 900
aagtttattt ctcctccaga tgagactctc cttcttttct ccgctagtta tcaaactata 960
aacctatttt acctcaaata cctccaacat cacccactta aacag 1005
<210> 7
<211> 1002
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 7
cagccattaa tctcacctca gtttttgaat cagtagaatt tttaatgaaa caaacggttg 60
gtatattatt tgatagagtt gccaaatttc caaagataaa tttttcatca ggtaatatcc 120
tgaataccgt aacatagtga ctattggaag acactgctat catattatat ttcggataaa 180
aatccaaacc ccagaccgac ctcttgagtc tcaactccaa gtcagccgca actttaatta 240
tccgtggatt gggagctagt ttggacaacg catcagtata atataacttt acggttccat 300
tatcagacgc tattgcaaga acttcctttc cattgatctc gccaatgcgg cagtaattga 360
tatcgtaggg taggtctgga aagacgctgg cgcttgtgtc ccattctgca ggaatctctg 420
gcacggtgct aatggtagtt atccaacgga gctgaggtag tcgatatatc tggatatgcc 480
gcctatagga taaaaacagg agagggtgaa ccttgcttat ggctactaga ttgttcttgt 540
actctgaatt ctcattatgg gaaactaaac taatctcatc tgtgtgttgc agtactattg 600
aatcgttgta gtatctacct ggagggcatt ccatgaatta gtgagataac agagttgggt 660
aactagagag aataatagac gtatgcatga ttactacaca acggatgtcg cactctttcc 720
ttagttaaaa ctatcatcca atcacaagat gcgggctgga aagacttgct cccgaaggat 780
aatcttctgc ttctatctcc cttcctcata tggtttcgca gggctcatgc cccttcttcc 840
ttcgaactgc ccgatgagga agtccttagc ctatcaaaga attcgggacc atcatcgatt 900
tttagagcct tacctgatcg caatcaggat ttcactactc atataaatac atcgctcaaa 960
gctccaactt tgcttgttca tacaattctt gatattcaca gg 1002
<210> 8
<211> 619
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 8
cttcagtaat gtcttgtttc ttttgttgca gtggtgagcc attttgactt cgtgaaagtt 60
tctttagaat agttgtttcc agaggccaaa cattccaccc gtagtaaagt gcaagcgtag 120
gaagaccaag actggcataa atcaggtata agtgtcgagc actggcaggt gatcttctga 180
aagtttctac tagcagataa gatccagtag tcatgcatat ggcaacaatg taccgtgtgg 240
atctaagaac gcgtcctact aaccttcgca ttcgttggtc cagtttgttg ttatcgatca 300
acgtgacaag gttgtcgatt ccgcgtaagc atgcataccc aaggacgcct gttgcaattc 360
caagtgagcc agttccaaca atctttgtaa tattagagca cttcattgtg ttgcgcttga 420
aagtaaaatg cgaacaaatt aagagataat ctcgaaaccg cgacttcaaa cgccaatatg 480
atgtgcggca cacaataagc gttcatatcc gctgggtgac tttctcgctt taaaaaatta 540
tccgaaaaaa ttttctagag tgttgttact ttatacttcc ggctcgtata atacgacaag 600
gtgtaaggag gactaaacc 619
<210> 9
<211> 261
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 9
tcaagaggat gtcagaatgc catttgcctg agagatgcag gcttcatttt tgatactttt 60
ttatttgtaa cctatatagt ataggatttt ttttgtcatt ttgtttcttc tcgtacgagc 120
ttgctcctga tcagcctatc tcgcagcaga tgaatatctt gtggtagggg tttgggaaaa 180
tcattcgagt ttgatgtttt tcttggtatt tcccactcct cttcagagta cagaagatta 240
agtgaaacct tcgtttgtgc g 261
<210> 10
<211> 476
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 10
aattgacacc ttacgattat ttagagagta tttattagtt ttattgtatg tatacggatg 60
ttttattatc tatttatgcc cttatattct gtaactatcc aaaagtccta tcttatcaag 120
ccagcaatct atgtccgcga acgtcaacta aaaataagct ttttatgctc ttctctcttt 180
ttttcccttc ggtataatta taccttgcat ccacagattc tcctgccaaa ttttgcataa 240
tcctttacaa catggctata tgggagcact tagcgccctc caaaacccat attgcctacg 300
catgtatagg tgttttttcc acaatatttt ctctgtgctc tctttttatt aaagagaagc 360
tctatatcgg agaagcttct gtggccgtta tattcggcct tatcgtggga ccacattgcc 420
tgaattggtt tgccccggaa gattggggaa acttggatct gattacctta gctgca 476
<210> 11
<211> 267
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 11
atgagattcc catctatttt caccgctgtc ttgttcgctg cctcctctgc attggctgcc 60
cctgttaaca ctaccactga agacgagact gctcaaattc cagctgaagc agttatcggt 120
tactctgacc ttgagggtga tttcgacgtc gctgttttgc ctttctctaa ctccactaac 180
aacggtttgt tgttcattaa caccactatc gcttccattg ctgctaagga agagggtgtc 240
tctctcgaga aaagagaggc cgaagct 267
<210> 12
<211> 267
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 12
atgagattcc cttctatttt cactgctgtt ttgttcgctg cttcttctgc tttggctgct 60
ccagttaaca ctactaccga agacgaaact gctcaaattc ctgctgaagc tgttattggt 120
tactctgact tggaaggtga cttcgacgtt gctgttttgc cattctctaa ctctactaac 180
aacggtttgt tgttcattaa cactactatt gcttctattg ctgctaagga agaaggtgtt 240
tctttggaca agagagaagc tgaagct 267
<210> 13
<211> 561
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 13
gctgaagtag actgctcaag atttccaaat gctactgaca aggaaggaaa ggatgtcctc 60
gtatgtaaca aggaccttag acccatttgc ggtacggatg gcgtgacata cactaatgat 120
tgtttactat gtgcctatag cattgagttc ggtacaaaca tctccaaaga gcacgatgga 180
gaatgtaaag agactgtccc tatgaactgt tcctcttacg caaatacaac ttcagaggac 240
ggtaaggtga tggtcttgtg taacagggct ttcaatccag tttgtggtac tgacggtgtt 300
acttacgata acgaatgtct gttgtgtgct cataaagttg agcaaggagc atctgttgat 360
aaaagacacg atggtggatg ccgtaaggaa ttggccgcag tttcggtgga ctgctccgaa 420
tatccaaaac ctgactgtac cgctgaggat cgtcctctgt gcggaagtga caacaagacc 480
tatggtaata agtgtaattt ctgtaatgct gttgttgaaa gcaatggtac attaacattg 540
tctcattttg gtaaatgtta a 561
<210> 14
<211> 558
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 14
gcagaagttg actgttctcg tttcccaaat gctactgaca aggaaggaaa agacgtcttg 60
gtgtgtaaca aggatttgag gccaatttgt ggtacagatg gtgtgactta cactaatgat 120
tgtctacttt gcgcatatag catcgagttt ggaaccaata tctcaaaaga gcacgacggt 180
gaatgtaaag agactgtccc aatgaactgt tcttcctacg ctaatacaac ctccgaggat 240
ggtaaagtaa tggttttgtg caacagagcc tttaatcctg tttgtggcac ggatggagtc 300
acttatgata atgaatgtct cctgtgcgcc cacaaggtag aacaaggtgc tagcgttgat 360
aagcgtcatg acggtggatg tagaaaggaa ttagctgctg tgtctgttga ttgttcagaa 420
tatcccaagc ctgactgtac agctgaggac agacctctgt gcggttccga caacaaaaca 480
tacggaaaca aatgcaactt ctgtaatgca gtggttgagt cgaatggaac attgacttta 540
agtcatttcg gtaaatgt 558
<210> 15
<211> 1113
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 15
ctagtaaagg tgcctctagt tagaaagaag agtctgagac aaaacctaat taagaacgga 60
aaactgaagg atttcttaaa aacgcataaa cataaccccg cctccaaata ctttcctgaa 120
gcagccgctt taataggcga cgaaccttta gaaaattact tagataccga gtatttcggc 180
actattggta ttggtacgcc cgcacaagat ttcacggtaa tcttcgacac cggcagttca 240
aatttatggg tgccctccgt gtattgtagt agtttggctt gctccgacca taatcagttc 300
aaccccgatg attcctccac gttcgaggcc acgagtcaag aattgagtat aacctacggc 360
accggttcca tgacaggcat cctaggatac gatacagtac aagtcggcgg catttccgac 420
accaatcaga tatttggcct aagtgagacc gagcccggat ctttcttgta ctacgcccct 480
ttcgacggaa tcttgggtct agcttatcct agtatatctg catccggagc tacacccgtg 540
tttgacaacc tatgggatca gggccttgtc tcccaggatc tattctcagt ctacctgagt 600
agtaatgatg attcaggctc agtagtgttg ctaggcggaa ttgattctag ttactacaca 660
ggttctctga actgggttcc tgtcagtgta gagggctatt ggcagatcac actggattcc 720
ataactatgg atggagagac catcgcctgc tccggcggtt gtcaggcaat agtggatacc 780
ggaaccagtc tgttgactgg ccctacctct gccatagcta atatacaaag tgatatagga 840
gcatctgaga actctgacgg cgagatggta atctcttgtt ctagtatcga ttcattacct 900
gacatagttt ttaccataaa tggtgttcaa taccccctaa gtccttccgc ctatatcttg 960
caagatgatg actcatgtac aagtggcttt gaaggtatgg atgtacccac gtcatcaggt 1020
gagctttgga tactgggcga tgtgtttatc aggcaatact acaccgtgtt cgatagggct 1080
aacaacaagg tgggtctagc acctgttgca taa 1113
<210> 16
<211> 474
<212> PRT
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 16
Met Arg Phe Pro Ser Ile Phe Thr Ala Val Leu Phe Ala Ala Ser Ser
1 5 10 15
Ala Leu Ala Ala Pro Val Asn Thr Thr Thr Glu Asp Glu Thr Ala Gln
20 25 30
Ile Pro Ala Glu Ala Val Ile Gly Tyr Ser Asp Leu Glu Gly Asp Phe
35 40 45
Asp Val Ala Val Leu Pro Phe Ser Asn Ser Thr Asn Asn Gly Leu Leu
50 55 60
Phe Ile Asn Thr Thr Ile Ala Ser Ile Ala Ala Lys Glu Glu Gly Val
65 70 75 80
Ser Leu Asp Lys Arg Glu Ala Glu Ala Gly Ser Ile Gly Ala Ala Ser
85 90 95
Met Glu Phe Cys Phe Asp Val Phe Lys Glu Leu Lys Val His His Ala
100 105 110
Asn Glu Asn Ile Phe Tyr Cys Pro Ile Ala Ile Met Ser Ala Leu Ala
115 120 125
Met Val Tyr Leu Gly Ala Lys Asp Ser Thr Arg Thr Gln Ile Asn Lys
130 135 140
Val Val Arg Phe Asp Lys Leu Pro Gly Phe Gly Asp Ser Ile Glu Ala
145 150 155 160
Gln Cys Gly Thr Ser Val Asn Val His Ser Ser Leu Arg Asp Ile Leu
165 170 175
Asn Gln Ile Thr Lys Pro Asn Asp Val Tyr Ser Phe Ser Leu Ala Ser
180 185 190
Arg Leu Tyr Ala Glu Glu Arg Tyr Pro Ile Leu Pro Glu Tyr Leu Gln
195 200 205
Cys Val Lys Glu Leu Tyr Arg Gly Gly Leu Glu Pro Ile Asn Phe Gln
210 215 220
Thr Ala Ala Asp Gln Ala Arg Glu Leu Ile Asn Ser Trp Val Glu Ser
225 230 235 240
Gln Thr Asn Gly Ile Ile Arg Asn Val Leu Gln Pro Ser Ser Val Asp
245 250 255
Ser Gln Thr Ala Met Val Leu Val Asn Ala Ile Val Phe Lys Gly Leu
260 265 270
Trp Glu Lys Ala Phe Lys Asp Glu Asp Thr Gln Ala Met Pro Phe Arg
275 280 285
Val Thr Glu Gln Glu Ser Lys Pro Val Gln Met Met Tyr Gln Ile Gly
290 295 300
Leu Phe Arg Val Ala Ser Met Ala Ser Glu Lys Met Lys Ile Leu Glu
305 310 315 320
Leu Pro Phe Ala Ser Gly Thr Met Ser Met Leu Val Leu Leu Pro Asp
325 330 335
Glu Val Ser Gly Leu Glu Gln Leu Glu Ser Ile Ile Asn Phe Glu Lys
340 345 350
Leu Thr Glu Trp Thr Ser Ser Asn Val Met Glu Glu Arg Lys Ile Lys
355 360 365
Val Tyr Leu Pro Arg Met Lys Met Glu Glu Lys Tyr Asn Leu Thr Ser
370 375 380
Val Leu Met Ala Met Gly Ile Thr Asp Val Phe Ser Ser Ser Ala Asn
385 390 395 400
Leu Ser Gly Ile Ser Ser Ala Glu Ser Leu Lys Ile Ser Gln Ala Val
405 410 415
His Ala Ala His Ala Glu Ile Asn Glu Ala Gly Arg Glu Val Val Gly
420 425 430
Ser Ala Glu Ala Gly Val Asp Ala Ala Ser Val Ser Glu Glu Phe Arg
435 440 445
Ala Asp His Pro Phe Leu Phe Cys Ile Lys His Ile Ala Thr Asn Ala
450 455 460
Val Leu Phe Phe Gly Arg Cys Val Ser Pro
465 470
<210> 17
<211> 1885
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 17
agtgaaaacg aaaagtgaaa atatcctgag gacgactttt attcttttgg ctggtgctag 60
cgctgcatgt tcgttactag ccgttcaata cccattttct aaagttcagt caatacattt 120
agcaaggttg gaagcgttgg atattttcaa cgagaactcc tgggataaga aaagtaaatt 180
ccgtctatat taccgatcat acttagatac attccaccag ttggtgagct tacatgagaa 240
gtctaaacta tcttggaccc gctggtttta taaagggttc gttaggaatg cgttaactac 300
cattccagca acatccgtgg ggcttctggt gtttgaaata ctgcgtcaaa aattgagcga 360
tgaaattgaa gatcgattca gttgaatcgc ccgaaacaat tgatcccctg tacatacttg 420
taatttacct cagaatattt tggtaagctt cccacccagc ttttctatac cgttcacctt 480
cttttaaggg atctctgccc ttgccaaaca aaccacgacc tacgattatg atgtcagtgc 540
cagtggaaaa tacttgactc actgttcgat attgttggcc tagagcatca ccagtgtcat 600
ccaaaccaac acctggtgtc ataataatcc aatcgaaccc ttcatcttgt cctcccatag 660
aattttgagc aataaaccca atgacgaatt ccttgtctga ttttgcaatt tctacagttt 720
cttcggtgta cttaccatgg gcaattgatc cctttgacga cagttcagcc aacatcaata 780
gtccccttgg ttgatctgtt gtctcagtgg ctgcctcctt tagacccttt acaattccac 840
taccaatgac accatgagca tttgtaatat ctgcccattg tgcaatcttg tagacacctc 900
cttgatattg atgcttgaca gtgttgccta tatcagcaaa ctttctgtcc tcaaaaatta 960
aaaacttgtg tttctttgat agttccaata aaggcagaat agttccatca tacgtgaagt 1020
catcaattat gtcgatatga gtcttggcca aacagataaa tgggcccaat ttatctagaa 1080
gctccaataa ttctttagtt gttctcacgt cgactgatgc gcataggtta ctctgtttct 1140
gttccataag cgcaaacagt cgtcgtgcca caggtgattg atgagtattt gctctctcgg 1200
cataactgcg agccattgtc taggtatcta tccctttgat caggttgatg ttaactcatt 1260
agagtggatc aatgcgaagg ataggtgcga cgtgtaccgt ccaaaaaact tttttcttca 1320
atcttgacaa aaactggtaa cagagagagc aagtgctaac tctaccccaa ccaagtacat 1380
cacaaaatgg acgcattgaa cgctaaagaa caacaagagt tccagaaact cgttgaacaa 1440
aaacaaatga aagacttcat gcgtctttac tccgatttgg ttagcaaatg ttttacagac 1500
tgtgtcaatg attttacatc taacaagttg acttctaagg aggaaggctg catcaacaag 1560
tgtgcagaaa agttcctcaa gcacagtgag agagttggtc aacgtttcca agaacaaaac 1620
caacttatga tgcaacagct aagacgttaa ccccatattt ttgtacataa agttcattgt 1680
ccaggactaa tccagacttt ctctgaacag ctctataatc ttagtagttt cttccatcat 1740
ttcaatcgtt agcttcgaaa catcactgtc ttcatcgtta tagatgatgg catttgtaaa 1800
catgatctgt agaactttag tcaattcgtc aaaggtggtt atctccccat ttctgcagtg 1860
cttgagaatg gtcttcagat cttga 1885
<210> 18
<211> 375
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 18
atggctaaac tcacctctgc tgttccagtc ctgactgctc gtgatgttgc tggtgctgtt 60
gagttctgga ctgatagact cggtttctcc cgtgacttcg tagaggacga ctttgccggt 120
gttgtacgtg acgacgttac cctgttcatc tccgcagttc aggaccaggt tgtgccagac 180
aacactctgg catgggtatg ggttcgtggt ctggacgaac tgtacgctga gtggtctgag 240
gtcgtgtcta ccaacttccg tgatgcatct ggtccagcta tgaccgagat cggtgaacag 300
ccctggggtc gtgagtttgc actgcgtgat ccagctggta actgcgtgca tttcgtcgca 360
gaagagcagg actaa 375
<210> 19
<211> 810
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 19
atgggtaaag agaaaacgca cgtcagtcgt ccaagattga actccaatat ggatgcagac 60
ctgtacggtt acaaatgggc tagagataac gttggacaat ctggtgcaac tatatataga 120
ttgtatggga agccagacgc accagagttg tttctaaagc atgggaaagg ctctgttgct 180
aatgatgtga ctgatgaaat ggtacgtttg aattggctaa cagagtttat gcccttgcct 240
actattaagc attttattcg tactcccgat gacgcttggt tgctaaccac cgcaattcct 300
ggtaaaactg cctttcaagt tctggaagaa tacccagatt ccggtgaaaa catcgttgac 360
gccttggctg ttttcctgcg aagacttcac tctattcccg tatgtaattg tccctttaat 420
tcagacagag tttttagatt ggctcaggct caatctagga tgaataatgg tttggttgat 480
gcaagtgact tcgatgacga aagaaacggt tggcctgtcg agcaggtgtg gaaggaaatg 540
cataagttac ttccattttc tcctgattct gttgtaaccc acggtgattt ttccctagac 600
aaccttatat tcgatgaggg caagttgatt ggttgtattg acgtcggcag agtgggtatc 660
gccgataggt atcaagattt agcaatactg tggaattgtc taggagaatt ttcacccagt 720
ctgcaaaaga gattgttcca gaaatacgga attgacaacc ccgatatgaa taagttgcag 780
tttcatttga tgttggacga gttcttctaa 810
<210> 20
<211> 1029
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 20
atgggaaaga aaccagagct gaccgcaacg agtgtcgaaa aatttcttat tgaaaaattt 60
gatagtgtgt ccgatttaat gcagcttagt gaaggcgaag agtcacgtgc tttctcattc 120
gacgttggtg gacgtggcta cgttttgaga gttaatagtt gtgcagatgg cttttataag 180
gatcgttatg tataccgtca ttttgctagt gcagccctgc caatcccaga ggttttagat 240
ataggtgagt ttagtgagtc tcttacttat tgtattagtc gtagagccca aggtgttacc 300
cttcaggatt tgccagagac tgagcttcct gctgtattgc aacctgtcgc tgaggctatg 360
gacgccattg ccgcagcaga tttatctcaa acgtcaggtt tcggcccctt cggcccacaa 420
ggcatcggac agtacacaac gtggcgtgac tttatctgtg ccatcgctga ccctcatgtc 480
taccactggc aaacggtcat ggatgacacg gtgtccgcct ctgtggccca agcattggat 540
gaactgatgc tttgggctga ggattgtccc gaagtccgtc acctggttca cgctgacttc 600
ggctccaaca atgttttgac cgacaatggc cgtatcaccg ctgtcatcga ctggtctgag 660
gcaatgtttg gcgactctca gtatgaagtc gccaatatat ttttttggag accctggttg 720
gcatgcatgg aacagcaaac tcgttacttt gaaagacgtc atccagagtt agctggtagt 780
ccacgtctgc gtgcttacat gttgcgtatc ggcttagacc aactgtatca gtcacttgtc 840
gatggtaact ttgatgacgc agcatgggca caaggacgtt gtgacgctat tgtacgttca 900
ggtgcaggca cggtcggccg tacacaaatt gcacgtagaa gtgcagcagt ctggaccgat 960
ggttgtgttg aggtccttgc agattcagga aatagacgtc catctactcg tcctcgtgct 1020
aaggaataa 1029
<210> 21
<211> 25
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 21
ggaattgtga gcggataaca attcc 25
<210> 22
<211> 1032
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 22
atggccaatt tactgaccgt acaccaaaat ttgcctgcat taccggtcga tgcaacgagt 60
gatgaggttc gcaagaacct gatggacatg ttcagggatc gccaggcgtt ttctgagcat 120
acctggaaaa tgcttctgtc cgtttgccgg tcgtgggcgg catggtgcaa gttgaataac 180
cggaaatggt ttcccgcaga acctgaagat gttcgcgatt atcttctata tcttcaggcg 240
cgcggtctgg cagtaaaaac tatccagcaa catttgggcc agctaaacat gcttcatcgt 300
cggtccgggc tgccacgacc aagtgacagc aatgctgttt cactggttat gcggcgcatc 360
cgaaaagaaa acgttgatgc cggtgaacgt gcaaaacagg ctctagcgtt cgaacgcact 420
gatttcgacc aggttcgttc actcatggaa aatagcgatc gctgccagga tatacgtaat 480
ctggcatttc tggggattgc ttataacacc ctgttacgta tagccgaaat tgccaggatc 540
agggttaaag atatctcacg tactgacggt gggagaatgt taatccatat tggcagaacg 600
aaaacgctgg ttagcaccgc aggtgtagag aaggcactta gcctgggggt aactaaactg 660
gtcgagcgat ggatttccgt ctctggtgta gctgatgatc cgaataacta cctgttttgc 720
cgggtcagaa aaaatggtgt tgccgcgcca tctgccacca gccagctatc aactcgcgcc 780
ctggaaggga tttttgaagc aactcatcga ttgatttacg gcgctaagga tgactctggt 840
cagagatacc tggcctggtc tggacacagt gcccgtgtcg gagccgcgcg agatatggcc 900
cgcgctggag tttcaatacc ggagatcatg caagctggtg gctggaccaa tgtaaatatt 960
gtcatgaact atatccgtaa cctggatagt gaaacagggg caatggtgcg cctgctggaa 1020
gatggcgatt aa 1032
<210> 23
<211> 34
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 23
ataacttcgt ataatgtatg ctatacgaac ggta 34
<210> 24
<211> 34
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 24
taccgttcgt ataatgtatg ctatacgaag ttat 34
<210> 25
<211> 673
<212> DNA
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 25
cccgtagaaa agatcaaagg atcttcttga gatccttttt ttctgcgcgt aatctgctgc 60
ttgcaaacaa aaaaaccacc gctaccagcg gtggtttgtt tgccggatca agagctacca 120
actctttttc cgaaggtaac tggcttcagc agagcgcaga taccaaatac tgttcttcta 180
gtgtagccgt agttaggcca ccacttcaag aactctgtag caccgcctac atacctcgct 240
ctgctaatcc tgttaccagt ggctgctgcc agtggcgata agtcgtgtct taccgggttg 300
gactcaagac gatagttacc ggataaggcg cagcggtcgg gctgaacggg gggttcgtgc 360
acacagccca gcttggagcg aacgacctac accgaactga gatacctaca gcgtgagcta 420
tgagaaagcg ccacgcttcc cgaagggaga aaggcggaca ggtatccggt aagcggcagg 480
gtcggaacag gagagcgcac gagggagctt ccagggggaa acgcctggta tctttatagt 540
cctgtcgggt ttcgccacct ctgacttgag cgtcgatttt tgtgatgctc gtcagggggg 600
cggagcctat ggaaaaacgc cagcaacgcg gcctttttac ggttcctggc cttttgctgg 660
ccttttgctc aca 673
<210> 26
<211> 1106
<212> PRT
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 26
Met Asp Arg Glu Gln Gly Ile Leu Pro Gln Asp Pro Phe Ser Asn Ser
1 5 10 15
Val His Val Pro Lys Leu Arg Ala Ser Ser Gly Gly Gln Pro Gln Lys
20 25 30
Pro Val Ile Gln Asn Ser Ala Pro Ala Thr Ala Arg Met Leu Arg Asn
35 40 45
Ala Ser Ser Ser Thr Ser Ala Ala Leu Leu Lys Glu Leu Asn Thr His
50 55 60
Glu His Ser Gln Arg Gln His Thr Pro Gln Lys Gln Pro Ser Leu Asp
65 70 75 80
Ala Pro Ala Ala Leu Val Pro Val Glu Ser Ala Thr Lys Gln Phe His
85 90 95
Arg Thr Ser Ile Gly Asp Trp Glu Phe Ser Asn Thr Ile Gly Ala Gly
100 105 110
Ser Met Gly Lys Val Lys Val Ala Lys His Arg Val Thr His Glu Val
115 120 125
Cys Ala Ile Lys Ile Val Ile Arg Ser Ala Lys Ile Trp Gln Arg Asn
130 135 140
His Gln Asn Asp Pro Glu Pro Glu Thr Glu Glu Lys Arg Lys Lys Leu
145 150 155 160
Arg Asp Glu Tyr Lys Lys Glu Leu Glu Arg Asp Glu Arg Thr Val Arg
165 170 175
Glu Ala Ala Leu Gly Lys Ile Met Tyr His Pro Asn Ile Cys Arg Leu
180 185 190
Phe Glu Cys Tyr Thr Met Ser Asn His Tyr Tyr Met Leu Phe Glu Ile
195 200 205
Val Gln Gly Val Gln Leu Leu Asp Tyr Ile Val Ser His Gly Lys Leu
210 215 220
Lys Glu Thr Arg Val Arg Gln Phe Ala Arg Ser Ile Ala Ser Ala Leu
225 230 235 240
Asp Tyr Cys His Ser Asn Asn Ile Val His Arg Asp Leu Lys Ile Glu
245 250 255
Asn Ile Met Ile Asn Asn Lys Gly Glu Ile Lys Leu Ile Asp Phe Gly
260 265 270
Leu Ser Asn Met Tyr Asp Arg Arg Asn Leu Leu Lys Thr Phe Cys Gly
275 280 285
Ser Leu Tyr Phe Ala Ala Pro Glu Leu Leu Ser Cys Arg Pro Tyr Ile
290 295 300
Gly Pro Glu Ile Asp Val Trp Ser Phe Gly Val Val Leu Phe Val Leu
305 310 315 320
Val Ser Gly Lys Val Pro Phe Asp Asp Asp Ser Val Pro Lys Leu His
325 330 335
Ala Lys Ile Lys Arg Gly Lys Val Glu Tyr Pro Glu Phe Ile Ser Pro
340 345 350
Leu Cys His Ser Leu Leu Ser Gln Met Leu Val Val Asn Pro Asp His
355 360 365
Arg Val Thr Leu Lys Ala Ala Met Glu His Pro Trp Met Thr Leu Gly
370 375 380
Phe Ala Gly Pro Pro Ser Asn Tyr Leu Pro Gln Arg Ser Pro Ile Val
385 390 395 400
Leu Pro Leu Asp Leu Ser Val Val Arg Glu Ile Ala Asn Leu Gly Leu
405 410 415
Gly Asn Glu Glu Gln Ile Ala Arg Asp Ile Thr Asn Leu Ile Ser Ser
420 425 430
Arg Glu Tyr Glu Ala Cys Val Glu Arg Trp Lys Leu Asp Gln Gln Lys
435 440 445
Ala Asn Ile Lys Gly Tyr Ser Ala Arg Asp Asp Ser Ala Ile Ile Ala
450 455 460
Phe His Pro Leu Leu Ser Thr Tyr Tyr Leu Val Asp Glu Met Arg Lys
465 470 475 480
Arg Lys Leu Ala Lys Gly Ala Leu Lys Gly Gln Thr Ser Val Leu Asp
485 490 495
Thr Val Lys Val Ser Pro Asp Ile Pro Lys Thr Pro Ala Ile Pro Gln
500 505 510
Lys Leu Glu Thr Thr Asp Val Glu Gln Pro Leu Leu Ala Thr Val Pro
515 520 525
Pro Ala Tyr Thr Ser Pro His Gly Gln Pro Ala Glu Leu Glu Ala Met
530 535 540
Ile Glu Pro Ala Gln Pro Leu Ser Ser Ala His Pro Phe Glu Met Asp
545 550 555 560
Met Thr Gln Gln Gln His Ala Ser Arg Lys Thr His Ile Lys His Ala
565 570 575
Pro Glu Arg Gln Asp Arg Gly Gly Tyr Asn Val His Lys Asn Asn Ser
580 585 590
Gly Gly Leu Asn Ser Leu Phe Arg Arg Leu Ser Gly Lys Arg Pro His
595 600 605
Lys Asn Glu Ala Glu Trp Glu Pro Ser Ser Pro Pro Pro Gln Val His
610 615 620
Pro Phe Ser Val Asn Asp Ala Asp Arg Thr Ser Val Arg Gly Val Ser
625 630 635 640
Pro Ile Thr Gln Pro Ala Ala Val Lys Asn Val Thr Ser Asn Asn Ser
645 650 655
Lys Asn Tyr Leu Asp Pro Val Asp Asp Ser Lys Leu Val Arg Arg Val
660 665 670
Gly Ser Leu Arg Ile Thr Asn Lys Glu Lys Gln Gln Val Thr Ser Asp
675 680 685
Phe Pro Arg Leu Pro Asn Phe Thr Ile Pro Glu Gln Pro Pro Lys Asn
690 695 700
Ala Pro Ile Pro Ile His Ala Gln Pro Thr Thr Thr Gly Thr Thr Phe
705 710 715 720
Gln Ser Asn Asp His Glu Ile Lys Lys Lys Leu Gln Ala Ser Thr Ser
725 730 735
Pro Asn Glu Gln Arg Gly Pro Pro Thr Leu Ala Pro Ser Gln Gln Arg
740 745 750
Arg Leu His Pro Thr Ala Arg Ala Lys Ser Leu Gly His Ser Arg Lys
755 760 765
Gln Ser Leu Asn Phe Lys Phe Gly Gly Pro Ala Asn Asn Gln Leu Pro
770 775 780
Ala Leu Pro Thr Lys Glu Asn Tyr Asp Val Phe Glu Asp Ala Gln Ile
785 790 795 800
Thr Asp Asn Asn Leu Leu Asn Pro Glu Gly Lys Tyr Ser Ala Asn Thr
805 810 815
Asn Val His Ile Lys Pro Met Thr Glu Ser Gln Ile Leu Phe Glu Ala
820 825 830
Glu His Ala Pro Pro Gly Thr Met Pro Ser Val Glu Tyr Pro Arg Thr
835 840 845
Leu Phe Leu Lys Gly Phe Phe Ser Val Gln Thr Thr Ser Ser Lys Pro
850 855 860
Leu Pro Val Ile Arg Tyr Asn Ile Ile Ala Ala Leu Cys Lys Leu Asn
865 870 875 880
Ile Gln Phe Thr Glu Val Asn Gly Gly Phe Val Cys Val Tyr Arg Lys
885 890 895
Thr Glu Asn Leu Gln Ile Gly Asp Ile Arg Ser Pro Val Ile Glu Ser
900 905 910
Arg Val Thr Asp Asp Thr Asp Ser Asp Val Ala Asn Ser Ser Lys Leu
915 920 925
Ser Ser Ser Ser Thr Ala Asn Thr Arg Val Asn Val Ile Glu Asp Asp
930 935 940
Ser Ser Ser Pro Ser Ser Ala Arg Leu Lys His Arg Arg Lys Phe Ser
945 950 955 960
Leu Gly Asn Gly Ile Leu Asn His Ile Arg Lys Pro Thr Leu Asp Gly
965 970 975
Thr Glu Phe Asp Asp Tyr Asp Ala Thr Val Asn Thr Pro Val Thr Pro
980 985 990
Ala Pro Ala Asn Val His Ser Arg Ser Ser Ser Tyr His Thr Glu Ser
995 1000 1005
Asp Asn Glu Ser Met Glu Ser Leu His Asp Ile Arg Gly Gly Ser
1010 1015 1020
Asp Met Ile Leu Lys Asn Val Pro Glu Arg Asn Ala Arg Gln Ile
1025 1030 1035
Asp Thr Val Lys Glu Glu Glu Thr Asp Asp Asp Asp Leu Gly Ser
1040 1045 1050
Ile Asn Glu Gly Ser Thr His Arg Thr Pro Leu Lys Phe Glu Ile
1055 1060 1065
His Ile Val Lys Val Pro Leu Val Gly Leu Tyr Gly Val Arg Phe
1070 1075 1080
Lys Lys Ile Leu Gly Asn Ala Trp Ile Tyr Lys Arg Leu Ala Ser
1085 1090 1095
Lys Leu Leu Gln Glu Leu Asn Leu
1100 1105
<210> 27
<211> 442
<212> PRT
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 27
Met Gly Lys Leu Ala Gln Leu Val Leu His Pro Leu Glu Leu Arg Ala
1 5 10 15
Ala Ile Gln Phe Lys Phe Phe Lys Gln Ser Leu His Pro Arg Gln Pro
20 25 30
Thr Asn Glu Arg Glu Thr Leu Lys His Cys Tyr Glu Leu Leu Ala Leu
35 40 45
Thr Ser Arg Ser Phe Cys Thr Val Ile Leu Glu Leu Asn Pro Glu Leu
50 55 60
Arg Asn Ala Ile Met Ile Phe Tyr Leu Val Leu Arg Ala Leu Asp Thr
65 70 75 80
Val Glu Asp Asp Met Thr Ile Lys Pro Asp Ile Lys Ile Pro Leu Leu
85 90 95
Arg Ser Phe Asp Glu Lys Leu Asn Leu Lys Ser Trp Ser Phe Asp Gly
100 105 110
Asn Ser Pro Asp Glu Lys Asp Arg Gln Val Leu Val Asp Phe Thr Asp
115 120 125
Val Leu Glu Glu Tyr His Arg Leu Lys Pro Val Tyr Gln Asp Val Ile
130 135 140
Lys Asp Ile Thr His Lys Met Gly Asn Gly Met Ala Asp Tyr Ile Thr
145 150 155 160
Asp Glu Glu Phe Asn Leu Asn Gly Val Ala Thr Val Lys Asp Tyr Asp
165 170 175
Leu Tyr Cys His Tyr Val Ala Gly Leu Val Gly Glu Gly Leu Thr His
180 185 190
Leu Ile Val Glu Ala Gly Phe Gly Asp Pro Lys Leu Glu Asp Asn Met
195 200 205
Gln Leu Ser Glu Ser Met Gly Leu Phe Leu Gln Lys Thr Asn Ile Ile
210 215 220
Arg Asp Tyr Arg Glu Asp Leu Asp Asp Gly Arg Ser Phe Trp Pro Lys
225 230 235 240
Glu Ile Trp Ser Lys Tyr Ala Asp Ser Leu Ser Asp Phe Ser Lys Arg
245 250 255
Glu Asn Tyr Glu Lys Gly Leu Asp Cys Ile Ser Glu Leu Val Leu Asn
260 265 270
Thr Met Asp His Ile Lys Asp Val Leu Val Tyr Leu Ser Ser Val Tyr
275 280 285
Asp Phe Ser Ser Tyr Asn Phe Cys Val Ile Pro Gln Val Met Ala Ile
290 295 300
Ala Thr Leu Ala Thr Val Phe Arg Asn Glu Lys Val Phe Glu Thr Asn
305 310 315 320
Val Lys Ile Arg Lys Gly Thr Thr Cys Tyr Leu Ile Leu Lys Ala Arg
325 330 335
Thr Phe Glu Gly Ala Cys Glu Ile Phe Ser Tyr Tyr Leu Arg Gln Ile
340 345 350
His His Ser Cys Pro Ile Thr Asp Ala Asn Tyr Ile Lys Ile Gly Ile
355 360 365
Lys Cys Gly Glu Leu Glu Gln Phe Leu Glu Ser Leu Asn Pro Ala Pro
370 375 380
His Val Pro Pro Gly Ala Thr Ile Pro Gln Thr Pro His Phe Val Lys
385 390 395 400
Ala Glu Arg Lys Arg Lys Leu Asp Arg Glu Leu Val Pro Thr Leu Ala
405 410 415
Ile Glu Ser Leu Lys Cys Asp Val Phe Leu Ser Leu Val Ala Leu Gly
420 425 430
Phe Leu Gly Val Ile Tyr Ser Ile Ser Ser
435 440
<210> 28
<211> 517
<212> PRT
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 28
Met Gln Phe Asn Trp Asp Ile Lys Thr Val Ala Ser Ile Leu Ser Ala
1 5 10 15
Leu Thr Leu Ala Gln Ala Ser Asp Gln Glu Ala Ile Ala Pro Glu Asp
20 25 30
Ser His Val Val Lys Leu Thr Glu Ala Thr Phe Glu Ser Phe Ile Thr
35 40 45
Ser Asn Pro His Val Leu Ala Glu Phe Phe Ala Pro Trp Cys Gly His
50 55 60
Cys Lys Lys Leu Gly Pro Glu Leu Val Ser Ala Ala Glu Ile Leu Lys
65 70 75 80
Asp Asn Glu Gln Val Lys Ile Ala Gln Ile Asp Cys Thr Glu Glu Lys
85 90 95
Glu Leu Cys Gln Gly Tyr Glu Ile Lys Gly Tyr Pro Thr Leu Lys Val
100 105 110
Phe His Gly Glu Val Glu Val Pro Ser Asp Tyr Gln Gly Gln Arg Gln
115 120 125
Ser Gln Ser Ile Val Ser Tyr Met Leu Lys Gln Ser Leu Pro Pro Val
130 135 140
Ser Glu Ile Asn Ala Thr Lys Asp Leu Asp Asp Thr Ile Ala Glu Ala
145 150 155 160
Lys Glu Pro Val Ile Val Gln Val Leu Pro Glu Asp Ala Ser Asn Leu
165 170 175
Glu Ser Asn Thr Thr Phe Tyr Gly Val Ala Gly Thr Leu Arg Glu Lys
180 185 190
Phe Thr Phe Val Ser Thr Lys Ser Thr Asp Tyr Ala Lys Lys Tyr Thr
195 200 205
Ser Asp Ser Thr Pro Ala Tyr Leu Leu Val Arg Pro Gly Glu Glu Pro
210 215 220
Ser Val Tyr Ser Gly Glu Glu Leu Asp Glu Thr His Leu Val His Trp
225 230 235 240
Ile Asp Ile Glu Ser Lys Pro Leu Phe Gly Asp Ile Asp Gly Ser Thr
245 250 255
Phe Lys Ser Tyr Ala Glu Ala Asn Ile Pro Leu Ala Tyr Tyr Phe Tyr
260 265 270
Glu Asn Glu Glu Gln Arg Ala Ala Ala Ala Asp Ile Ile Lys Pro Phe
275 280 285
Ala Lys Glu Gln Arg Gly Lys Ile Asn Phe Val Gly Leu Asp Ala Val
290 295 300
Lys Phe Gly Lys His Ala Lys Asn Leu Asn Met Asp Glu Glu Lys Leu
305 310 315 320
Pro Leu Phe Val Ile His Asp Leu Val Ser Asn Lys Lys Phe Gly Val
325 330 335
Pro Gln Asp Gln Glu Leu Thr Asn Lys Asp Val Thr Glu Leu Ile Glu
340 345 350
Lys Phe Ile Ala Gly Glu Ala Glu Pro Ile Val Lys Ser Glu Pro Ile
355 360 365
Pro Glu Ile Gln Glu Glu Lys Val Phe Lys Leu Val Gly Lys Ala His
370 375 380
Asp Glu Val Val Phe Asp Glu Ser Lys Asp Val Leu Val Lys Tyr Tyr
385 390 395 400
Ala Pro Trp Cys Gly His Cys Lys Arg Met Ala Pro Ala Tyr Glu Glu
405 410 415
Leu Ala Thr Leu Tyr Ala Asn Asp Glu Asp Ala Ser Ser Lys Val Val
420 425 430
Ile Ala Lys Leu Asp His Thr Leu Asn Asp Val Asp Asn Val Asp Ile
435 440 445
Gln Gly Tyr Pro Thr Leu Ile Leu Tyr Pro Ala Gly Asp Lys Ser Asn
450 455 460
Pro Gln Leu Tyr Asp Gly Ser Arg Asp Leu Glu Ser Leu Ala Glu Phe
465 470 475 480
Val Lys Glu Arg Gly Thr His Lys Val Asp Ala Leu Ala Leu Arg Pro
485 490 495
Val Glu Glu Glu Lys Glu Ala Glu Glu Glu Ala Glu Ser Glu Ala Asp
500 505 510
Ala His Asp Glu Leu
515
<210> 29
<211> 645
<212> PRT
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 29
Met Pro Ala Val Gly Ile Asp Leu Gly Thr Thr Tyr Ser Cys Val Ala
1 5 10 15
His Phe Ala Asn Asp Arg Val Glu Ile Ile Ala Asn Asp Gln Gly Asn
20 25 30
Arg Thr Thr Pro Ser Phe Val Ala Phe Thr Asp Thr Glu Arg Leu Ile
35 40 45
Gly Asp Ala Ala Lys Asn Gln Ala Ala Met Asn Pro Ala Asn Thr Val
50 55 60
Phe Asp Ala Lys Arg Leu Ile Gly Arg Lys Phe Ser Asp Ala Glu Thr
65 70 75 80
Gln Ala Asp Ile Lys His Phe Pro Phe Lys Val Val Asp Lys Gly Gly
85 90 95
Lys Pro Asn Ile Gln Val Glu Phe Lys Gly Glu Thr Lys Val Phe Thr
100 105 110
Pro Glu Glu Ile Ser Ser Met Val Leu Thr Lys Met Lys Asp Thr Ala
115 120 125
Glu Gln Phe Leu Gly Asp Lys Val Asn Asp Ala Val Val Thr Val Pro
130 135 140
Ala Tyr Phe Asn Asp Ser Gln Arg Gln Ala Thr Lys Asp Ala Gly Leu
145 150 155 160
Ile Ala Gly Leu Asn Val Met Arg Ile Ile Asn Glu Pro Thr Ala Ala
165 170 175
Ala Ile Ala Tyr Gly Leu Asp Lys Lys Ala Glu Gly Glu Lys Asn Val
180 185 190
Leu Ile Phe Asp Leu Gly Gly Gly Thr Phe Asp Val Ser Leu Leu Ser
195 200 205
Ile Glu Asp Gly Ile Phe Glu Val Lys Ala Thr Ala Gly Asp Thr His
210 215 220
Leu Gly Gly Glu Asp Phe Asp Asn Arg Leu Val Asn His Phe Ile Ala
225 230 235 240
Glu Phe Lys Arg Lys Asn Lys Lys Asp Leu Ser Ser Asn Gln Arg Ala
245 250 255
Leu Arg Arg Leu Arg Thr Ala Cys Glu Arg Ala Lys Arg Thr Leu Ser
260 265 270
Ser Ser Ala Gln Thr Ser Ile Glu Ile Asp Ser Leu Phe Glu Gly Val
275 280 285
Asp Phe Tyr Thr Ser Leu Thr Arg Ala Arg Phe Glu Glu Leu Cys Gly
290 295 300
Asp Leu Phe Arg Ser Thr Ile Glu Pro Val Glu Lys Val Leu Lys Asp
305 310 315 320
Ala Lys Leu Asp Lys Ser Gln Val Asn Glu Ile Val Leu Val Gly Gly
325 330 335
Ser Thr Arg Ile Pro Lys Val Gln Lys Leu Val Ser Asp Phe Phe Asn
340 345 350
Gly Lys Glu Pro Asn Arg Ser Ile Asn Pro Asp Glu Ala Val Ala Tyr
355 360 365
Gly Ala Ala Val Gln Ala Ala Ile Leu Ser Gly Asp Thr Ser Ser Lys
370 375 380
Thr Gln Asp Leu Leu Leu Leu Asp Val Ala Pro Leu Ser Leu Gly Ile
385 390 395 400
Glu Thr Ala Gly Gly Ile Met Thr Lys Leu Ile Pro Arg Asn Ser Thr
405 410 415
Ile Pro Thr Lys Lys Ser Glu Thr Phe Ser Thr Tyr Ala Asp Asn Gln
420 425 430
Pro Gly Val Leu Ile Gln Val Tyr Glu Gly Glu Arg Ala Lys Thr Ala
435 440 445
Asp Asn Asn Leu Leu Gly Lys Phe Glu Leu Ser Gly Ile Pro Pro Ala
450 455 460
Pro Arg Gly Val Pro Gln Ile Glu Val Thr Phe Asp Met Asp Ala Asn
465 470 475 480
Gly Ile Leu Asn Val Ser Ala Val Glu Lys Gly Thr Gly Lys Ala Gln
485 490 495
Gln Ile Thr Ile Thr Asn Asp Lys Gly Arg Leu Ser Lys Glu Asp Ile
500 505 510
Glu Ala Met Ile Ser Glu Ala Glu Lys Tyr Lys Asp Glu Asp Glu Lys
515 520 525
Glu Ala Ala Arg Ile Gln Ala Arg Asn Ala Leu Glu Ser Tyr Ser Phe
530 535 540
Ser Leu Lys Asn Thr Leu Asn Glu Lys Glu Val Gly Glu Lys Leu Asp
545 550 555 560
Ala Ala Asp Lys Glu Ser Leu Thr Lys Ala Ile Asp Glu Thr Thr Ser
565 570 575
Trp Ile Asp Glu Asn Gln Thr Ala Thr Thr Glu Glu Phe Glu Ala Lys
580 585 590
Gln Lys Glu Leu Glu Gly Val Ala Asn Pro Ile Met Thr Lys Phe Tyr
595 600 605
Gln Ala Asn Gly Gly Ala Pro Gly Gly Ala Ala Pro Gly Gly Phe Pro
610 615 620
Gly Ala Ala Gly Ala Gly Ala Glu Ala Pro Gly Ala Asp Gly Pro Thr
625 630 635 640
Val Glu Glu Val Asp
645
<210> 30
<211> 657
<212> PRT
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 30
Met Gly Lys Ser Ile Gly Ile Asp Leu Gly Thr Thr Tyr Ser Cys Val
1 5 10 15
Ala His Phe Ala Asn Asp Arg Val Glu Ile Ile Ala Asn Asp Gln Gly
20 25 30
Asn Arg Thr Thr Pro Ser Phe Val Ala Phe Thr Asp Thr Glu Arg Leu
35 40 45
Ile Gly Asp Ala Ala Lys Asn Gln Ala Ala Met Asn Pro Ala Asn Thr
50 55 60
Val Phe Asp Ala Lys Arg Leu Ile Gly Arg Lys Phe Asp Asp Pro Glu
65 70 75 80
Thr Gln Ala Asp Ile Lys His Phe Pro Phe Lys Val Ile Asn Lys Gly
85 90 95
Gly Lys Pro Asn Ile Gln Val Glu Phe Lys Gly Glu Thr Lys Val Phe
100 105 110
Ser Pro Glu Glu Ile Ser Ser Met Val Leu Thr Lys Met Lys Asp Thr
115 120 125
Ala Glu Gln Tyr Leu Gly Glu Lys Ile Asn Asp Ala Val Val Thr Val
130 135 140
Pro Ala Tyr Phe Asn Asp Ser Gln Arg Gln Ala Thr Lys Asp Ala Gly
145 150 155 160
Leu Ile Ala Gly Leu Asn Val Gln Arg Ile Ile Asn Glu Pro Thr Ala
165 170 175
Ala Ala Ile Ala Tyr Gly Leu Asp Lys Lys Asp Ala Gly His Gly Glu
180 185 190
His Asn Ile Leu Ile Phe Asp Leu Gly Gly Gly Thr Phe Asp Val Ser
195 200 205
Leu Leu Ser Ile Asp Glu Gly Ile Phe Glu Val Lys Ala Thr Ala Gly
210 215 220
Asp Thr His Leu Gly Gly Glu Asp Phe Asp Asn Arg Leu Val Asn His
225 230 235 240
Phe Ile Ala Glu Phe Lys Arg Lys Thr Lys Lys Asp Leu Ser Thr Asn
245 250 255
Gln Arg Ser Leu Arg Arg Leu Arg Thr Ala Cys Glu Arg Ala Lys Arg
260 265 270
Thr Leu Ser Ser Ser Ala Gln Thr Ser Ile Glu Ile Asp Ser Leu Phe
275 280 285
Glu Gly Ile Asp Phe Tyr Thr Ser Ile Thr Arg Ala Arg Phe Glu Glu
290 295 300
Leu Cys Ala Asp Leu Phe Arg Ser Thr Ile Glu Pro Val Glu Arg Val
305 310 315 320
Leu Lys Asp Ser Lys Leu Asp Lys Ser Gln Val His Glu Ile Val Leu
325 330 335
Val Gly Gly Ser Thr Arg Ile Pro Lys Val Gln Lys Leu Val Ser Asp
340 345 350
Phe Phe Asn Gly Lys Glu Pro Asn Lys Ser Ile Asn Pro Asp Glu Ala
355 360 365
Val Ala Tyr Gly Ala Ala Val Gln Ala Ala Ile Leu Ser Gly Asp Thr
370 375 380
Ser Ser Lys Thr Gln Asp Leu Leu Leu Leu Asp Val Ala Pro Leu Ser
385 390 395 400
Leu Gly Ile Glu Thr Ala Gly Gly Ile Met Thr Lys Leu Ile Pro Arg
405 410 415
Asn Ser Thr Ile Pro Ala Lys Lys Ser Glu Ile Phe Ser Thr Tyr Ala
420 425 430
Asp Asn Gln Pro Gly Val Leu Ile Gln Val Phe Glu Gly Glu Arg Thr
435 440 445
Arg Thr Lys Asp Asn Asn Leu Leu Gly Lys Phe Glu Leu Ser Gly Ile
450 455 460
Pro Pro Ala Pro Arg Gly Val Pro Gln Ile Glu Val Thr Phe Asp Met
465 470 475 480
Asp Ala Asn Gly Ile Leu Asn Val Ser Ala Val Glu Lys Gly Thr Gly
485 490 495
Lys Thr Gln Lys Ile Thr Ile Thr Asn Asp Lys Gly Arg Leu Ser Lys
500 505 510
Glu Asp Ile Glu Arg Met Val Ser Glu Ala Glu Lys Phe Lys Asp Glu
515 520 525
Asp Glu Lys Glu Ala Glu Arg Val Ala Ala Lys Asn Gly Leu Glu Ser
530 535 540
Tyr Ala Tyr Ser Leu Lys Asn Ser Ala Ala Glu Ser Gly Phe Lys Asp
545 550 555 560
Lys Val Gly Glu Asp Asp Leu Ala Lys Leu Asn Lys Ser Val Glu Glu
565 570 575
Thr Ile Ser Trp Leu Asp Glu Ser Gln Ser Ala Ser Thr Asp Glu Tyr
580 585 590
Lys Asp Arg Gln Lys Glu Leu Glu Glu Val Ala Asn Pro Ile Met Ser
595 600 605
Lys Phe Tyr Gly Ala Ala Gly Gly Ala Pro Gly Gly Ala Pro Gly Gly
610 615 620
Phe Pro Gly Gly Phe Pro Gly Gly Ala Gly Ala Ala Gly Gly Ala Pro
625 630 635 640
Gly Gly Ala Ala Pro Gly Gly Asp Ser Gly Pro Thr Val Glu Glu Val
645 650 655
Asp
<210> 31
<211> 613
<212> PRT
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 31
Met Ala Asp Gly Val Phe Gln Gly Ala Ile Gly Ile Asp Leu Gly Thr
1 5 10 15
Thr Tyr Ser Cys Val Ala Thr Tyr Asp Ser Ala Val Glu Ile Ile Ala
20 25 30
Asn Glu Gln Gly Asn Arg Val Thr Pro Ser Phe Val Ala Phe Thr Pro
35 40 45
Glu Glu Arg Leu Ile Gly Asp Ala Ala Lys Asn Gln Ala Ala Leu Asn
50 55 60
Pro Lys Asn Thr Val Phe Asp Ala Lys Arg Leu Ile Gly Arg Ala Phe
65 70 75 80
Asp Asp Glu Ser Val Gln Lys Asp Ile Lys Ser Trp Pro Phe Lys Val
85 90 95
Val Asn Asp Asn Gly Asn Pro Leu Ile Glu Val Glu Tyr Leu Gly Glu
100 105 110
Thr Lys Gln Phe Ser Pro Gln Glu Ile Ser Ser Met Val Leu Thr Lys
115 120 125
Met Lys Glu Val Ala Glu Ala Lys Ile Gly Gln Lys Val Glu Lys Ala
130 135 140
Val Val Thr Val Pro Ala Tyr Phe Asn Asp Ala Gln Arg Gln Ala Thr
145 150 155 160
Lys Asp Ala Gly Ala Ile Ser Gly Leu Asn Val Leu Arg Ile Ile Asn
165 170 175
Glu Pro Thr Ala Ala Ala Ile Ala Tyr Gly Leu Gly Ala Gly Lys Ser
180 185 190
Glu Glu Glu Lys His Val Leu Ile Phe Asp Leu Gly Gly Gly Thr Phe
195 200 205
Asp Val Ser Leu Leu His Ile Ala Gly Gly Val Phe Thr Val Lys Ala
210 215 220
Thr Ala Gly Asp Thr His Leu Gly Gly Gln Asp Phe Asp Thr Asn Leu
225 230 235 240
Leu Glu Phe Phe Lys Lys Glu Phe Gln Lys Lys Thr Gly Lys Asp Ile
245 250 255
Ser Asp Asp Ala Arg Ala Leu Arg Arg Leu Arg Thr Ala Cys Glu Arg
260 265 270
Ala Lys Arg Thr Leu Ser Ser Val Ala Gln Thr Thr Val Glu Val Asp
275 280 285
Ser Leu Phe Asp Gly Glu Asp Phe Thr Ala Glu Ile Ser Arg Ala Lys
290 295 300
Phe Glu Ala Ile Asn Ala Asp Leu Phe Lys Ser Thr Leu Glu Pro Val
305 310 315 320
Glu Gln Val Leu Lys Asp Ser Lys Ile Glu Lys Ser Lys Val Asp Asp
325 330 335
Val Val Leu Val Gly Gly Ser Thr Arg Ile Pro Lys Val Gln Lys Leu
340 345 350
Leu Ser Asp Phe Phe Asp Gly Lys Gln Leu Glu Lys Ser Ile Asn Pro
355 360 365
Asp Glu Ala Val Ala Tyr Gly Ala Ala Val Gln Gly Ala Ile Leu Thr
370 375 380
Gly Gln Ser Thr Ser Glu Glu Thr Lys Asp Leu Leu Leu Leu Asp Val
385 390 395 400
Ile Pro Leu Ser Leu Gly Val Ala Met Gln Gly Asn Val Phe Ala Pro
405 410 415
Val Val Pro Arg Asn Thr Thr Val Pro Thr Ile Lys Arg Arg Thr Phe
420 425 430
Thr Thr Val Asp Asp His Gln Thr Thr Val Gln Phe Pro Val Tyr Gln
435 440 445
Gly Glu Arg Val Asn Cys Ser Glu Asn Thr Leu Leu Gly Glu Phe Asp
450 455 460
Leu Lys Asn Ile Pro Pro Met Ser Ala Gly Glu Pro Val Leu Glu Ala
465 470 475 480
Ile Phe Glu Ile Asp Ala Asn Gly Ile Leu Lys Val Thr Ala Val Glu
485 490 495
Lys Ser Thr Gly Arg Ser Ala Asn Ile Thr Ile Ser Asn Ser Ile Gly
500 505 510
Arg Leu Ser Ser Ser Glu Ile Glu Lys Met Ile Asn Asp Ala Asp Lys
515 520 525
Phe Lys Lys Ala Asp Glu Asp Phe Ala Asn Arg His Glu Ser Lys Gln
530 535 540
Lys Leu Glu Ala Tyr Val Ser Ser Ile Glu Ser Thr Ile Thr Asp Pro
545 550 555 560
Ile Leu Ser Ser Lys Leu Lys Arg Ser Ala Lys Asp Lys Ile Glu Ser
565 570 575
Ala Leu Ser Asp Ala Leu Ala Ala Leu Glu Leu Glu Asp Ala Ser Gly
580 585 590
Asp Asp Phe Arg Lys Ala Glu Leu Ala Leu Lys Arg Val Val Thr Lys
595 600 605
Ala Met Ala Thr Arg
610
<210> 32
<211> 743
<212> PRT
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 32
Met Arg Asp Gly Glu Phe Phe Ser Phe Ser Leu Asn Ser Val Ala Arg
1 5 10 15
Pro Met Gln Ser Phe Phe Gly Lys Thr Asn Ile Leu Ala Asn Leu Arg
20 25 30
Arg Asn Ser Glu Thr Met Ser Val Pro Phe Gly Val Asp Leu Gly Asn
35 40 45
Asn Asn Thr Val Ile Gly Val Ala Arg Asn Arg Gly Ile Asp Ile Leu
50 55 60
Val Asn Glu Val Ser Asn Arg Gln Thr Pro Ser Ile Val Gly Phe Gly
65 70 75 80
Ala Lys Ser Arg Ala Ile Gly Glu Ser Gly Lys Thr Gln Gln Asn Ser
85 90 95
Asn Leu Lys Asn Thr Val Glu His Leu Val Arg Ile Leu Gly Leu Pro
100 105 110
Ala Asp Ser Pro Asp Tyr Glu Ile Glu Lys Lys Phe Phe Thr Ser Pro
115 120 125
Leu Ile Glu Lys Asp Asn Glu Ile Leu Ser Glu Val Asn Phe Gln Gly
130 135 140
Lys Lys Thr Thr Phe Thr Pro Ile Gln Leu Val Ala Met Tyr Leu Asn
145 150 155 160
Lys Ile Lys Asn Thr Ala Ile Lys Glu Thr Lys Gly Lys Phe Thr Asp
165 170 175
Ile Cys Leu Ala Val Pro Val Trp Phe Thr Glu Lys Gln Arg Ser Ala
180 185 190
Ala Ser Asp Ala Cys Lys Val Ala Gly Leu Asn Pro Val Arg Ile Val
195 200 205
Asn Asp Ile Thr Ala Ala Ala Val Gly Tyr Gly Val Phe Lys Thr Asp
210 215 220
Leu Pro Glu Asp Glu Pro Lys Lys Val Ala Ile Val Asp Ile Gly His
225 230 235 240
Ser Thr Tyr Ser Val Leu Ile Ala Ala Phe Lys Lys Gly Glu Leu Lys
245 250 255
Val Leu Gly Ser Ala Ser Asp Lys His Phe Gly Gly Arg Asp Phe Asp
260 265 270
Tyr Ala Ile Thr Lys His Phe Ala Glu Glu Phe Lys Ser Lys Tyr Lys
275 280 285
Ile Asp Ile Thr Gln Asn Pro Lys Ala Trp Ser Arg Val Tyr Thr Ala
290 295 300
Ala Glu Arg Leu Lys Lys Val Leu Ser Ala Asn Thr Thr Ala Pro Phe
305 310 315 320
Asn Val Glu Ser Val Met Asn Asp Val Asp Val Ser Ser Ser Leu Thr
325 330 335
Arg Glu Glu Leu Glu Lys Leu Val Gln Pro Leu Leu Asp Arg Ala His
340 345 350
Ile Pro Val Glu Arg Ala Leu Ala Met Ala Gly Leu Lys Ala Glu Asp
355 360 365
Val Asp Thr Val Glu Val Val Gly Gly Cys Thr Arg Val Pro Thr Leu
370 375 380
Lys Ala Thr Leu Ser Glu Val Phe Gly Lys Pro Leu Ser Phe Thr Leu
385 390 395 400
Asn Gln Asp Glu Ala Ile Ala Arg Gly Ala Ala Phe Ile Cys Ala Met
405 410 415
His Ser Pro Thr Leu Arg Val Arg Pro Phe Lys Phe Glu Asp Val Asn
420 425 430
Pro Tyr Ser Val Ser Tyr Tyr Trp Asp Lys Asp Pro Ala Ala Glu Asp
435 440 445
Asp Asp His Leu Glu Val Phe Pro Val Gly Gly Ser Phe Pro Ser Thr
450 455 460
Lys Val Ile Thr Leu Tyr Arg Ser Gln Asp Phe Asn Ile Glu Ala Arg
465 470 475 480
Tyr Thr Asp Lys Asn Ala Leu Pro Ala Gly Thr Gln Glu Phe Ile Gly
485 490 495
Arg Trp Ser Ile Lys Gly Val Val Val Asn Glu Gly Glu Asp Thr Ile
500 505 510
Gln Thr Lys Ile Lys Leu Arg Asn Asp Pro Ser Gly Phe His Ile Val
515 520 525
Glu Ser Ala Tyr Thr Val Glu Lys Lys Thr Ile Gln Glu Pro Ile Glu
530 535 540
Asp Pro Glu Ala Asp Glu Asp Ala Glu Pro Gln Tyr Arg Thr Val Glu
545 550 555 560
Lys Leu Val Lys Lys Asn Asp Leu Glu Ile Thr Gly Gln Thr Leu His
565 570 575
Leu Pro Asp Glu Leu Leu Asn Ser Tyr Leu Glu Thr Glu Ala Ala Leu
580 585 590
Glu Val Gln Asp Lys Leu Val Ala Asp Thr Glu Glu Arg Lys Asn Ala
595 600 605
Leu Glu Glu Tyr Ile Tyr Glu Leu Arg Gly Lys Leu Glu Asp Gln Tyr
610 615 620
Lys Glu Phe Ala Ser Glu Gln Glu Lys Thr Lys Leu Thr Ala Lys Leu
625 630 635 640
Glu Lys Ala Glu Glu Trp Leu Tyr Asp Glu Gly Tyr Asp Ser Thr Lys
645 650 655
Ala Lys Tyr Ile Ala Lys Tyr Glu Glu Leu Ala Ser Ile Gly Asn Val
660 665 670
Ile Arg Gly Arg Tyr Leu Ala Lys Glu Glu Glu Lys Lys Gln Ala Ile
675 680 685
Arg Glu Lys Glu Glu Ser Lys Lys Ala Ser Ala Ile Ala Glu Lys Met
690 695 700
Ala Ala Glu Arg Ala Ser Arg Glu Ala Ala Gly Ser Thr Asn Glu Gln
705 710 715 720
Ala Gln Lys Asn Glu Glu Asn Thr Lys Asp Ala Asp Gly Asp Val Ser
725 730 735
Met Asn Gln Asp Glu Leu Asp
740
<210> 33
<211> 304
<212> PRT
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 33
Met Pro Val Asp Ser Ser His Lys Thr Ala Ser Pro Leu Pro Pro Arg
1 5 10 15
Lys Arg Ala Lys Thr Glu Glu Glu Lys Glu Gln Arg Arg Val Glu Arg
20 25 30
Ile Leu Arg Asn Arg Arg Ala Ala His Ala Ser Arg Glu Lys Lys Arg
35 40 45
Arg His Val Glu Phe Leu Glu Asn His Val Val Asp Leu Glu Ser Ala
50 55 60
Leu Gln Glu Ser Ala Lys Ala Thr Asn Lys Leu Lys Gln Ile Gln Asp
65 70 75 80
Ile Ile Val Ser Arg Leu Glu Ala Leu Gly Gly Thr Val Ser Asp Leu
85 90 95
Asp Leu Ala Val Pro Glu Val Asp Phe Pro Lys Phe Ser Asp Leu Glu
100 105 110
Leu Ser Thr Asp Leu Ser Ser Ser Thr Lys Ser Glu Lys Ala Ser Thr
115 120 125
Ser Thr Cys Arg Ser Ser Thr Glu Asp Leu Asp Glu Asp Gly Val Ala
130 135 140
Glu Tyr Asp Asp Glu Glu Asp Glu Glu Leu Pro Arg Lys Lys Asn Val
145 150 155 160
Leu Asn Asp Lys Ser Lys Asn Arg Thr Ile Lys Gln Glu Lys Leu Asn
165 170 175
Glu Leu Pro Ser Pro Leu Ser Ser Asp Phe Ser Asp Val Asp Glu Glu
180 185 190
Lys Ser Thr Leu Thr His Phe Gln Leu Gln Gln Gln Gln Gln Gln Gln
195 200 205
Pro Val Asp Asn Tyr Val Ser Thr Pro Leu Ser Leu Pro Glu Asp Ser
210 215 220
Ile Asp Phe Ile Asn Pro Gly Ser Leu Lys Ile Glu Ser Asp Glu Asn
225 230 235 240
Phe Leu Leu Gly Ser Ser Thr Leu Gln Ile Lys His Glu Asn Asp Thr
245 250 255
Glu Tyr Ile Pro Thr Ala Pro Ser Gly Ser Ile Asn Asp Phe Phe Asn
260 265 270
Ser Tyr Asp Ile Ser Glu Ser Asn Arg Leu His His Pro Ala Ala Pro
275 280 285
Phe Thr Ala Asn Ala Phe Asp Leu Asn Asp Phe Val Phe Phe Gln Glu
290 295 300
<210> 34
<211> 831
<212> PRT
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 34
Met Asn Gly Lys His Leu Leu Leu Gln Val Leu Leu Val Gln Leu Val
1 5 10 15
Ala Ala Val Leu Asp Thr Gln Val Gly Tyr Ile Asp Trp Leu Val Thr
20 25 30
Ser Thr Gly Ser Phe Leu Asp Leu Ser Ser Cys Leu Phe Asn Tyr Glu
35 40 45
Gln Ile Tyr Cys Leu Thr Glu Ala Asn Asp Leu Ile Gly Leu Asp Ser
50 55 60
Asp Ala Gln Ile Thr Tyr Arg Leu His Leu Asp Gly Pro Asp Gln Gly
65 70 75 80
Lys Leu Thr Lys Leu Asn Asn Lys Lys Phe Gly Ser Val Arg Gly Asn
85 90 95
Tyr Leu Asp Ile Phe Asn Glu Lys Gly His Leu Leu His Thr Glu Lys
100 105 110
Phe Pro Ser Pro Ile Val Asp Val Tyr Leu Asp Asn Ser Leu Leu Ala
115 120 125
Val Asp Leu Glu Gly Val Val Arg Glu Ile Asp Leu Ser Thr His Ser
130 135 140
Ser Lys Glu Val Ala Thr Leu Gln Ser Leu Ala Cys Ala Met Phe Ser
145 150 155 160
Lys Val Asp Asp Lys Val Thr Ile Ala Phe Lys Gly Ser Asn Ser Asp
165 170 175
Phe Val Lys Ile Ala Ile Leu Glu Asp Lys Val Ser Thr Ile Ser Thr
180 185 190
Asn Ile Ser Ser Val Val His Ile Lys Asn Asn Leu Leu Glu Thr Asp
195 200 205
Glu Gly Ile Tyr Ser Ile Glu Gly Ser Thr Val Lys Lys Ile Leu Asp
210 215 220
Gly Thr Ala Tyr Leu Thr Asp Ile Gly Ala Ile Ser Val Asp Thr Val
225 230 235 240
Lys Asn Ser Val Arg Ser Ser Gly Asn Ser Phe Glu Pro Gln Ser Lys
245 250 255
Ile Leu Lys Val His Ala Glu Asp Glu Phe Ile Val Val Leu Thr Val
260 265 270
Asp Glu Val Leu Glu Ile Asp Leu Glu Thr Phe Asp Leu Ser Ser Val
275 280 285
Lys Glu Asn Ser Leu Thr Glu Glu Tyr Leu Asn Ser Val Asp Tyr Glu
290 295 300
Ile Phe Phe Lys Asn Gln Glu Val Gln Leu Ile Ile Gln Asp Arg Ser
305 310 315 320
Ala Arg Glu Leu Ile Ile Thr Asn Gly Val Ile Gln Lys Val Leu Asp
325 330 335
Leu Ser Leu Asn Asp Val Val Asp Tyr Ser Ile Val Thr Leu Gln Pro
340 345 350
Gln Leu Lys Ala Ile Glu Asp Glu Ile Ile Glu Glu Glu Asn Ser Thr
355 360 365
Phe Phe Lys Ala Tyr Thr Ser Arg Leu Phe Asn Thr Leu Ala Ala Leu
370 375 380
Lys Glu Asn Ile Lys Lys Arg Glu Phe Thr Ser Leu Phe Gln Tyr Asp
385 390 395 400
Thr Ser Gly Gln Asp Gln Ser Phe Gly Leu Asp Lys Arg Leu Val Ile
405 410 415
Gly Cys Ser His Gly Lys Leu Ser Ala Tyr His Leu Leu Thr Lys Thr
420 425 430
Pro Gln Leu Ser Trp Glu Ile Gln Leu Pro Leu Ile Asp Glu Val Ser
435 440 445
Ser Phe Asn Glu Gly Glu Val Ser Val Leu Ser Gly Thr Thr Val Phe
450 455 460
Thr Ile Asp Ala Glu Thr Gly Asp Ile Leu Ser Glu Thr Val Ala Thr
465 470 475 480
Ala Glu Asp Pro Gln Lys Glu Phe Asp Ile Lys Ser Asp Asp Arg Thr
485 490 495
Ile Ser Gly Leu Lys Leu Ile Asn Asn Glu Tyr Ser Ser Thr Trp Thr
500 505 510
Phe Lys Ala Ser Pro Glu Glu Lys Ile Leu Lys Val Val Arg Arg Glu
515 520 525
Asp Asp Asn Ser Asn Val Ala Ser Ala Gly His Ile Leu Gly Asn Asn
530 535 540
Ser Val Leu Phe Lys Tyr Leu Phe Gln Asn Leu Ile Ser Ala Val Leu
545 550 555 560
Leu Asn Glu His Thr Asn Asp Ile Arg Phe Val Ile Leu Asn Ala Ile
565 570 575
Thr Gly Gln Gln Val Tyr Ser Asp Val His Ser Gly Ile Asp Ser Asn
580 585 590
Thr Asn Val Asn Leu Ile Tyr Asp Glu Asn Phe Ile Val Val Ser Tyr
595 600 605
Phe Gly Ser Asp Pro Ile Pro Glu Gln His Ile Val Val Tyr Asp Leu
610 615 620
Tyr Glu Ser Leu Thr Pro Asn Lys Arg Val Glu Pro Lys Asp Gly Leu
625 630 635 640
Val Ser Asn Phe Asp Thr Asp Thr Pro Ile Pro Gln Ile Ser Ser Gln
645 650 655
Ser Phe Leu Phe Pro Ser Arg Ile Asn Phe Ile Ala Ala Ser Arg Ser
660 665 670
Lys Phe Gly Ile Ala Ser Lys Trp Ile Ile Ser Val Leu Glu Asn Gly
675 680 685
Gln Ile Phe Ala Ile Pro Lys Val Val Leu Asn Ser Arg Arg Val Val
690 695 700
Gly Arg Asp Leu Thr Ser Thr Glu Lys Gln Glu Tyr Gly Met Ser Val
705 710 715 720
Tyr Ser Pro Phe Ile Ser Leu Pro Glu Asn Ile Phe Thr Ile Ser Asn
725 730 735
Ile Arg Asn Leu Val Leu Asp Asn Asn Ser Asn Thr Leu Pro Ser Gly
740 745 750
Lys Pro Ile Leu Thr Val Glu Pro Thr Gly Leu Ala Ser Thr Ser Phe
755 760 765
Val Cys Leu Ile Asn Ser Phe Asn Val Tyr Cys Thr Gln Ile Ser Pro
770 775 780
Ser Lys Lys Phe Asp Met Leu Arg Glu Asn Phe Asp Gln Tyr Lys Leu
785 790 795 800
Leu Leu Ser Ile Phe Gly Leu Leu Ala Ile Val Leu Leu Val Arg Pro
805 810 815
Tyr Val Tyr Ser Arg Asn Val Gln Lys Leu Trp Thr Thr Lys Ile
820 825 830
<210> 35
<211> 677
<212> PRT
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 35
Met Leu Ser Leu Lys Pro Ser Trp Leu Thr Leu Ala Ala Leu Leu Tyr
1 5 10 15
Ala Met Leu Met Val Val Val Pro Phe Ala Lys Pro Val Arg Ala Asp
20 25 30
Asp Val Glu Ser Tyr Gly Thr Val Ile Gly Ile Asp Leu Gly Thr Thr
35 40 45
Tyr Ser Cys Val Gly Val Met Lys Ser Gly Arg Val Glu Ile Leu Ala
50 55 60
Asn Asp Gln Gly Asn Arg Ile Thr Pro Ser Tyr Val Ser Phe Thr Glu
65 70 75 80
Asp Glu Arg Leu Val Gly Asp Ala Ala Lys Asn Leu Ala Ala Ser Asn
85 90 95
Pro Lys Asn Thr Ile Phe Asp Ile Lys Arg Leu Ile Gly Met Lys Phe
100 105 110
Asp Ser Pro Glu Val Gln Arg Asp Leu Lys Arg Leu Pro Tyr Ser Val
115 120 125
Lys Ser Lys Asn Gly Gln Pro Ile Val Ser Val Glu Tyr Lys Gly Glu
130 135 140
Glu Lys Ser Phe Thr Pro Glu Glu Ile Ser Ala Met Val Leu Gly Lys
145 150 155 160
Met Lys Leu Ile Ala Glu Asp Tyr Leu Gly Lys Lys Val Thr His Ala
165 170 175
Val Val Thr Val Pro Ala Tyr Phe Asn Asp Ala Gln Arg Gln Ala Thr
180 185 190
Lys Asp Ala Gly Leu Ile Ala Gly Leu Thr Val Leu Arg Ile Val Asn
195 200 205
Glu Pro Thr Ala Ala Ala Leu Ala Tyr Gly Leu Asp Lys Thr Gly Glu
210 215 220
Glu Arg Gln Ile Ile Val Tyr Asp Leu Gly Gly Gly Thr Phe Asp Val
225 230 235 240
Ser Leu Leu Ser Ile Glu Gly Gly Ala Phe Glu Val Leu Ala Thr Ala
245 250 255
Gly Asp Thr His Leu Gly Gly Glu Asp Phe Asp Tyr Arg Val Val Arg
260 265 270
His Phe Val Lys Ile Phe Lys Lys Lys His Asn Ile Asp Ile Ser Asp
275 280 285
Asn Asp Lys Ala Leu Gly Lys Leu Lys Arg Glu Val Glu Lys Ala Lys
290 295 300
Arg Thr Leu Ser Ser Gln Met Thr Thr Arg Ile Glu Ile Asp Ser Phe
305 310 315 320
Val Asp Gly Ile Asp Phe Ser Glu Gln Leu Ser Arg Ala Lys Phe Glu
325 330 335
Glu Ile Asn Ile Glu Leu Phe Lys Lys Thr Leu Lys Pro Val Glu Gln
340 345 350
Val Leu Lys Asp Ala Gly Val Lys Lys Ser Glu Ile Asp Asp Ile Val
355 360 365
Leu Val Gly Gly Ser Thr Arg Ile Pro Lys Val Gln Gln Leu Leu Glu
370 375 380
Asp Phe Phe Asp Gly Lys Lys Ala Ser Lys Gly Ile Asn Pro Asp Glu
385 390 395 400
Ala Val Ala Tyr Gly Ala Ala Val Gln Ala Gly Val Leu Ser Gly Glu
405 410 415
Glu Gly Val Asp Asp Ile Val Leu Leu Asp Val Asn Pro Leu Thr Leu
420 425 430
Gly Ile Glu Thr Thr Gly Gly Val Met Thr Thr Leu Ile Asn Arg Asn
435 440 445
Thr Ala Ile Pro Thr Lys Lys Ser Gln Ile Phe Ser Thr Ala Ala Asp
450 455 460
Asn Gln Pro Thr Val Leu Ile Gln Val Tyr Glu Gly Glu Arg Ala Leu
465 470 475 480
Ala Lys Asp Asn Asn Leu Leu Gly Lys Phe Glu Leu Thr Gly Ile Pro
485 490 495
Pro Ala Pro Arg Gly Thr Pro Gln Val Glu Val Thr Phe Val Leu Asp
500 505 510
Ala Asn Gly Ile Leu Lys Val Ser Ala Thr Asp Lys Gly Thr Gly Lys
515 520 525
Ser Glu Ser Ile Thr Ile Asn Asn Asp Arg Gly Arg Leu Ser Lys Glu
530 535 540
Glu Val Asp Arg Met Val Glu Glu Ala Glu Lys Tyr Ala Ala Glu Asp
545 550 555 560
Ala Ala Leu Arg Glu Lys Ile Glu Ala Arg Asn Ala Leu Glu Asn Tyr
565 570 575
Ala His Ser Leu Arg Asn Gln Val Thr Asp Asp Ser Glu Thr Gly Leu
580 585 590
Gly Ser Lys Leu Asp Glu Asp Asp Lys Glu Thr Leu Thr Asp Ala Ile
595 600 605
Lys Asp Thr Leu Glu Phe Leu Glu Asp Asn Phe Asp Thr Ala Thr Lys
610 615 620
Glu Glu Leu Asp Glu Gln Arg Glu Lys Leu Ser Lys Ile Ala Tyr Pro
625 630 635 640
Ile Thr Ser Lys Leu Tyr Gly Ala Pro Glu Gly Gly Ala Pro Pro Gly
645 650 655
Gln Gly Phe Asp Asp Asp Asp Gly Asp Phe Asp Tyr Asp Tyr Asp Tyr
660 665 670
Asp His Asp Glu Leu
675
<210> 36
<211> 441
<212> PRT
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 36
Met Pro Ile Asp Ile Ile Asn Thr Leu Val Val Lys Gly Thr Asp Gly
1 5 10 15
Ile Pro Gly Trp Pro Ile Ile Lys Arg Tyr Gly Leu Pro Phe Val Ala
20 25 30
Leu Ser Leu Leu Lys Val Tyr Cys Gly Gly Lys Leu Asn Pro Trp Gln
35 40 45
Arg Asp Val His Gly Lys Val Tyr Ile Leu Thr Gly Ala Thr Ala Gly
50 55 60
Val Gly Ser Gln Leu Ala Glu Glu Leu Ala Lys Gly Gly Ala Gln Leu
65 70 75 80
Ile Leu Leu Val Lys Asp Pro Ser Ser Ser Trp Thr Val Glu Phe Val
85 90 95
Asp Asp Leu Arg Glu Arg Thr Gly Asn Pro Leu Val Tyr Ala Glu Gln
100 105 110
Cys Asp Leu Ala Asp Leu His Ser Val Arg Lys Phe Ala Thr Arg Trp
115 120 125
Leu Asp Asn Thr Pro Pro Arg Arg Leu Asp Gly Ile Val Gly Cys Ala
130 135 140
Gly Glu Ala Leu Pro Leu Gly Ala Ala Arg Ser Thr Ser Ser Asp Gly
145 150 155 160
Val Glu Arg Gln Val Ala Val Asn Tyr Leu Gly His Phe His Leu Leu
165 170 175
Ala Leu Leu Ser Pro Ser Leu Arg Ala Gln Pro Ala Asp Arg Asp Val
180 185 190
Arg Val Val Leu Thr Thr Cys Thr Thr Gln Ala Met Gly Gln Val Ser
195 200 205
Leu Asp Asp Pro Leu Trp Leu Asp Ser Gln Tyr Pro Ser Lys Arg Pro
210 215 220
Trp Gln Val Phe Gly Gly Ala Lys Leu Met Leu Gly Cys Phe Ala Gln
225 230 235 240
Glu Phe Gln Arg Arg Leu Asp Ala Thr Pro Arg Gly Asp Lys Met Pro
245 250 255
Ser Lys Leu Arg Val Asn Val Val Asn Pro Gly Phe Met Arg Thr Ala
260 265 270
Ser Thr Ala Arg Val Leu Ser Phe Gly Ser Leu Trp Gly Leu Leu Leu
275 280 285
Tyr Leu Leu Leu Tyr Pro Ile Trp Phe Ile Leu Phe Lys Thr Pro Ile
290 295 300
Gln Gly Ala Gln Ser Tyr Leu Ala Ala Leu Phe Ala Glu His Phe Ile
305 310 315 320
Glu Leu Pro Gly Gly Gln Phe Ile Gln Asp Cys Lys Ile Val Lys Pro
325 330 335
Ala Arg Lys Glu Leu Ser Asp Phe Thr Phe Gln Asn Lys Leu Tyr Glu
340 345 350
Lys Thr Glu Lys Leu Ile Asp Gln Leu Glu Arg Gln Ser Ala Lys Gln
355 360 365
Arg Val Arg Ser Lys Pro Lys Ser Asn Ser Lys Ser Lys Pro Ser Lys
370 375 380
Lys Ser Gly Thr Ala Asn Val Gly Pro Glu Lys Glu Asn Asp Val Phe
385 390 395 400
Ala Ser Ala Leu Lys Ala Thr Pro Pro Asp Leu Phe Pro His Gln Arg
405 410 415
Ala Asp Pro Ala Gly Asn Lys Tyr Leu Asp Gln Leu Glu Lys Lys Leu
420 425 430
Ala Glu Gln Ser Lys Lys His Ser Thr
435 440
<210> 37
<211> 441
<212> PRT
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 37
Met Ser Phe Phe Ser Gln Leu Thr Gly Ala Leu Asp Lys Pro Gly Phe
1 5 10 15
Asn Trp Lys Leu Leu Ile Ala Gly Phe Ser Ser Ala Glu Phe Ala Phe
20 25 30
Glu Ala Tyr Leu Ser Tyr Arg Gln Ile Lys Lys Leu Gln Glu Lys Gly
35 40 45
His Gln Val Pro Gln Ser Leu Lys Gly Lys Ile Glu Glu Asp Val Ala
50 55 60
Leu Lys Ser Gln Asp Tyr Ser Phe Thr Lys Leu Lys Phe Gly Ile Phe
65 70 75 80
Ser Asp Ala Val Asn Leu Leu Tyr Asn Leu Thr Trp Ile Lys Phe Asp
85 90 95
Ile Leu Pro Lys Leu Trp Asn Leu Ser Gly Asn Leu Leu Ala Asn Ser
100 105 110
Leu Ala Phe Leu Pro Trp Lys Gly Thr Leu Val Gln Ser Leu Val Phe
115 120 125
Val Asn Leu Leu Ser Ile Ala Gly Leu Val Val Ser Leu Pro Leu Ser
130 135 140
Tyr Tyr Ser Thr Phe Val Ile Glu Glu Lys Phe Gly Phe Asn Lys Gln
145 150 155 160
Thr Leu Lys Leu Trp Ile Thr Asp Ala Ile Lys Gly Leu Leu Leu Ser
165 170 175
Phe Val Phe Gly Thr Ala Ile Tyr Ala Gly Phe Leu Lys Ile Val Asp
180 185 190
Tyr Phe Ser Asp Thr Phe Met Phe Tyr Met Ser Val Phe Met Phe Val
195 200 205
Ile Gln Ile Phe Phe Ile Ile Phe Tyr Pro Lys Phe Ile Gln Pro Leu
210 215 220
Phe Asn Lys Leu Thr Pro Leu Glu Asp Gly Glu Leu Lys Gln Ser Ile
225 230 235 240
Glu Lys Leu Ala Ala Asp Gln Lys Phe Pro Leu Asp Lys Leu Tyr Val
245 250 255
Ile Asp Gly Ser Lys Arg Ser Ser His Ser Asn Ala Tyr Phe Leu Gly
260 265 270
Leu Pro Trp Gly Thr Lys Gln Ile Val Ile Phe Asp Thr Leu Ile Glu
275 280 285
Lys Ser Ser Val Asp Glu Val Thr Ala Val Leu Gly His Glu Ile Gly
290 295 300
His Trp Ala Leu Ser His Thr Thr Lys Leu Leu Leu Ile Asn Gln Val
305 310 315 320
Gln Leu Phe Ser Ile Phe Ser Leu Phe Ala Leu Phe Phe Lys Asn Lys
325 330 335
Ser Leu Tyr Gln Ser Phe Gly Phe Ser Gly Gln Pro Val Ile Ile Gly
340 345 350
Phe Thr Leu Phe Ser Asp Val Leu Lys Pro Phe Asn Ala Val Leu Ser
355 360 365
Phe Ala Thr Asn Leu Leu Ser Arg Asn Tyr Glu Tyr Gln Ala Asp Glu
370 375 380
Tyr Ala Val Asp Leu Gly Tyr Ser Ser Asp Leu Ser Ser Ala Leu Ile
385 390 395 400
Ser Leu His Lys Glu Asn Leu Ser Ser Leu His Val Asp Trp Leu Tyr
405 410 415
Ser Ala Tyr Ser His Ser His Pro His Leu Thr Glu Arg Leu Gln Ala
420 425 430
Ile Glu Phe Asn Ala Lys Lys Glu Lys
435 440
<210> 38
<211> 257
<212> PRT
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 38
Met Ser Arg Glu Asp Ser Val Tyr Leu Ala Lys Leu Ala Glu Gln Ala
1 5 10 15
Glu Arg Tyr Glu Glu Met Val Glu Asn Met Lys Thr Val Ala Ser Ser
20 25 30
Gly Leu Glu Leu Ser Val Glu Glu Arg Asn Leu Leu Ser Val Ala Tyr
35 40 45
Lys Asn Val Ile Gly Ala Arg Arg Ala Ser Trp Arg Ile Val Ser Ser
50 55 60
Ile Glu Gln Lys Glu Glu Ala Lys Gly Asn Gln Ser Gln Val Ser Leu
65 70 75 80
Ile Arg Glu Tyr Arg Ser Lys Ile Glu Thr Glu Leu Ala Asn Ile Cys
85 90 95
Glu Asp Ile Leu Ser Val Leu Ser Glu His Leu Ile Pro Ser Ala Arg
100 105 110
Thr Gly Glu Ser Lys Val Phe Tyr Phe Lys Met Lys Gly Asp Tyr His
115 120 125
Arg Tyr Leu Ala Glu Phe Ala Val Gly Asp Lys Arg Lys Glu Ala Ala
130 135 140
Asn Leu Ser Leu Glu Ala Tyr Lys Ser Ala Ser Asp Val Ala Val Thr
145 150 155 160
Glu Leu Pro Pro Thr His Pro Ile Arg Leu Gly Leu Ala Leu Asn Phe
165 170 175
Ser Val Phe Tyr Tyr Glu Ile Leu Asn Ser Pro Asp Arg Ala Cys His
180 185 190
Leu Ala Lys Gln Ala Phe Asp Asp Ala Ile Ala Glu Leu Glu Thr Leu
195 200 205
Ser Glu Glu Ser Tyr Lys Asp Ser Thr Leu Ile Met Gln Leu Leu Arg
210 215 220
Asp Asn Leu Thr Leu Trp Thr Ser Asp Met Ser Glu Thr Gly Gln Glu
225 230 235 240
Glu Ser Ser Asn Ser Gln Asp Lys Thr Glu Ala Ala Pro Lys Asp Glu
245 250 255
Glu
<210> 39
<211> 527
<212> PRT
<213> 人工序列
<220>
<223> 合成的聚合物
<400> 39
Met Arg Ile Val Arg Ser Val Ala Ile Ala Ile Ala Cys His Cys Ile
1 5 10 15
Thr Ala Leu Ala Asn Pro Gln Ile Pro Phe Asp Gly Asn Tyr Thr Glu
20 25 30
Ile Ile Val Pro Asp Thr Glu Val Asn Ile Gly Gln Ile Val Asp Ile
35 40 45
Asn His Glu Ile Lys Pro Lys Leu Val Glu Leu Val Asn Thr Asp Phe
50 55 60
Phe Lys Tyr Tyr Lys Leu Asn Leu Trp Lys Pro Cys Pro Phe Trp Asn
65 70 75 80
Gly Asp Glu Gly Phe Cys Lys Tyr Lys Asp Cys Ser Val Asp Phe Ile
85 90 95
Thr Asp Trp Ser Gln Val Pro Asp Ile Trp Gln Pro Asp Gln Leu Gly
100 105 110
Lys Leu Gly Asp Asn Thr Val His Lys Asp Lys Gly Gln Asp Glu Asn
115 120 125
Glu Leu Ser Ser Asn Asp Tyr Cys Ala Leu Asp Lys Asp Asp Asp Glu
130 135 140
Asp Leu Val Tyr Val Asn Leu Ile Asp Asn Pro Glu Arg Phe Thr Gly
145 150 155 160
Tyr Gly Gly Gln Gln Ser Glu Ser Ile Trp Thr Ala Val Tyr Asp Glu
165 170 175
Asn Cys Phe Gln Pro Asn Glu Gly Ser Gln Leu Gly Gln Val Glu Asp
180 185 190
Leu Cys Leu Glu Lys Gln Ile Phe Tyr Arg Leu Val Ser Gly Leu His
195 200 205
Ser Ser Ile Ser Thr His Leu Thr Asn Glu Tyr Leu Asn Leu Lys Asn
210 215 220
Gly Ala Tyr Glu Pro Asn Leu Lys Gln Phe Met Ile Lys Val Gly Tyr
225 230 235 240
Phe Thr Glu Arg Ile Gln Asn Leu His Leu Asn Tyr Val Leu Val Leu
245 250 255
Lys Ser Leu Ile Lys Leu Gln Glu Tyr Asn Val Ile Asp Asn Leu Pro
260 265 270
Leu Asp Asp Ser Leu Lys Ala Gly Leu Ser Gly Leu Ile Ser Gln Gly
275 280 285
Ala Gln Gly Ile Asn Gln Ser Ser Asp Asp Tyr Leu Phe Asn Glu Lys
290 295 300
Val Leu Phe Gln Asn Asp Gln Asn Asp Asp Leu Lys Asn Glu Phe Arg
305 310 315 320
Asp Lys Phe Arg Asn Val Thr Arg Leu Met Asp Cys Val His Cys Glu
325 330 335
Arg Cys Lys Leu Trp Gly Lys Leu Gln Thr Thr Gly Tyr Gly Thr Ala
340 345 350
Leu Lys Ile Leu Phe Asp Leu Lys Asn Pro Asn Asp Ser Ile Asn Leu
355 360 365
Lys Arg Val Glu Leu Val Ala Leu Val Asn Thr Phe His Arg Leu Ser
370 375 380
Lys Ser Val Glu Ser Ile Glu Asn Phe Glu Lys Leu Tyr Lys Ile Gln
385 390 395 400
Pro Pro Thr Gln Asp Arg Ala Ser Ala Ser Ser Glu Ser Leu Gly Leu
405 410 415
Phe Asp Asn Glu Asp Glu Gln Asn Leu Leu Asn Ser Phe Ser Val Asp
420 425 430
Gln Ala Val Ile Ser Ser Lys Glu Ala Pro Glu Glu Ile Lys Ser Lys
435 440 445
Pro Val Gly Lys Ala Ala Tyr Lys Gln Asn Ser Cys Pro Ser Leu Gly
450 455 460
Ser Lys Ser Ile Lys Glu Ala Phe His Glu Glu Leu His Ala Phe Ile
465 470 475 480
Asp Ala Ile Gly Phe Ile Leu Asn Ser Tyr Arg Thr Leu Pro Lys Leu
485 490 495
Leu Tyr Thr Leu Phe Leu Val Lys Ser Ser Glu Leu Trp Asp Ile Phe
500 505 510
Ile Gly Thr Gln Arg His Arg Asp Thr Thr Tyr Arg Val Asp Leu
515 520 525
Claims (95)
1.一种用于表达异源蛋白质的工程化宿主细胞,所述工程化宿主细胞包含至少三个不同表达盒,所述至少三个不同表达盒被整合至所述工程化宿主细胞的基因组中,其中,
a.第一表达盒,其包含与编码所述异源蛋白质的异源基因序列可操作地连接的第一启动子;
b.第二表达盒,其包含与编码所述异源蛋白质的异源基因序列可操作地连接的第二启动子;
c.第三表达盒,其包含与辅助因子序列可操作地连接的第三启动子;并且
d.所述辅助因子编码序列与所述异源蛋白质编码序列的拷贝数比为至少1:10。
2.一种用于表达异源蛋白质的工程化宿主细胞,所述工程化宿主细胞包含至少三个不同表达盒,所述至少三个不同表达盒被整合至所述工程化宿主细胞的基因组中,其中;
a.第一表达盒,其包含与编码所述异源蛋白质的异源基因序列可操作地连接的第一启动子;
b.第二表达盒,其包含与编码所述异源蛋白质的异源基因序列可操作地连接的第二启动子;
c.第三表达盒,其包含与辅助因子序列可操作地连接的第三启动子;并且
d.所述辅助因子编码序列与所述异源蛋白质编码序列的拷贝数比为至多1:2。
3.根据权利要求1或2所述的工程化宿主细胞,其中所述辅助因子编码序列与所述异源蛋白质编码序列的拷贝数比为至少1:10、1:9、1:8、1:7、1:6、1:5、1:4或1:3。
4.根据权利要求1或2所述的工程化宿主细胞,其中所述辅助因子编码序列与所述异源蛋白质编码序列的拷贝数比为至多1:9、1:8、1:7、1:6、1:5、1:4、1:3或1:2。
5.根据权利要求1或2所述的工程化宿主细胞,其中至少一个启动子是诱导型启动子。
6.根据权利要求1或2所述的工程化宿主细胞,其中所有启动子均是诱导型启动子。
7.根据权利要求5或6所述的工程化宿主细胞,其中所述诱导型启动子是甲醇诱导型启动子。
8.根据权利要求7所述的工程化宿主细胞,其中每个所述甲醇诱导型启动子独立地选自AOX1、AOX2、DAK2、DAS2、FDH1、FGH1、FLD1和PEX11或其甲醇诱导型片段。
9.根据权利要求1至3中任一项所述的工程化宿主细胞,其中至少一个启动子是组成型启动子。
10.根据权利要求9所述的工程化宿主细胞,其中每个所述组成型启动子独立地选自GAP和GCW14。
11.根据权利要求1至10中任一项所述的工程化宿主细胞,其中所述宿主细胞包含所述第一表达盒的至少2个拷贝。
12.根据权利要求1至11中任一项所述的工程化宿主细胞,其中所述宿主细胞包含所述第二表达盒的至少2个拷贝。
13.根据权利要求1至12中任一项所述的工程化宿主细胞,其中所述宿主细胞包含第四表达盒的至少1个拷贝,所述第四表达盒包含与所述异源基因序列可操作地连接的第四启动子。
14.根据权利要求1至13中任一项所述的工程化宿主细胞,其中所述第一盒和所述第二盒以相同的5’至3’方向被整合至所述基因组中。
15.根据权利要求1至13中任一项所述的工程化宿主细胞,其中所述第一盒和所述第二盒以相对的5’至3’方向被整合至所述基因组中。
16.根据前述权利要求中任一项所述的工程化宿主细胞,其中所述宿主细胞在1或2个表达盒中包含所述辅助因子编码序列的至少2个拷贝。
17.根据前述权利要求中任一项所述的工程化宿主细胞,其中所述宿主细胞在1、2、3、4或5个表达盒中包含所述辅助因子编码序列的至少3、4或5个拷贝。
18.根据前述权利要求中任一项所述的工程化宿主细胞,其中所述宿主细胞在1、2、3、4、5、6、7、8、9、10、11、12、13、14、15或16个表达盒中包含所述异源编码序列的至少3、4、5、6、7、8、9、10、11、12、13、14、15或16个拷贝。
19.根据前述权利要求中任一项所述的工程化宿主细胞,其中所述异源蛋白质是食物相关蛋白质。
20.根据权利要求19所述的工程化宿主细胞,其中所述食物相关蛋白质包括酶、营养蛋白质、食物成分或食物添加剂。
21.根据权利要求20所述的工程化宿主细胞,其中所述食物相关蛋白质是胃蛋白酶原蛋白质。
22.根据权利要求21所述的工程化宿主细胞,其中所述辅助因子编码序列与胃蛋白酶原编码序列的拷贝数比为1:2至1:5。
23.根据权利要求20所述的工程化宿主细胞,其中所述食物相关蛋白质包括卵白蛋白质。
24.根据权利要求23所述的工程化宿主细胞,其中所述卵白蛋白质是卵类黏蛋白。
25.根据权利要求24所述的工程化宿主细胞,其中所述辅助因子编码序列与卵类黏蛋白编码序列的拷贝数比为1:3至1:6。
26.根据权利要求23所述的工程化宿主细胞,其中所述卵白蛋白质是卵清蛋白。
27.根据权利要求26所述的工程化宿主细胞,其中所述辅助因子编码序列与卵清蛋白编码序列的拷贝数比为1:3至1:8。
28.根据前述权利要求中任一项所述的工程化宿主细胞,其中在发酵条件下,所述工程化宿主细胞能够产生每升至少约5g的所述异源蛋白质。
29.根据前述权利要求中任一项所述的工程化宿主细胞,其中在发酵条件下,所述工程化宿主细胞能够产生每升至少约10g的所述异源蛋白质。
30.根据前述权利要求中任一项所述的工程化宿主细胞,其中在发酵条件下,所述工程化宿主细胞能够产生每升至少约20g的所述异源蛋白质。
31.根据前述权利要求中任一项所述的工程化宿主细胞,其中所述表达盒中的至少一个包含分泌信号。
32.根据前述权利要求中任一项所述的工程化宿主细胞,其中所述表达盒中的至少一个包含终止序列。
33.根据前述权利要求中任一项所述的工程化宿主细胞,其中所述辅助因子基因序列中的每一个编码一蛋白质,所述蛋白质独立地选自HAC1、丝氨酸/苏氨酸蛋白激酶2(Kin2)、鲨烯合成酶(ERG9)、蛋白质二硫键异构酶1(PDI1)、SSA1、SSA4、SSB1、SSE1、BiP、ER膜蛋白复合物亚基1(EMC1)、YNL181W氧化还原酶、整合膜蛋白锌金属蛋白酶Ste24、14-3-3蛋白Bmh2和内质网氧化还原蛋白1(Ero1)。
34.根据前述权利要求中任一项所述的工程化宿主细胞,其中将所述宿主细胞工程化以有利于非同源整合而不是同源整合并且/或者基于比同源整合更多的非同源整合对所述宿主细胞进行选择。
35.根据前述权利要求中任一项所述的工程化宿主细胞,其中包含所述异源基因序列的所述表达盒中的至少两个在不同整合位点处整合。
36.根据前述权利要求中任一项所述的工程化宿主细胞,其中所述宿主细胞是酵母细胞。
37.根据权利要求36所述的工程化宿主细胞,其中所述酵母细胞是毕赤酵母。
38.根据权利要求1-37所述的工程化宿主细胞,其中通过对所述宿主细胞的基因组进行测序来测量所述拷贝数。
39.一种在宿主细胞中产生重组异源蛋白质的方法,所述方法包括:
a.将第一媒介物转化至所述宿主细胞中;其中所述第一媒介物包含一个或多个第一表达盒;其中所述第一表达盒中的每一个至少包含与编码所述异源蛋白质的异源基因序列可操作地连接的第一启动子;
b.将所述一个或多个第一表达盒随机整合至所述宿主细胞中;
c.鉴定所述一个或多个第一表达盒在所述宿主细胞中的整合;
d.将第二媒介物转化至所述宿主细胞中;其中所述第二媒介物包含一个或多个第二表达盒;其中所述第二表达盒中的每一个至少包含与所述异源基因序列可操作地连接的第二启动子;其中所述第二启动子与所述第一启动子不同;以及
e.将所述一个或多个第二表达盒随机整合至所述宿主细胞中;
其中所述宿主细胞是酵母或丝状真菌,并且其中在发酵条件下,工程化细胞能够产生每升至少5g的所述异源蛋白质。
40.根据权利要求39所述的方法,其中步骤(d)进一步包括转化除了所述第二媒介物之外的多个媒介物,其中所述多个媒介物中的每一个包含一个或多个表达盒,所述一个或多个表达盒各自包含驱动编码所述异源蛋白质的所述异源基因序列进行表达的一个或多个启动子。
41.根据权利要求40所述的方法,其中所述一个或多个启动子包括所述第一启动子、所述第二启动子或其组合。
42.根据权利要求40所述的方法,其中所述一个或多个启动子包括所述第一启动子、所述第二启动子、除了所述第一启动子或第二启动子之外的启动子或其组合。
43.根据权利要求39所述的方法,其中鉴定所述一个或多个第一表达盒的整合包括对获自所述宿主细胞的核酸进行测序。
44.根据权利要求39-43所述的方法,其中鉴定所述一个或多个第一表达盒的整合包括鉴定是否存在抗性标志物;其中所述第一表达盒或第一质粒包含编码所述抗性标志物的序列。
45.根据权利要求39至44中任一项所述的方法,其中在发酵期间,所述异源蛋白质被分泌到培养基中,并且其中从发酵培养基收获所述异源重组蛋白质。
46.根据权利要求39至45中任一项所述的方法,其中所述第一表达盒和所述第二表达盒是线性分子,并且其中所述第一表达盒和所述第二表达盒在5’端有少于700bp与天然宿主细胞的基因组基因座同源。
47.根据权利要求39至46中任一项所述的方法,其中将所述宿主细胞工程化以有利于非同源整合而不是同源整合并且/或者基于比同源整合更多的非同源整合对所述宿主细胞进行选择。
48.根据权利要求39至47中任一项所述的方法,其中所述方法进一步包括将辅助媒介物转化至所述宿主细胞中;其中所述辅助媒介物包含一个或多个辅助表达盒;其中所述辅助表达盒中的每一个包含与编码辅助因子蛋白质的基因序列可操作地连接的至少一个启动子。
49.根据权利要求48所述的方法,其中所述一个或多个辅助表达盒中的启动子与所述第一启动子或第二启动子相同。
50.根据权利要求48所述的方法,其中所述一个或多个辅助表达盒中的启动子与所述第一启动子或第二启动子不同。
51.根据权利要求39-50中任一项所述的方法,其中所述媒介物是质粒。
52.根据权利要求39-50中任一项所述的方法,其中所述媒介物是线性化质粒。
53.一种在宿主细胞中产生重组异源蛋白质的方法,所述方法包括:
a.将多个质粒转化至所述宿主细胞中;其中所述多个质粒包含至少三个质粒,所述至少三个质粒中的每一个包含不同表达盒;其中所述不同表达盒中的每一个包含与异源基因序列可操作地连接的不同启动子;
b.将所述至少三个不同表达盒中的每一个的至少一个拷贝整合至所述宿主细胞中;
其中所述至少三个表达盒中的至少一个包含与辅助因子基因序列可操作地连接的启动子;
其中所述辅助因子基因与所述异源基因的拷贝数比为至少1:10。
54.一种在宿主细胞中产生重组异源蛋白质的方法,所述方法包括:
a.将多个质粒转化至所述宿主细胞中;其中所述多个质粒包含至少三个质粒,所述至少三个质粒中的每一个包含不同表达盒;其中所述不同表达盒中的每一个包含与异源基因序列可操作地连接的不同启动子;
b.将所述至少三个不同表达盒中的每一个的至少一个拷贝整合至所述宿主细胞中;
其中所述至少三个表达盒中的至少一个包含与辅助因子基因序列可操作地连接的启动子;
其中所述辅助因子基因与所述异源基因的拷贝数比为至多1:2。
55.根据权利要求53或54所述的方法,其中所述辅助因子编码序列与所述异源蛋白质编码序列的拷贝数比为至少1:10、1:9、1:8、1:7、1:6、1:5、1:4或1:3。
56.根据权利要求53或54所述的方法,其中所述辅助因子编码序列与所述异源蛋白质编码序列的拷贝数比为至多1:9、1:8、1:7、1:6、1:5、1:4、1:3或1:2。
57.根据权利要求53或54所述的方法,其中至少一个启动子是诱导型启动子。
58.根据权利要求53或54所述的方法,其中所有启动子均是诱导型启动子。
59.根据权利要求57或58所述的方法,其中所述诱导型启动子是甲醇诱导型启动子。
60.根据权利要求59所述的方法,其中每个甲醇诱导型启动子独立地选自AOX1、AOX2、DAK2、DAS2、FDH1、FGH1、FLD1和PEX11或其甲醇诱导型片段。
61.根据权利要求53至60中任一项所述的方法,其中至少一个启动子是组成型启动子。
62.根据权利要求61所述的方法,其中每个组成型启动子独立地选自GAP和GCW14。
63.根据权利要求53至62中任一项所述的方法,其中所述宿主细胞包含第一表达盒的至少2个拷贝。
64.根据权利要求53至63中任一项所述的方法,其中所述宿主细胞包含第二表达盒的至少2个拷贝。
65.根据权利要求53至64中任一项所述的方法,其中所述宿主细胞包含第三表达盒的至少1个拷贝,所述第三表达盒包含与所述异源基因序列可操作地连接的第三启动子。
66.根据权利要求53至65中任一项所述的方法,其中所述宿主细胞包含第四表达盒的至少1个拷贝,所述第四表达盒包含与所述异源基因序列可操作地连接的第四启动子。
67.根据权利要求63至66中任一项所述的方法,其中所述第一盒和所述第二盒以相同的5’至3’方向被整合至所述基因组中。
68.根据权利要求63至66中任一项所述的方法,其中所述第一盒和所述第二盒以相对的5’至3’方向被整合至所述基因组中。
69.根据权利要求53-68中任一项所述的方法,其中所述宿主细胞在1或2个表达盒中包含辅助因子编码序列的至少2个拷贝。
70.根据权利要求53-69中任一项所述的方法,其中所述宿主细胞在1、2、3、4或5个表达盒中包含所述辅助因子编码序列的至少3、4或5个拷贝。
71.根据权利要求53-70中任一项所述的方法,其中所述宿主细胞在1、2、3、4、5、6、7、8、9、10、11、12、13、14、15或16个表达盒中包含所述异源编码序列的至少3、4、5、6、7、8、9、10、11、12、13、14、15或16个拷贝。
72.根据权利要求53-72中任一项所述的方法,其中所述异源蛋白质是食物相关蛋白质。
73.根据权利要求72所述的方法,其中所述食物相关蛋白质包括酶、营养蛋白质、食物成分或食物添加剂。
74.根据权利要求73所述的方法,其中所述食物相关蛋白质是胃蛋白酶原蛋白质。
75.根据权利要求74所述的方法,其中所述辅助因子编码序列与胃蛋白酶原编码序列的拷贝数比为1:2至1:5。
76.根据权利要求72所述的方法,其中所述食物相关蛋白质包括卵白蛋白质。
77.根据权利要求76所述的方法,其中所述卵白蛋白质是卵类黏蛋白。
78.根据权利要求77所述的方法,其中所述辅助因子编码序列与卵类黏蛋白编码序列的拷贝数比为1:3至1:6。
79.根据权利要求76所述的方法,其中所述卵白蛋白质是卵清蛋白。
80.根据权利要求79所述的方法,其中所述辅助因子编码序列与卵清蛋白编码序列的拷贝数比为1:3至1:8。
81.根据权利要求53-80中任一项所述的方法,其中在发酵条件下,所述工程化宿主细胞能够产生每升至少约5g的所述异源蛋白质。
82.根据权利要求53-81中任一项所述的方法,其中在发酵条件下,所述工程化宿主细胞能够产生每升至少约10g的所述异源蛋白质。
83.根据权利要求53-82中任一项所述的方法,其中在发酵条件下,所述工程化宿主细胞能够产生每升至少约20g的所述异源蛋白质。
84.根据权利要求53-83中任一项所述的方法,其中所述表达盒中的至少一个包含分泌信号。
85.根据权利要求53-84中任一项所述的方法,其中所述表达盒中的至少一个包含终止序列。
86.根据权利要求53-85中任一项所述的方法,其中所述辅助因子基因序列中的每一个编码一蛋白质,所述蛋白质独立地选自HAC1、丝氨酸/苏氨酸蛋白激酶2(Kin2)、鲨烯合成酶(ERG9)、蛋白质二硫键异构酶1(PDI1)、SSA1、SSA4、SSB1、SSE1、BiP、ER膜蛋白复合物亚基1(EMC1)、YNL181W氧化还原酶、整合膜蛋白锌金属蛋白酶Ste24、14-3-3蛋白Bmh2和内质网氧化还原蛋白1(Ero1)。
87.根据权利要求53-86中任一项所述的方法,其中将所述宿主细胞工程化以有利于非同源整合而不是同源整合并且/或者基于比同源整合更多的非同源整合对所述宿主细胞进行选择。
88.根据权利要求53-87中任一项所述的方法,其中包含所述异源基因序列的所述表达盒中的至少两个在不同整合位点处整合。
89.根据权利要求53-88中任一项所述的方法,其中所述宿主细胞是酵母细胞。
90.根据权利要求89所述的方法,其中所述酵母细胞是毕赤酵母。
91.根据权利要求53或54中任一项所述的方法,其中所述方法进一步包括鉴定所述整合的表达盒。
92.根据权利要求91所述的方法,其中所述鉴定包括对所述宿主细胞的基因组进行测序。
93.根据权利要求91所述的方法,其中所述鉴定包括确定是否存在与所述异源基因序列可操作地连接的启动子。
94.根据权利要求93所述的方法,其中所述方法进一步包括转化包含一个或多个表达盒的至少一个质粒,其中所述表达盒中的每一个包含与所述异源基因序列可操作地连接的启动子,其中所述启动子被鉴定为存在于所述宿主细胞基因组中。
95.根据权利要求93所述的方法,其中所述方法进一步包括转化包含一个或多个表达盒的至少一个质粒,其中所述表达盒中的每一个包含与所述异源基因序列可操作地连接的启动子,其中所述启动子被鉴定为不存在于所述宿主细胞基因组中。
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