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欧洲防风黄点病毒多聚蛋白的序列分析:与小RNA病毒亲缘关系的证据

Sequence analysis of the parsnip yellow fleck virus polyprotein: evidence of affinities with picornaviruses.

作者信息

Turnbull-Ross A D, Mayo M A, Reavy B, Murant A F

机构信息

Scottish Crop Research Institute, Invergowrie, Dundee, U.K.

出版信息

J Gen Virol. 1993 Apr;74 ( Pt 4):555-61. doi: 10.1099/0022-1317-74-4-555.

Abstract

The 9.9 kb monopartite ssRNA genome of parsnip yellow fleck virus (PYFV) encodes a polyprotein from which the functional proteins are assumed to arise by proteolytic cleavage. The 22.5K, 26K and 31K particle proteins were mapped in the polyprotein by determining their N-terminal amino acid sequences, and were found to begin at amino acid positions 395, 589 and 811, respectively. There could be polypeptide(s) of up to 43K on the N-terminal side of the particle protein sequences. A region within the 26K particle protein has sequence similarity to the VP3 particle protein of picornaviruses. Three other regions in the PYFV polyprotein have sequence similarity to regions thought to have RNA polymerase, NTP-binding and protease functions in the polyproteins of picornaviruses, comoviruses and nepoviruses. Despite these similarities in sequence and in genome organization to viruses in the picorna-like supergroup, PYFV is distinct from all other plant and animal viruses described. This justifies placing it in a separate plant virus genus for which the name 'sequivirus' has been proposed.

摘要

欧洲防风黄点病毒(PYFV)的9.9 kb单分体ssRNA基因组编码一种多聚蛋白,据推测功能性蛋白通过蛋白水解切割产生。通过确定其N端氨基酸序列,在多聚蛋白中定位了22.5K、26K和31K的病毒粒子蛋白,发现它们分别从氨基酸位置395、589和811开始。在病毒粒子蛋白序列的N端一侧可能存在大小达43K的多肽。26K病毒粒子蛋白内的一个区域与小RNA病毒的VP3病毒粒子蛋白具有序列相似性。PYFV多聚蛋白中的其他三个区域与小RNA病毒、豇豆花叶病毒和线虫传多面体病毒的多聚蛋白中被认为具有RNA聚合酶、NTP结合和蛋白酶功能的区域具有序列相似性。尽管在序列和基因组组织上与类小RNA病毒超群中的病毒存在这些相似性,但PYFV与所有其他已描述的动植物病毒不同。这证明将其置于一个单独的植物病毒属是合理的,已有人提议将该属命名为“序列病毒属”。

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