THE PREDICTED PRIMARY STRUCTURE OF THE MEASLES-VIRUS HEMAGGLUTININ
THE PREDICTED PRIMARY STRUCTURE OF THE MEASLES-VIRUS HEMAGGLUTININ
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DOI：
10.1016/0042-6822(86)90312-0
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发表时间：
1986-04-30
期刊：
影响因子：
3.7
通讯作者：
BRIEDIS, DJ
中科院分区：
文献类型：
--
作者：
ALKHATIB, G;BRIEDIS, DJ
已确定了与编码麻疹病毒血凝素（H）蛋白的mRNA全长对应的克隆cDNA的完整核苷酸序列。该mRNA含有一个大的开放阅读框，能够编码617个氨基酸的蛋白质，分子量为69，250 Da。推导的蛋白质的氨基酸结构表明，唯一的主要疏水区的长度足够锚的分子在膜位于氨基末端附近。麻疹病毒H蛋白的氨基酸结构与仙台病毒和猴病毒5型（SV 5）的血凝素-神经氨酸酶（HN）分子的氨基酸结构比较显示同源性很小。然而，麻疹H蛋白中发现的13个半胱氨酸残基中的11个可以与仙台病毒HN蛋白中的半胱氨酸在相对于彼此的相似位置上对齐。麻疹H蛋白序列中存在五个潜在的N-连接糖基化位点。这些相对紧密地聚集在分子的氨基末端一半的氨基酸残基168和240之间。麻疹H蛋白氨基酸序列中不存在明显的结构特征，这可能解释了报道的与该分子相关的神经氨酸酶活性的缺失。
The complete nucleotide sequence of cloned cDNAs corresponding to the full length of the mRNA encoding the measles virus hemagglutinin (H) protein has been determined. The mRNA contains a single large open reading frame which is capable of encoding a protein of 617 amino acids with a molecular mass of 69,250 Da. The deduced amino acid structure of the protein indicates that the only major hydrophobic region of sufficient length to anchor the molecule in membranes is located near the amino terminus. Comparison of the amino acid structure of the measles virus H protein with that of the hemagglutinin-neuraminidase (HN) molecules of Sendai virus and simian virus 5 (SV5) reveals little homology. However, 11 of the 13 cysteine residues found in the measles H protein can be aligned with cysteines in the Sendai virus HN protein in similar positions relative to one another. Five potential N-linked glycosylation sites are present in the measles H protein sequence. These are relatively closely grouped between amino acids residues 168 and 240 in the amino terminal half of the molecule. No obvious structural features are present in the measles H protein amino acid sequence which might explain the reported absence of neuraminidase activity associated with the molecule.