NUCLEOTIDE-SEQUENCE OF THE GENE ENCODING THE FUSION (F) GLYCOPROTEIN OF HUMAN RESPIRATORY SYNCYTIAL VIRUS

NUCLEOTIDE-SEQUENCE OF THE GENE ENCODING THE FUSION (F) GLYCOPROTEIN OF HUMAN RESPIRATORY SYNCYTIAL VIRUS
复制标题

DOI:
10.1073/pnas.81.24.7683
复制
发表时间:
1984-01-01
期刊:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES
影响因子:
--
通讯作者:
WERTZ, GW
WERTZ, GW
中科院分区:
其他
文献类型:
--
作者:
COLLINS, PL;HUANG, YT;WERTZ, GW

文献摘要

被引文献

相似文献

从含有完整mRNA序列的cDNA [互补DNA]克隆中确定编码呼吸道合胞(RS)病毒(A2株)F蛋白的mRNA的核苷酸序列。mRNA的长度为1899个核苷酸,不包括聚腺苷酸。单个主要开放阅读框编码574个氨基酸的蛋白质,计算的MW为63,453。从氨基酸序列预测的主要结构特征包括NH 2-末端信号序列(残基1-22),疏水跨膜锚序列(残基525-550),5个潜在的天冬酰胺连接的碳水化合物的受体位点,和一个潜在的位点(残基131-136)用于产生二硫键连接的F1和F2亚基的蛋白水解裂解,通过与其它副粘病毒类似,构成F蛋白的生物活性形式。该序列还含有一个内部疏水结构域(残基137-154),作为上述激活蛋白水解切割的结果,该结构域将成为较大F1亚基的NH 2末端。已知F1亚基疏水末端的氨基酸序列在几种副粘病毒中高度保守,但与RS病毒明显不同。F2亚基是相对亲水性的,含有5个潜在的碳水化合物受体位点中的4个。亚基顺序为NH 2-F2-F1-COOH。在迄今为止测序的8种RS病毒mRNA中,5“和3”mRNA末端的核苷酸序列是保守的。保守序列为:**图形 **。这些是病毒转录信号的候选者。所描述的核苷酸和氨基酸序列进一步确定了RS病毒和其他副粘病毒之间的关系。
The nucleotide sequence of the mRNA encoding the F protein of respiratory syncytial (RS) virus (strain A2) was determined from cDNA [complementary DNA] clones that contain the complete mRNA sequence. The mRNA is 1899 nucleotides long exclusive of polyadenylylate. The single major open reading frame encodes a protein of 574 amino acids, with a calculated MW of 63,453. Major structural features predicted from the amino acid sequence include an NH2-terminal signal sequence (residues 1-22), hydrophobic transmembrane anchor sequence (residues 525-550), 5 potential acceptor sites for asparagine-linked carbohydrate, and a potential site (residues 131-136) for the proteolytic cleavage that generates the disulfide-linked F1 and F2 subunits, which, by analogy to other paramyxoviruses, constitute the biologically active form of the F protein. The sequence also contains an internal hydrophobic domain (residues 137-154) that, as a consequence of the activating proteolytic cleavage described above, would become the NH2 terminus of the larger, F1 subunit. The amino acid sequence of the hydrophobic terminus of the F1 subunit is known to be highly conserved among several paramyxoviruses but is markedly dissimilar for RS virus. The F2 subunit is relatively hydrophilic and contains 4 of the 5 potential carbohydrate acceptor sites. The subunit order is NH2-F2-F1-COOH. The nucleotide sequences at the 5'' and 3'' mRNA termini are conserved among the 8 RS viral mRNA sequenced to date. The conserved sequences are: .**GRAPHIC**. These are candidates to be signals for viral transcription. The nucleotide and amino acid sequences described further define the relationship between RS virus and other paramyxoviruses.