MATRIX GENES OF MEASLES-VIRUS AND CANINE-DISTEMPER VIRUS - CLONING, NUCLEOTIDE-SEQUENCES, AND DEDUCED AMINO-ACID-SEQUENCES

MATRIX GENES OF MEASLES-VIRUS AND CANINE-DISTEMPER VIRUS - CLONING, NUCLEOTIDE-SEQUENCES, AND DEDUCED AMINO-ACID-SEQUENCES
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DOI:
10.1128/jvi.58.2.408-416.1986
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发表时间:
1986-05-01
影响因子:
5.4
通讯作者:
LAZZARINI, RA
LAZZARINI, RA
中科院分区:
医学2区
文献类型:
--
作者:
BELLINI, WJ;ENGLUND, G;LAZZARINI, RA

文献摘要

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编码麻疹病毒(MV)和犬瘟热病毒(CDV)的基质(M)蛋白的核苷酸序列从完整地含有这些基因的cDNA克隆中确定。在这两种情况下,从核苷酸序列预测了指定335个氨基酸残基的碱性蛋白质的单个开放阅读框。这两种病毒信息都由大约1,450个核苷酸组成,在它们各自的3“端含有400个推定非编码序列的核苷酸。MV和CDV M蛋白编码区核苷酸同源性为67%,氨基酸同源性为76%。在400个核苷酸的尾部序列中仅观察到偶然同源性。MV和CDV的M蛋白序列与仙台病毒报道的序列(B. M. Blumberg,K.罗斯,M。G.西蒙娜湖鲁角Giorgi和D. Kolakofsky,J. Virol,52:656-663; Y.日高、T. Kanda,K. Iwasaki,A. Nomoto,T. Shioda和H. Shibuta,Nucleic Acids Res.12:7965-7973)表明这些M蛋白在分子的羧基末端三分之一处具有最大的同源性。这个共享区域的二级结构分析表明,结构保守,疏水序列,可能与脂质双层相互作用。
The nucleotide sequences encoding the matrix (M) proteins of measles virus (MV) and canine distemper virus (CDV) were determined from cDNA clones containing these genes in their entirety. In both cases, single open reading frames specifying basic proteins of 335 amino acid residues were predicted from the nucleotide sequences. Both viral messages were composed of approximately 1,450 nucleotides and contained 400 nucleotides of presumptive noncoding sequences at their respective 3'' ends. MV and CDV M-protein-coding regions were 67% homologous at the nucleotide level and 76% homologous at the amino acid level. Only chance homology was observed in the 400-nucleotide trailer sequences. Comparisons of the M protein sequences of MV and CDV with the sequence reported for Sendai virus (B. M. Blumberg, K. Rose, M. G. Simona, L. Roux, C. Giorgi, and D. Kolakofsky, J. Virol, 52:656-663; Y. Hidaka, T. Kanda, K. Iwasaki, A. Nomoto, T. Shioda, and H. Shibuta, Nucleic Acids Res. 12:7965-7973) indicated the greatest homology among these M proteins in the carboxyterminal third of the molecule. Secondary-structure analyses of this shared region indicated a structurally conserved, hydrophobic sequence which possibly interacted with the lipid bilayer.