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表达的牛冠状病毒血凝素酯酶蛋白的结构与取向

Structure and orientation of expressed bovine coronavirus hemagglutinin-esterase protein.

作者信息

Kienzle T E, Abraham S, Hogue B G, Brian D A

机构信息

Department of Microbiology, University of Tennessee, Knoxville 37996-0845.

出版信息

J Virol. 1990 Apr;64(4):1834-8. doi: 10.1128/JVI.64.4.1834-1838.1990.

DOI:10.1128/JVI.64.4.1834-1838.1990
PMID:2319653
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC249325/
Abstract

The sequence of the hemagglutinin-esterase (HE) gene for the Mebus strain of bovine coronavirus was obtained from cDNA clones, and its deduced product is a 47,700-kilodalton apoprotein of 424 amino acids. Expression of the HE protein in vitro in the presence of microsomes revealed N-terminal signal peptide cleavage and C-terminal anchorage but not disulfide-linked dimerization. Dimerization was observed only after expression in vivo, during which HE was also transported to the cell surface.

摘要

从cDNA克隆中获得了牛冠状病毒梅布斯株血凝素酯酶（HE）基因的序列，其推导产物是一种由424个氨基酸组成的47,700千道尔顿脱辅基蛋白。在微粒体存在的情况下，HE蛋白在体外表达时显示出N端信号肽的切割和C端锚定，但没有二硫键连接的二聚化。只有在体内表达后才观察到二聚化，在此期间HE也被转运到细胞表面。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e71/249325/e09d14e100d4/jvirol00059-0429-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e71/249325/f8a006dfe987/jvirol00059-0428-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e71/249325/e09d14e100d4/jvirol00059-0429-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e71/249325/f8a006dfe987/jvirol00059-0428-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0e71/249325/e09d14e100d4/jvirol00059-0429-a.jpg

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