Bovine papillomavirus type 1 alters the processing of host glucose- and calcium-modulated endoplasmic reticulum proteins.

Bovine papillomavirus type 1 alters the processing of host glucose- and calcium-modulated endoplasmic reticulum proteins.
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1 型牛乳头瘤病毒改变宿主葡萄糖和钙调节内质网蛋白的加工。

DOI:
10.1128/jvi.65.7.3481-3488.1991
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发表时间:
1991
影响因子:
5.4
通讯作者:
Young,DA
Young,DA
中科院分区:
医学2区
文献类型:
--
作者:
O'Banion,MK;Young,DA

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我们先前已经鉴定了C127小鼠成纤维细胞中牛乳头瘤病毒1型(BPV-1)的E2开放阅读框(ORF)区诱导的五种蛋白(R. M. Levenson,U. G. Brinckmann,M. K. O'Banion,E. J. Androphy,J. T. Schiller,F.塔巴塔巴伊湖P. Turek,K. Neary,M. T. Chin,T. R.布里克湖T. Chow和D. A. Young,Virology 172:170-179,1989)。通过特异性免疫沉淀,我们发现乳头瘤病毒相关蛋白(pvp 1)是一种高度糖基化的葡萄糖调节蛋白100(grp 100),grp 100是内质网的主要成分。第二组pvps(2、3和4)显示为已经存在于C127细胞中的另一种蛋白质(蛋白质B)的相关前体。基于它们被钙离子载体A23187诱导以及它们在巨大的二维凝胶上的位置,我们已经初步鉴定pvp 2、pvp-3、pvp-4和pvp B是钙调节蛋白55的形式,钙调节蛋白55是内质网的另一种成分(D. R. Macer和G. L. E. Koch,J. Cell Sci. 91:61-70,1988)。BPV-1引起这些变化的机制尚未确定;然而,它不太可能涉及钙水平扰动或转化本身,因为离子载体处理改变了C127细胞中未观察到的BPV的其他蛋白质,并且在携带E2 ORF区域的非转化细胞中发现了乳头瘤病毒相关蛋白。此外,BPV的变化是不相关的grp mRNA水平的增加,发生在离子载体处理的细胞。相反,BPV-1似乎以某种方式阻碍了这些被认为是宿主蛋白质加工和组装的关键调节剂的内质网蛋白的正常加工。
We have previously characterized five proteins induced by the presence of the E2 open reading frame (ORF) region of bovine papillomavirus type 1 (BPV-1) in C127 mouse fibroblasts (R. M. Levenson, U. G. Brinckmann, M. K. O'Banion, E. J. Androphy, J. T. Schiller, F. Tabatabai, L. P. Turek, K. Neary, M. T. Chin, T. R. Broker, L. T. Chow, and D. A. Young, Virology 172:170-179, 1989). By specific immunoprecipitation, we now find that one of the papillomavirus-associated proteins (pvp1) is a highly glycosylated form of glucose-regulated protein 100 (grp100), a major constituent of the endoplasmic reticulum. A second set of pvps (2, 3, and 4) are shown to be related precursors of another protein already present in C127 cells (protein B). Based on their induction by the calcium ionophore A23187 and their positions on giant two-dimensional gels, we have tentatively identified pvp2, -3, and -4 and B as forms of calcium-regulated protein 55, another constituent of the endoplasmic reticulum (D. R. J. Macer and G. L. E. Koch, J. Cell Sci. 91:61-70, 1988). The mechanism by which BPV-1 brings about these changes is not yet defined; however, it is unlikely to involve calcium level perturbations or transformation per se, since ionophore treatment changes other proteins in C127 cells not seen with BPV and the papillomavirus-associated proteins are found in nontransformed cells harboring the E2 ORF region. Furthermore, the BPV changes are not associated with increased grp mRNA levels, as occurs in ionophore-treated cells. Rather, it appears that BPV-1 somehow retards the normal processing of these resident endoplasmic reticulum proteins that are believed to serve as critical regulators of host protein processing and assembly.
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