小鼠冠状病毒p28裂解位点的鉴定
Identification of the murine coronavirus p28 cleavage site.
作者信息
Hughes S A, Bonilla P J, Weiss S R
机构信息
Department of Microbiology, University of Pennsylvania School of Medicine, Philadelphia 94104-6076.
出版信息
J Virol. 1995 Feb;69(2):809-13. doi: 10.1128/JVI.69.2.809-813.1995.
Abstract
Mouse hepatitis virus strain A59 encodes a papain-like cysteine proteinase (PLP-1) that, during translation of ORF1a, cleaves p28 from the amino terminus of the growing polypeptide chain. In order to determine the amino acid sequences surrounding the p28 cleavage site, the first 4.6 kb of murine hepatitis virus strain A59 ORF1a was expressed in a cell-free transcription-translation system. Amino-terminal radiosequencing of the resulting downstream cleavage product demonstrated that cleavage occurs between Gly-247 and Val-248. Site-directed mutagenesis of amino acids surrounding the p28 cleavage site revealed that substitutions of Arg-246 (P2) and Gly-247 (P1) nearly eliminated cleavage of p28. Single-amino-acid substitutions of other residues between P7 and P2' were generally permissive for cleavage, although a few changes did greatly reduce proteolysis. The relationship between the p28 cleavage site and other viral and cellular papain proteinase cleavage sites is discussed.
摘要
小鼠肝炎病毒A59株编码一种木瓜蛋白酶样半胱氨酸蛋白酶（PLP-1），在ORF1a翻译过程中，它从正在生长的多肽链的氨基末端切割下p28。为了确定p28切割位点周围的氨基酸序列，在无细胞转录-翻译系统中表达了小鼠肝炎病毒A59株ORF1a的前4.6 kb。对所得下游切割产物进行氨基末端放射性测序表明，切割发生在Gly-247和Val-248之间。对p28切割位点周围氨基酸进行定点诱变发现，Arg-246（P2）和Gly-247（P1）的取代几乎消除了p28的切割。P7和P2'之间其他残基的单氨基酸取代通常允许切割，尽管有一些变化确实大大降低了蛋白水解作用。文中讨论了p28切割位点与其他病毒和细胞木瓜蛋白酶切割位点之间的关系。
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