Nucleotide sequence of the gene encoding respiratory syncytial virus matrix protein

Nucleotide sequence of the gene encoding respiratory syncytial virus matrix protein
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编码呼吸道合胞病毒基质蛋白的基因的核苷酸序列

DOI:
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发表时间:
1984
影响因子:
5.4
通讯作者:
S. Venkatesan
S. Venkatesan
中科院分区:
医学2区
文献类型:
--
作者:
M. Satake;S. Venkatesan

文献摘要

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人呼吸道合胞病毒(RS病毒)的基质蛋白的氨基酸序列是从含有该基因的几乎全长拷贝的重组质粒中的cDNA插入物的序列推导出来的。它特异性地与来自感染细胞的单个1,050个碱基的mRNA杂交。重组体含有944 bp的RS病毒基质蛋白基因序列,在mRNA的5'端缺少5个核苷酸。用双脱氧测序法测定mRNA 5 ′端的核苷酸序列,发现是5 ′ NGGGC,其中C残基是克隆的病毒序列上游的一个核苷酸。基质蛋白的起始ATG密码子嵌入AATATGG序列中,该序列类似于存在于功能性真核翻译起始密码子周围的典型PXXATGG序列。与水泡性口炎病毒和仙台病毒不同,聚腺苷酸尾上游没有保守序列,其中聚腺苷酸尾上游的四个核苷酸在所有基因中都是保守的。在多聚腺苷酸尾的上游没有真核多聚腺苷酸信号AAUAAA的等价物。基质蛋白分子量为28,717道尔顿,含有256个氨基酸。它是相对碱性和适度疏水性的。在蛋白质的C-末端三分之一处有两簇疏水氨基酸残基,它们可能与感染细胞的膜组分相互作用。RS病毒的基质蛋白与其他负链RNA病毒的基质蛋白没有同源性,表明RS病毒经历了广泛的进化分化。第二个开放的阅读框可能编码75个氨基酸的蛋白质和部分重叠的基质蛋白的C末端也被确定。
The amino acid sequence of the matrix protein of the human respiratory syncytial virus (RS virus) was deduced from the sequence of a cDNA insert in a recombinant plasmid harboring an almost full-length copy of this gene. It specifically hybridized to a single 1,050-base mRNA from infected cells. The recombinant containing 944 base pairs of RS viral matrix protein gene sequence lacked five nucleotides corresponding to the 5' end of the mRNA. The nucleotide sequence of the 5' end of the mRNA was determined by the dideoxy sequencing method and found to be 5' NGGGC, wherein the C residue is one nucleotide upstream of the cloned viral sequence. The initiator ATG codon for the matrix protein is embedded in an AATATGG sequence similar to the canonical PXXATGG sequence present around functional eucaryotic translation initiation codons. There is no conserved sequence upstream of the polyadenylate tail, unlike vesicular stomatitis virus and Sendai virus, in which four nucleotides upstream of the polyadenylate tail are conserved in all genes. There is no equivalent of the eucaryotic polyadenylation signal AAUAAA upstream of the polyadenylate tail. The matrix protein of 28,717 daltons has 256 amino acids. It is relatively basic and moderately hydrophobic. There are two clusters of hydrophobic amino acid residues in the C-terminal third of the protein that could potentially interact with the membrane components of the infected cell. The matrix protein has no homology with the matrix proteins of other negative-strand RNA viruses, implying that RS virus has undergone extensive evolutionary divergence. A second open reading frame potentially encoding a protein of 75 amino acids and partially overlapping the C terminus of the matrix protein was also identified.