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腮腺炎病毒融合蛋白mRNA序列及副黏病毒科蛋白质间的同源性。

The mumps virus fusion protein mRNA sequence and homology among the paramyxoviridae proteins.

作者信息

Elango N, Varsanyi T M, Kövamees J, Norrby E

机构信息

Department of Virology, School of Medicine, Karolinska Institute, Stockholm, Sweden.

出版信息

J Gen Virol. 1989 Apr;70 ( Pt 4):801-7. doi: 10.1099/0022-1317-70-4-801.

Abstract

The complete nucleotide sequence of the fusion protein (F) mRNA of the virulent SBL-1 strain of mumps virus has been determined by sequencing cDNA clones and mRNA and confirmed by partially sequencing the genomic RNA. The mRNA was 1721 nucleotides long excluding the poly(A) sequence and had one long open reading frame which encoded a protein of 538 amino acids with a calculated Mr of 58,791. The predicted amino acid sequence had a proteolytic cleavage/activation site, Arg Arg His Lys Arg, cleavage at which yields proteins F2 and F1. The uncleaved protein contained three highly hydrophobic regions: (i) the amino-terminal signal peptide, (ii) the amino-terminal region of F1 and (iii) the carboxy-terminal membrane anchorage domain. There were seven potential N-glycosylation sites, two in F2 and five in F1. Comparison of the virulent strain F protein sequence with that of an avirulent strain of mumps virus showed a difference of 14 amino acids. Among paramyxoviruses, mumps virus fusion protein shows the highest degree of homology with the fusion proteins of simian virus 5 and Newcastle disease virus.

摘要

通过对腮腺炎病毒强毒株SBL-1的融合蛋白(F)mRNA的cDNA克隆和mRNA进行测序,并对基因组RNA进行部分测序,确定了其完整的核苷酸序列。该mRNA长度为1721个核苷酸(不包括聚腺苷酸序列),有一个长的开放阅读框,编码一个538个氨基酸的蛋白质,计算分子量为58791。预测的氨基酸序列有一个蛋白水解切割/激活位点,即精氨酸-精氨酸-组氨酸-赖氨酸-精氨酸,在此处切割产生F2和F1蛋白。未切割的蛋白包含三个高度疏水区域:(i)氨基末端信号肽,(ii)F1的氨基末端区域,以及(iii)羧基末端膜锚定结构域。有七个潜在的N-糖基化位点,其中两个在F2中,五个在F1中。将强毒株F蛋白序列与腮腺炎病毒无毒株的序列进行比较,发现有14个氨基酸的差异。在副粘病毒中,腮腺炎病毒融合蛋白与猴病毒5和新城疫病毒的融合蛋白具有最高程度的同源性。

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