扇贝丝氨酸蛋白酶及其抑制剂基因的克隆与表达
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摘要
扇贝是我国海水养殖的重要品种,但自1994年以来,养殖扇贝陆续爆发的大规模死亡,不但造成了巨大的经济损失,而且直接威胁到现有产业的生存和发展。引起扇贝大规模死亡原因是多方面的,其主要原因是养殖环境恶化、扇贝种质衰退和抗病力下降。因此,在积极调整产业结构、加强环境治理、开展扇贝病原及流行病学研究的同时,深入研究扇贝免疫防御机制,探讨提高机体抗病力的有效途径和方法,改良种质和培育抗病品系,无疑是解决目前困扰扇贝养殖业健康可持续发展的必经之路。
丝氨酸蛋白酶及其抑制因子在无脊椎动物的免疫应答中起着核心作用,它们的协同作用不但直接导致免疫信号转导和级联放大,还可激活特异性防御体系,如黑化反应、血液凝结和抗菌肽的合成等。本研究采用大规模EST测序方法,结合cDNA末端快速扩增技术,直接从cDNA文库中分离、克隆了9个扇贝免疫相关的丝氨酸蛋白酶及其抑制剂基因的全长cDNA序列,应用Northern blotting和RT-PCR方法检测了这些基因的组织定位及在损伤和不同类型微生物感染下的表达规律。
栉孔扇贝丝氨酸蛋白酶基因CFPS1和CFPS2的cDNA全长分别为1211-bp和1152-bp,分别编码354和336个氨基酸,均为具有信号肽执行胞外功能的分泌蛋白。两个基因结构相似,在成熟肽中,氨基端的clip结构域(clip domain)都由37个氨基酸残基组成,六个形成二硫键的保守半胱氨酸的排列顺序与大环卫素的半胱氨酸排列顺序相似。羧基端是典型起催化作用的丝氨酸蛋白酶结构域(Tryp_SPc domain),活性部位催化三联体(H、D、S)和六个形成二硫键的半胱氨酸非常保守。两个结构域之间通过连接区域相连。CFPS1和CFPS2都以酶原形式存在,以类似于胰蛋白酶原激活方式被特异性的蛋白水解酶切。应用Northern blotting方法检测CFPS1和CFPS2基因在不同组织或器官中的表达发现,两个基因都主要在血细胞中表达。用RT-PCR检测CFPS1和CFPS2基因在损伤、不同类型微生物感染后的表达显示,损伤和鳗弧菌感染可以诱导CFPS1基因的表达,在两种刺激后16小时,CFPS1基因表达明显升高; 同样鳗弧菌感染也可以诱导CFPS2基因的表达,感染16小时后,CFPS2基因的表达也明显升高,但溶壁微球菌和巴氏毕赤酵母感染对CFPS2基因的表达差异不显著。
Scallop culture is an important marine aquaculture industry in China. But since 1994, scallop aquaculture in China has been experiencing a continual large-scale mortality, which not only caused a great economic loss but also threatened the existence and development of the culture industry. Although it is still unclear about the causes for the scallop mortality, deterioration water quality and deterioration of the stock are suspected to be the most important causes. With the improvement and control of the marine environment, enhancing the disease resistance of scallop is commonly believed to be the resolution to the control of the disease. The cloning and expression of the genes involved in immune defense are now considered to be a basic solution in the disease control because of their potential use in the development of therapeutic agents, study of immune defense mechanism and genetic improvement to increase the resistance to disease. Serine proteases and their inhibitors play a central role in the invertebrate immune response. They are mainly involved in signaling and amplification cascades that lead to the activation of specific defense mechanisms, such as melanization, coagulation and induction of antimicrobial peptides. In the present study, large scale EST sequencing method together with RACE technique was used to isolate and clone the serine proteases and serine proteases inhibitors involved in the immune defence from scallop cDNA libraries. Nine full length cDNA sequences of immune-related serine proteases and serine protease inhibitors were obtained and the tissue distribution and the temporal expression of these genes after injury and microbe challenge were measured by Northern blotting and RT-PCR.
The full length of serine protease genes CFPS1 and CFPS2 from scallop Chlamys farreri was 1211 and 1152-bp encoded 354 and 336 amino acids, respectively. CFPS1 and CFPS2 are believed to be the secreted protein. They have the typical signal peptide at the N-terminus and the resulting mature CFPS1 and CFPS2 lack transmembrane domains and retention signals. The deduced amino-acid sequences of CFPS1 and CFPS2 consist
of two parts, a regulatory amino-terminal clip domain and a catalytic serine proteinase domain at the carboxyl terminus. A linking sequence connects the two domains. Clip domains are 37 amino acid residue sequences which are knitted together by three disulfide bonds and thus are expected to form a quite compact structure. The CFPS1 and CFPS2 are synthesized as zymogens and are activated by a specific proteolytic cleavage, in a manner similar to the activation of trypsinogen or chymotrypsinogen. The activation site is between the clip domain and the catalytic domain. An additional pair of cysteine residues links the two domains such that when the CFPS1 and CFPS2 are activated, the catalytic heavy chain remains covalently attached by a disulfide bond to the light chain, which contains the clip domain. Northern blotting analyses using CFPS1 and CFPS2 probe confirmed the presence of approximately 1.3-kb transcript for C. farreri that were most strongly expressed within collected hemocytes, respectively. The temporal expression of CFPS1 and CFPS2 were measured by RT-PCR after injury or microbe challenge, respectively. After the adductor was wounded or injected with Vibrio Anguillarum, the mRNA expression of CFPS1 in hemolymph was up-regulated and reached the maximum level at 16 h, respectively. The mRNA expression of CFPS2 in hemolymph also was up-regulated and reached the maximum level at 16 h after injected with V. Anguillarum, but there was no significant difference in CFPS2 gene expression among the control, blank, and challenged samples after M. luteus and P. pastoris challenge, respectively. These results indicated that CFPS1 and CFPS2 could play an important role in injury healing and immune response in mollusks as it could be induced by injury and microbe challenge. The full length of serine protease inhibitor genes CFPSI-1, CFPSI-2, CFPSI-3, CFPSI-4 from scallop C. farreri and AISPI-1, AISPI-2, AISPI-3 from the bay scallop Argopecten irradians was 1841, 1358, 1187 ,1064, 1020, 897 and 642-bp, encoded 508, 347, 364 323, 278, 238 and 153 amino acids, respectively. They are believed to be the secreted protein and have the typical signal peptide at the N-terminus. The deduced amino-acid sequence of CFPSI-1, CFPSI-2, CFPSI-3, CFPSI-4, AISPI-1, AISPI-2 and AISPI-3 contained 12, 8, 8, 7, 6, 5 and 3 tandem and homologous domains similar to that of kazal-type serine protease inhibitors, respectively, including the conserved sequence
C-X(7)-C-X(6)-Y-X(3)-C-X(2,3)-C and 6 cysteine residues responsible for the formation of disulfide bridges, indicating that the CFPSI-1, CFPSI-2, CFPSI-3 and CFPSI-4 protein from scallop C. farreri and AISPI-1, AISPI-2, AISPI-3 from the bay scallop A. irradians should be members of Kazal-type serine protease inhibitor family. Northern blotting analyses using CFPSI-1, CFPSI-2, CFPSI-3, CFPSI-4, AISPI-1、AISPI-2 and AISPI-3 probe confirmed the presence of approximately 1.9, 1.4 1.3 and 1.2-kb transcript for C. farreri and 1.1, 1.0 and 0.7-kb transcript for A. irradians that were most strongly expressed within collected hemocytes, respectively. The temporal expression of CFPSI-1, CFPSI-2, CFPSI-3, CFPSI-4, AISPI-1、AISPI-2 and AISPI-3 was measured by RT-PCR after injury or microbe challenge, respectively. After the adductor was wounded or injected with V. Anguillarum, the mRNA expression of CFPSI-1, CFPSI-2 in hemolymph was down-regulated, respectively. But the mRNA expression of CFPSI-3 and CFPSI-4 in hemolymph was up-regulated and reached the maximum level at 8 h after injected with V. Anguillarum and M. luteus. There was no significant difference in CFPSI-3 and CFPSI-4 gene expression among the control, blank, and challenged samples after P. pastoris challenge. After the adductor was wounded or injected with V. Anguillarum, the mRNA expression of AISPI-1 in hemolymph was up-regulated and reached the maximum level at 8 and 16 h, respectively, and then progressively dropped back to the original level. The mRNA expression of AISPI-2 and AISPI-3 in hemolymph was also up-regulated and reached the maximum level at 4, 6 and 2 h after injected with V. Anguillarum, M. luteus and P. pastoris. These results indicated that CFPSI-1, CFPSI-2, CFPSI-3, CFPSI-4, AISPI-1、AISPI-2 and AISPI-3 could play an important role in injury healing and immune response in mollusks as it could be induced or inhibited by injury and microbe challenge.
丝氨酸蛋白酶及其抑制因子在无脊椎动物的免疫应答中起着核心作用,它们的协同作用不但直接导致免疫信号转导和级联放大,还可激活特异性防御体系,如黑化反应、血液凝结和抗菌肽的合成等。本研究采用大规模EST测序方法,结合cDNA末端快速扩增技术,直接从cDNA文库中分离、克隆了9个扇贝免疫相关的丝氨酸蛋白酶及其抑制剂基因的全长cDNA序列,应用Northern blotting和RT-PCR方法检测了这些基因的组织定位及在损伤和不同类型微生物感染下的表达规律。
栉孔扇贝丝氨酸蛋白酶基因CFPS1和CFPS2的cDNA全长分别为1211-bp和1152-bp,分别编码354和336个氨基酸,均为具有信号肽执行胞外功能的分泌蛋白。两个基因结构相似,在成熟肽中,氨基端的clip结构域(clip domain)都由37个氨基酸残基组成,六个形成二硫键的保守半胱氨酸的排列顺序与大环卫素的半胱氨酸排列顺序相似。羧基端是典型起催化作用的丝氨酸蛋白酶结构域(Tryp_SPc domain),活性部位催化三联体(H、D、S)和六个形成二硫键的半胱氨酸非常保守。两个结构域之间通过连接区域相连。CFPS1和CFPS2都以酶原形式存在,以类似于胰蛋白酶原激活方式被特异性的蛋白水解酶切。应用Northern blotting方法检测CFPS1和CFPS2基因在不同组织或器官中的表达发现,两个基因都主要在血细胞中表达。用RT-PCR检测CFPS1和CFPS2基因在损伤、不同类型微生物感染后的表达显示,损伤和鳗弧菌感染可以诱导CFPS1基因的表达,在两种刺激后16小时,CFPS1基因表达明显升高; 同样鳗弧菌感染也可以诱导CFPS2基因的表达,感染16小时后,CFPS2基因的表达也明显升高,但溶壁微球菌和巴氏毕赤酵母感染对CFPS2基因的表达差异不显著。
Scallop culture is an important marine aquaculture industry in China. But since 1994, scallop aquaculture in China has been experiencing a continual large-scale mortality, which not only caused a great economic loss but also threatened the existence and development of the culture industry. Although it is still unclear about the causes for the scallop mortality, deterioration water quality and deterioration of the stock are suspected to be the most important causes. With the improvement and control of the marine environment, enhancing the disease resistance of scallop is commonly believed to be the resolution to the control of the disease. The cloning and expression of the genes involved in immune defense are now considered to be a basic solution in the disease control because of their potential use in the development of therapeutic agents, study of immune defense mechanism and genetic improvement to increase the resistance to disease. Serine proteases and their inhibitors play a central role in the invertebrate immune response. They are mainly involved in signaling and amplification cascades that lead to the activation of specific defense mechanisms, such as melanization, coagulation and induction of antimicrobial peptides. In the present study, large scale EST sequencing method together with RACE technique was used to isolate and clone the serine proteases and serine proteases inhibitors involved in the immune defence from scallop cDNA libraries. Nine full length cDNA sequences of immune-related serine proteases and serine protease inhibitors were obtained and the tissue distribution and the temporal expression of these genes after injury and microbe challenge were measured by Northern blotting and RT-PCR.
The full length of serine protease genes CFPS1 and CFPS2 from scallop Chlamys farreri was 1211 and 1152-bp encoded 354 and 336 amino acids, respectively. CFPS1 and CFPS2 are believed to be the secreted protein. They have the typical signal peptide at the N-terminus and the resulting mature CFPS1 and CFPS2 lack transmembrane domains and retention signals. The deduced amino-acid sequences of CFPS1 and CFPS2 consist
of two parts, a regulatory amino-terminal clip domain and a catalytic serine proteinase domain at the carboxyl terminus. A linking sequence connects the two domains. Clip domains are 37 amino acid residue sequences which are knitted together by three disulfide bonds and thus are expected to form a quite compact structure. The CFPS1 and CFPS2 are synthesized as zymogens and are activated by a specific proteolytic cleavage, in a manner similar to the activation of trypsinogen or chymotrypsinogen. The activation site is between the clip domain and the catalytic domain. An additional pair of cysteine residues links the two domains such that when the CFPS1 and CFPS2 are activated, the catalytic heavy chain remains covalently attached by a disulfide bond to the light chain, which contains the clip domain. Northern blotting analyses using CFPS1 and CFPS2 probe confirmed the presence of approximately 1.3-kb transcript for C. farreri that were most strongly expressed within collected hemocytes, respectively. The temporal expression of CFPS1 and CFPS2 were measured by RT-PCR after injury or microbe challenge, respectively. After the adductor was wounded or injected with Vibrio Anguillarum, the mRNA expression of CFPS1 in hemolymph was up-regulated and reached the maximum level at 16 h, respectively. The mRNA expression of CFPS2 in hemolymph also was up-regulated and reached the maximum level at 16 h after injected with V. Anguillarum, but there was no significant difference in CFPS2 gene expression among the control, blank, and challenged samples after M. luteus and P. pastoris challenge, respectively. These results indicated that CFPS1 and CFPS2 could play an important role in injury healing and immune response in mollusks as it could be induced by injury and microbe challenge. The full length of serine protease inhibitor genes CFPSI-1, CFPSI-2, CFPSI-3, CFPSI-4 from scallop C. farreri and AISPI-1, AISPI-2, AISPI-3 from the bay scallop Argopecten irradians was 1841, 1358, 1187 ,1064, 1020, 897 and 642-bp, encoded 508, 347, 364 323, 278, 238 and 153 amino acids, respectively. They are believed to be the secreted protein and have the typical signal peptide at the N-terminus. The deduced amino-acid sequence of CFPSI-1, CFPSI-2, CFPSI-3, CFPSI-4, AISPI-1, AISPI-2 and AISPI-3 contained 12, 8, 8, 7, 6, 5 and 3 tandem and homologous domains similar to that of kazal-type serine protease inhibitors, respectively, including the conserved sequence
C-X(7)-C-X(6)-Y-X(3)-C-X(2,3)-C and 6 cysteine residues responsible for the formation of disulfide bridges, indicating that the CFPSI-1, CFPSI-2, CFPSI-3 and CFPSI-4 protein from scallop C. farreri and AISPI-1, AISPI-2, AISPI-3 from the bay scallop A. irradians should be members of Kazal-type serine protease inhibitor family. Northern blotting analyses using CFPSI-1, CFPSI-2, CFPSI-3, CFPSI-4, AISPI-1、AISPI-2 and AISPI-3 probe confirmed the presence of approximately 1.9, 1.4 1.3 and 1.2-kb transcript for C. farreri and 1.1, 1.0 and 0.7-kb transcript for A. irradians that were most strongly expressed within collected hemocytes, respectively. The temporal expression of CFPSI-1, CFPSI-2, CFPSI-3, CFPSI-4, AISPI-1、AISPI-2 and AISPI-3 was measured by RT-PCR after injury or microbe challenge, respectively. After the adductor was wounded or injected with V. Anguillarum, the mRNA expression of CFPSI-1, CFPSI-2 in hemolymph was down-regulated, respectively. But the mRNA expression of CFPSI-3 and CFPSI-4 in hemolymph was up-regulated and reached the maximum level at 8 h after injected with V. Anguillarum and M. luteus. There was no significant difference in CFPSI-3 and CFPSI-4 gene expression among the control, blank, and challenged samples after P. pastoris challenge. After the adductor was wounded or injected with V. Anguillarum, the mRNA expression of AISPI-1 in hemolymph was up-regulated and reached the maximum level at 8 and 16 h, respectively, and then progressively dropped back to the original level. The mRNA expression of AISPI-2 and AISPI-3 in hemolymph was also up-regulated and reached the maximum level at 4, 6 and 2 h after injected with V. Anguillarum, M. luteus and P. pastoris. These results indicated that CFPSI-1, CFPSI-2, CFPSI-3, CFPSI-4, AISPI-1、AISPI-2 and AISPI-3 could play an important role in injury healing and immune response in mollusks as it could be induced or inhibited by injury and microbe challenge.
引文
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