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新城疫病毒糖蛋白在无糖基化情况下的合成、稳定性及裂解

Synthesis, stability, and cleavage of Newcastle disease virus glycoproteins in the absence of glycosylation.

作者信息

Morrison T G, Simpson D

出版信息

J Virol. 1980 Oct;36(1):171-80. doi: 10.1128/JVI.36.1.171-180.1980.

DOI:10.1128/JVI.36.1.171-180.1980
PMID:7441820
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC353628/
Abstract

Polypeptides synthesized in Newcastle disease virus (NDV)-infected CHO cells in the absence of glycosylation were characterized. Incorporation of either [3H]mannose of [3H]glucosamine into NDV polypeptides was inhibited to greater than 99% by the antibiotic tunicamycin. Under these conditions, infected cells synthesized proteins which comigrated on polyacrylamide gels with the viral L protein, nucleocapsid protein, membrane protein, and a polypeptide with a molecular weight of 55,000 (P55). These cells did not synthesize polypeptides with the size of the hemagglutinin-neuraminidase (HN) protein or the fusion (F0) protein. They did, however, synthesize new polypeptides with molecular weights of 75,000 (P75), 67,000 (P67), and 52,000 (P52). Peptide analysis revealed that P75 was a host cell protein whose synthesis is enhanced by tunicamycin. P67 corresponded to the unglycosylated forms of the glycoproteins were found to be relatively stable in infected cells. P55, previously thought to correspond to the cleaved form of F0, was found to be a unique viral protein which is associated with intracellular nucleocapsid structures.

摘要

对在新城疫病毒(NDV)感染的缺乏糖基化的中国仓鼠卵巢(CHO)细胞中合成的多肽进行了表征。抗生素衣霉素将[³H]甘露糖或[³H]葡糖胺掺入NDV多肽的比例抑制到99%以上。在这些条件下,受感染的细胞合成的蛋白质在聚丙烯酰胺凝胶上与病毒L蛋白、核衣壳蛋白、膜蛋白以及分子量为55,000的多肽(P55)迁移率相同。这些细胞没有合成血凝素神经氨酸酶(HN)蛋白或融合(F0)蛋白大小的多肽。然而,它们确实合成了分子量为75,000(P75)、67,000(P67)和52,000(P52)的新多肽。肽分析表明,P75是一种宿主细胞蛋白,其合成受衣霉素增强。P67对应于糖蛋白的未糖基化形式,发现在受感染细胞中相对稳定。P55以前被认为对应于F0的裂解形式,现发现是一种与细胞内核衣壳结构相关的独特病毒蛋白。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18ea/353628/025fbd988987/jvirol00178-0187-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18ea/353628/c244045e52c4/jvirol00178-0183-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18ea/353628/db93064ef6c3/jvirol00178-0186-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18ea/353628/025fbd988987/jvirol00178-0187-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18ea/353628/c244045e52c4/jvirol00178-0183-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18ea/353628/db93064ef6c3/jvirol00178-0186-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/18ea/353628/025fbd988987/jvirol00178-0187-a.jpg

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引用本文的文献

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本文引用的文献

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Cleavage of structural proteins during the assembly of the head of bacteriophage T4.在噬菌体T4头部组装过程中结构蛋白的切割
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Biochemical study of the Feline Herpesvirus 1. Identification of glycoproteins by affinity.猫疱疹病毒1型的生化研究。通过亲和法鉴定糖蛋白。
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