绒山羊和绵羊Izumo1和CD9基因的克隆及其相互作用的初步研究
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摘要
哺乳动物受精是由一系列复杂有序的步骤组成的细胞相互作用过程,最终导致精卵质膜融合形成受精卵。尽管运用基因组学和蛋白质组学技术在精子和卵子上面各鉴定出若干与精卵融合有关的分子,但顶体反应后的精子与卵细胞膜上的受体结合从而引发精卵融合的分子机制尚不清楚。在这些精卵融合候选分子中,只有精子上的免疫球蛋白超家族(IgSF)新成员Izumo1和卵子上的四次跨膜蛋白超家族(TM4SF)成员CD9被基因敲除小鼠证明是精卵融合必需的分子。绵羊和绒山羊是重要的家畜,是羊肉、羊毛和羊绒的主要来源,然而未见关于其Izumo1和CD9的研究报道。由于这一信息对于了解绵羊和绒山羊的生殖和受精调节机制有重要的意义,本研究克隆了绵羊和绒山羊的Izumo1基因组DNA和cDNA以及CD9的cDNA,并且实现了在大肠杆菌中表达,然后制备并纯化了小鼠抗羊Izumo1的腹水多克隆抗体,用纯化的Izumo1抗体研究了Izumo1蛋白在睾丸和精子上的细胞定位。本文还制备了地高辛标记的绒山羊Izumo1 RNA探针,用RNA原位杂交技术检测了Izumo1在睾丸中的转录细胞定位。最后用双分子荧光互补(BiFC)技术初步研究了绒山羊Izumo1和CD9在人肝癌细胞内能否直接相互结合。
本研究克隆的绵羊Izumo1基因长4600 bp,绒山羊Izumo1基因长4598 bp,二者同源性高达99.9%,并与牛、鼠和人Izumo1基因高度同源。将绵羊和绒山羊的Izumo1 DNA和cDNA序列对比分析后发现羊Izumo1有多种选择性剪接形式,其中完整的开放阅读框(ORF)长963 bp,由8个外显子剪接而成,编码320个氨基酸的肽链。该肽链在C端有1个跨膜结构域,胞外有免疫球蛋白样结构域。绒山羊Izumo1 cDNA具有del 69、del 182和del 217三种选择性剪接异构体;绵羊Izumo1 cDNA具有del 69和ins 30两种选择性剪接异构体。所有这4种选择性剪接均是典型的GT-AG内含子剪接,但由于肽链中间缺失或者C端截短,它们都部分或全部失去了免疫球蛋白样结构域。
对羊Izumo1的氨基酸序列进行生物信息学分析显示其在结构上与小鼠Izumo1相似,N端有一个氨基酸1-22组成的信号肽、C末端有一个氨基酸302-319组成的跨膜区,中间有一个氨基酸161-252组成的免疫球蛋白结构域,并在其上有一个潜在的N-糖基化位点(N~(205))。对15种哺乳动物的Izumo1氨基酸序列进行比对分析,发现它们的序列同源性并不太高,尤其是在C末端。但也有一些极为保守的基序,如能形成二硫键桥的LDC和YRC基序、免疫球蛋白样结构域上游的CPNKCG基序、N-糖基化位点上游的GLTDYSFYRVW基序以及绝大部分半胱氨酸残基。这些保守特征可能与Izumo1的功能有关。用Izumo1 cDNA序列进行分子系统发生学研究的结果与形态学分类一致,确认绵羊和绒山羊聚为一支并与牛亲缘关系最近。
绵羊和绒山羊CD9 cDNA克隆均得到1123 bp序列,包含一个681 bp的完整开放阅读框,编码226个氨基酸的肽链。该肽链具有典型的4次跨膜蛋白家族特征。一个N-糖基化位点(N~(50))、4个跨膜区、两个胞外环和一个被公认为4次跨膜蛋白家族标志的CCG基序。绵羊和绒山羊CD9氨基酸序列有99.1%相同,并与牛、鼠和人的CD9高度同源。本研究对26种动物的CD9氨基酸序列进行了比对分析,发现相同科属的动物CD9同源性很高,并且在小胞外环(SEL)上发现了一个前人没注意到的极为保守的LWLR基序。另外本实验还发现前人在小鼠CD9大胞外环(LEL)上鉴定为精卵融合关键的SFQ(173-175aa)基序只存在于小鼠和大鼠CD9中,别的动物的CD9上并没有这个基序;一直被称之为“糖蛋白”的CD9的N-糖基化位点在位置和序列上并不保守,有些动物的CD9甚至没有糖基化位点。这些结果为进一步研究CD9在精卵融合中的功能提供了新的线索。用CD9 cDNA序列进行分子系统发生学研究的结果与形态学分类一致,确认绵羊和绒山羊聚为一支并与牛亲缘关系最近。
本实验在大肠杆菌中表达了绵羊CD9和绒山羊Izumo1重组蛋白,并成功地制作了小鼠抗羊Izumo1腹水多克隆抗体。用自制的抗体进行免疫组化研究显示绒山羊的Izumo1蛋白存在于睾丸精子发生过程中减数分裂各期细胞中,定位于单倍体圆形精细胞的细胞核内,随着精细胞变形,在长形精子中形成窄条状分布,最终转位至成熟精子头部的赤道环上。RNA原位杂交结果显示绒山羊Izumo1基因在初级精母细胞中转录。
BiFC载体BiFC-VC155-CD9和BiFC-VN173-Izumo1共转染Hep-G2细胞后只观察到零星的荧光细胞,不能支持CD9与Izumo1结合的猜想。
Mammalian fertilization consists of an intricate cascade of cell-cell interactions that culminate in the fusion of sperm and egg membranes and formation of a zygote.A number of molecules with putative roles in sperm-oocyte fusion have recently been identified with genomic and proteomic techniques. However,the mechanisms by which acrosome-reacted spermatozoa bind to receptor molecules on the oocyte plasma membrane and the subsequent fusion with the oolemma remain unknown.It has been established in knockout mice that Izumol,a novel member of immunoglobulin superfamily(IgSF) located on the sperm,and CD9,a member of tetraspanin superfamily(TM4SF) located on the oocyte,are crucial for sperm-egg fusion.Sheep and goat are a major source of food,wool and cashmere,but little research on the sperm-egg fusion has been reported in these livestocks.Since the mechanisms of sperm-egg fusion are important for us to understand the regulatory aspects of caprine and ovine fertilization and reproduction,we cloned and characterized the Izumol and CD9 genes in sheep and chashmere goat,and expressed their recombinant proteins in E.coli.To demonstrate the expression pattern of Izumol in testis and its localization in sperms,we generated ascitic polyclonal antibodies against caprine and ovine Izumol proteins and synthesized DIG-tagged Izumol RNA probes in vitro.We also attempted to study the interactions between caprine Izumol and CD9 using BiFC assay in human Hep-G2 cells.
Alignment of the cloned 4600 bp sequence of sheep Izumol gene with the 4598 bp of goat Izumol gene as well as other animals' Izumol gene revealed 99.9% identity between sheep and goat Izumol,and they both share high homology with their counterparts in cattle,mouse,rat and human.Extensive cDNA cloning captured a canonical open reading frame(ORF) of 963 bp which made of eight exons and three(del 69,del 182 and del 217) alternative splicing isoforms in goat and two(del 69 and ins 30) in sheep Izumol.Bioinformatics analysis showed that the canonical caprine and ovine Izumol cDNA both encode a peptide of 320amino acides(aa) which shares similar structure with their murine orthologue in a feature that there are a signal peptide at the N-terminus(1-22aa),a transmembrane domain at the C-terminus(302-319aa),and an extracellular immunoglobulin-like(Ig-like) region with a putative N-linked glycosylation site(N~(205)-N-S) in the middle (161-252aa).All of those isoforms are derived from alternative splicing at the typical GT-AG sites resulting in the Ig-like domain partially truncated or completely deleted.
Alignment of Izumol protein sequences among 15mammalian species displayed several highly conserved regions,including LDC and YRC motifs with cysteine residues for potential disulfide bridge formation,CPNKCG motif upstream of the Ig-like domain,GLTDYSFYRVW motif upstream of the putative N-linked glycosylation site,and a number of scattered cysteine residues.These conservation features are very informative to pinpoint the key motifs related to Izumol function. The C-terminal regions,however,are more variable across species.The molecular phylogenetic tree constructed using Izumol cDNA sequences is consistent with their morphological taxonomy,for which sheep and goat are in the same cluster and are closely related to cattle.
We also cloned CD9 cDNA of 1.1kb in length from sheep and cashmere goat. Both of them have an ORF of 681 bp encoding a predicted protein of 226 amino acids with a typical TM4SF structure.The deduced peptide consists of a putative N-linked glycosylation site(N-X-S/T)(N~(50)),four transmembrane domains,two extracellular domains and a CCG motif which is a hallmark of the TM4SF.The sheep and goat CD9 proteins share 99.1%identity and are highly homologous to their orthologues in cattle,mouse and human.Alignment of CD9 protein sequences among 26 mammalian species revealed extensive homologies within the same family and a highly conserved LWLR motif in the small extracellular loop(SEL) in all species.The SFQ(173-175) motif within the large extracellular loop(LEL), which was reported as a key motif for mediating sperm-egg fusion,is found only in mouse and rat.Although CD9 is generally annotated as a glycoprotein,we found that the N-linked glycosylation sites are missing in some species and are thus less conserved as expected.These results present new clues for CD9's function in sperm-egg fusion.Molecular phylogenetic analysis based on CD9 cDNA sequences indicated that goat and sheep are closely related to cattle,which is consistent with their morphological taxonomy.
We expressed the recombinant sheep CD9 and goat Izumol proteins in E.coli and succeeded in generating ascitic polyclonal antibodies against the goat Izumol protein.Immunohistochemical analysis showed that Izumol proteins present in the meiotic male germ cells and are stored in the nucleus.Concomitant with spermatid maturation,Izumol proteins contract to a narrow area in elongated spermatids and finally concentrate in the equatorial segment of the mature sperm head where sperm-egg fusion is initiated.RNA in situ hybridization analysis with DIG-tagged anti-sense Izumol riboprobes indicated that the goat Izumol gene is mainly transcribed in the primary spermatocytes.
Finally,we constructed BiFC expression vectors BiFC-VC155-CD9 and BiFC-VN173-Izumol and transiently cotransfected them into human hepatocellular line Hep-G2 to examine the binding ability of Izumol to CD9 in cytoplasm. However,that only a small number of fluorescent cells were observed was not conclusive for the binding activity between caprine CD9 and Izumol proteins.
本研究克隆的绵羊Izumo1基因长4600 bp,绒山羊Izumo1基因长4598 bp,二者同源性高达99.9%,并与牛、鼠和人Izumo1基因高度同源。将绵羊和绒山羊的Izumo1 DNA和cDNA序列对比分析后发现羊Izumo1有多种选择性剪接形式,其中完整的开放阅读框(ORF)长963 bp,由8个外显子剪接而成,编码320个氨基酸的肽链。该肽链在C端有1个跨膜结构域,胞外有免疫球蛋白样结构域。绒山羊Izumo1 cDNA具有del 69、del 182和del 217三种选择性剪接异构体;绵羊Izumo1 cDNA具有del 69和ins 30两种选择性剪接异构体。所有这4种选择性剪接均是典型的GT-AG内含子剪接,但由于肽链中间缺失或者C端截短,它们都部分或全部失去了免疫球蛋白样结构域。
对羊Izumo1的氨基酸序列进行生物信息学分析显示其在结构上与小鼠Izumo1相似,N端有一个氨基酸1-22组成的信号肽、C末端有一个氨基酸302-319组成的跨膜区,中间有一个氨基酸161-252组成的免疫球蛋白结构域,并在其上有一个潜在的N-糖基化位点(N~(205))。对15种哺乳动物的Izumo1氨基酸序列进行比对分析,发现它们的序列同源性并不太高,尤其是在C末端。但也有一些极为保守的基序,如能形成二硫键桥的LDC和YRC基序、免疫球蛋白样结构域上游的CPNKCG基序、N-糖基化位点上游的GLTDYSFYRVW基序以及绝大部分半胱氨酸残基。这些保守特征可能与Izumo1的功能有关。用Izumo1 cDNA序列进行分子系统发生学研究的结果与形态学分类一致,确认绵羊和绒山羊聚为一支并与牛亲缘关系最近。
绵羊和绒山羊CD9 cDNA克隆均得到1123 bp序列,包含一个681 bp的完整开放阅读框,编码226个氨基酸的肽链。该肽链具有典型的4次跨膜蛋白家族特征。一个N-糖基化位点(N~(50))、4个跨膜区、两个胞外环和一个被公认为4次跨膜蛋白家族标志的CCG基序。绵羊和绒山羊CD9氨基酸序列有99.1%相同,并与牛、鼠和人的CD9高度同源。本研究对26种动物的CD9氨基酸序列进行了比对分析,发现相同科属的动物CD9同源性很高,并且在小胞外环(SEL)上发现了一个前人没注意到的极为保守的LWLR基序。另外本实验还发现前人在小鼠CD9大胞外环(LEL)上鉴定为精卵融合关键的SFQ(173-175aa)基序只存在于小鼠和大鼠CD9中,别的动物的CD9上并没有这个基序;一直被称之为“糖蛋白”的CD9的N-糖基化位点在位置和序列上并不保守,有些动物的CD9甚至没有糖基化位点。这些结果为进一步研究CD9在精卵融合中的功能提供了新的线索。用CD9 cDNA序列进行分子系统发生学研究的结果与形态学分类一致,确认绵羊和绒山羊聚为一支并与牛亲缘关系最近。
本实验在大肠杆菌中表达了绵羊CD9和绒山羊Izumo1重组蛋白,并成功地制作了小鼠抗羊Izumo1腹水多克隆抗体。用自制的抗体进行免疫组化研究显示绒山羊的Izumo1蛋白存在于睾丸精子发生过程中减数分裂各期细胞中,定位于单倍体圆形精细胞的细胞核内,随着精细胞变形,在长形精子中形成窄条状分布,最终转位至成熟精子头部的赤道环上。RNA原位杂交结果显示绒山羊Izumo1基因在初级精母细胞中转录。
BiFC载体BiFC-VC155-CD9和BiFC-VN173-Izumo1共转染Hep-G2细胞后只观察到零星的荧光细胞,不能支持CD9与Izumo1结合的猜想。
Mammalian fertilization consists of an intricate cascade of cell-cell interactions that culminate in the fusion of sperm and egg membranes and formation of a zygote.A number of molecules with putative roles in sperm-oocyte fusion have recently been identified with genomic and proteomic techniques. However,the mechanisms by which acrosome-reacted spermatozoa bind to receptor molecules on the oocyte plasma membrane and the subsequent fusion with the oolemma remain unknown.It has been established in knockout mice that Izumol,a novel member of immunoglobulin superfamily(IgSF) located on the sperm,and CD9,a member of tetraspanin superfamily(TM4SF) located on the oocyte,are crucial for sperm-egg fusion.Sheep and goat are a major source of food,wool and cashmere,but little research on the sperm-egg fusion has been reported in these livestocks.Since the mechanisms of sperm-egg fusion are important for us to understand the regulatory aspects of caprine and ovine fertilization and reproduction,we cloned and characterized the Izumol and CD9 genes in sheep and chashmere goat,and expressed their recombinant proteins in E.coli.To demonstrate the expression pattern of Izumol in testis and its localization in sperms,we generated ascitic polyclonal antibodies against caprine and ovine Izumol proteins and synthesized DIG-tagged Izumol RNA probes in vitro.We also attempted to study the interactions between caprine Izumol and CD9 using BiFC assay in human Hep-G2 cells.
Alignment of the cloned 4600 bp sequence of sheep Izumol gene with the 4598 bp of goat Izumol gene as well as other animals' Izumol gene revealed 99.9% identity between sheep and goat Izumol,and they both share high homology with their counterparts in cattle,mouse,rat and human.Extensive cDNA cloning captured a canonical open reading frame(ORF) of 963 bp which made of eight exons and three(del 69,del 182 and del 217) alternative splicing isoforms in goat and two(del 69 and ins 30) in sheep Izumol.Bioinformatics analysis showed that the canonical caprine and ovine Izumol cDNA both encode a peptide of 320amino acides(aa) which shares similar structure with their murine orthologue in a feature that there are a signal peptide at the N-terminus(1-22aa),a transmembrane domain at the C-terminus(302-319aa),and an extracellular immunoglobulin-like(Ig-like) region with a putative N-linked glycosylation site(N~(205)-N-S) in the middle (161-252aa).All of those isoforms are derived from alternative splicing at the typical GT-AG sites resulting in the Ig-like domain partially truncated or completely deleted.
Alignment of Izumol protein sequences among 15mammalian species displayed several highly conserved regions,including LDC and YRC motifs with cysteine residues for potential disulfide bridge formation,CPNKCG motif upstream of the Ig-like domain,GLTDYSFYRVW motif upstream of the putative N-linked glycosylation site,and a number of scattered cysteine residues.These conservation features are very informative to pinpoint the key motifs related to Izumol function. The C-terminal regions,however,are more variable across species.The molecular phylogenetic tree constructed using Izumol cDNA sequences is consistent with their morphological taxonomy,for which sheep and goat are in the same cluster and are closely related to cattle.
We also cloned CD9 cDNA of 1.1kb in length from sheep and cashmere goat. Both of them have an ORF of 681 bp encoding a predicted protein of 226 amino acids with a typical TM4SF structure.The deduced peptide consists of a putative N-linked glycosylation site(N-X-S/T)(N~(50)),four transmembrane domains,two extracellular domains and a CCG motif which is a hallmark of the TM4SF.The sheep and goat CD9 proteins share 99.1%identity and are highly homologous to their orthologues in cattle,mouse and human.Alignment of CD9 protein sequences among 26 mammalian species revealed extensive homologies within the same family and a highly conserved LWLR motif in the small extracellular loop(SEL) in all species.The SFQ(173-175) motif within the large extracellular loop(LEL), which was reported as a key motif for mediating sperm-egg fusion,is found only in mouse and rat.Although CD9 is generally annotated as a glycoprotein,we found that the N-linked glycosylation sites are missing in some species and are thus less conserved as expected.These results present new clues for CD9's function in sperm-egg fusion.Molecular phylogenetic analysis based on CD9 cDNA sequences indicated that goat and sheep are closely related to cattle,which is consistent with their morphological taxonomy.
We expressed the recombinant sheep CD9 and goat Izumol proteins in E.coli and succeeded in generating ascitic polyclonal antibodies against the goat Izumol protein.Immunohistochemical analysis showed that Izumol proteins present in the meiotic male germ cells and are stored in the nucleus.Concomitant with spermatid maturation,Izumol proteins contract to a narrow area in elongated spermatids and finally concentrate in the equatorial segment of the mature sperm head where sperm-egg fusion is initiated.RNA in situ hybridization analysis with DIG-tagged anti-sense Izumol riboprobes indicated that the goat Izumol gene is mainly transcribed in the primary spermatocytes.
Finally,we constructed BiFC expression vectors BiFC-VC155-CD9 and BiFC-VN173-Izumol and transiently cotransfected them into human hepatocellular line Hep-G2 to examine the binding ability of Izumol to CD9 in cytoplasm. However,that only a small number of fluorescent cells were observed was not conclusive for the binding activity between caprine CD9 and Izumol proteins.
引文
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