小球藻病毒PBCV-1及其抗原变体中的蛋白质糖基化和豆蔻酰化作用

Protein glycosylation and myristylation in Chlorella virus PBCV-1 and its antigenic variants.

作者信息

Que Q, Li Y, Wang I N, Lane L C, Chaney W G, Van Etten J L

机构信息

Department of Plant Pathology, University of Nebraska, Lincoln 68583-0722.

出版信息

Virology. 1994 Sep;203(2):320-7. doi: 10.1006/viro.1994.1490.

DOI:10.1006/viro.1994.1490

PMID:8053156

Abstract

Chlorella virus PBCV-1 particles contain three glycoproteins, the major capsid protein Vp54 and two minor proteins Vp280 and Vp260. The major capsid protein is myristylated as well as glycosylated. Both modifications are in the carboxyl-terminal portion of the protein. A gene which is modified in a PBCV-1 antiserum-resistant mutant was cloned and sequenced. This gene has an open reading frame of 3099 bases and encodes one of the two large virion glycoproteins (Vp260). Vp260 contains 13 tandem repeats of 61 to 65 amino acids. The mutation deletes the equivalent of four of the amino acid repeat sequences and duplicates one of these sequences.

摘要

小球藻病毒PBCV-1颗粒含有三种糖蛋白，主要衣壳蛋白Vp54以及两种次要蛋白Vp280和Vp260。主要衣壳蛋白既进行了肉豆蔻酰化修饰，也进行了糖基化修饰。这两种修饰都在该蛋白的羧基末端部分。克隆并测序了一个在PBCV-1抗血清抗性突变体中发生修饰的基因。该基因有一个3099个碱基的开放阅读框，编码两种大型病毒体糖蛋白之一（Vp260）。Vp260含有13个由61至65个氨基酸组成的串联重复序列。该突变缺失了相当于四个氨基酸重复序列，并重复了其中一个序列。