Genetic definition of a new bovine papillomavirus type 1 open reading frame, E5B, that encodes a hydrophobic protein involved in altering host-cell protein processing.
Genetic definition of a new bovine papillomavirus type 1 open reading frame, E5B, that encodes a hydrophobic protein involved in altering host-cell protein processing.
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一种新的 1 型牛乳头瘤病毒开放阅读框 E5B 的遗传定义，它编码参与改变宿主细胞蛋白质加工的疏水蛋白。
DOI：
10.1128/jvi.67.6.3427-3434.1993
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发表时间：
1993
影响因子：
5.4
通讯作者：
Young,DA
中科院分区：
文献类型：
--
作者：
O'Banion,MK;Winn,VD;Settleman,J;Young,DA
我们之前观察到，牛乳头瘤病毒1型（BPV-1）诱导C127小鼠成纤维细胞中出现5种细胞蛋白，其中4种似乎是通过改变内质网蛋白的加工而产生的。对多种细胞系的研究表明，BPV早期区域3'端的表达足以诱导这些变化。为了确定BPV基因，我们使用了猴病毒40 (SV40)/BPV-1重组病毒Pava-1，该病毒在SV40早期启动子后面表达BPV早期区域的3'端。感染Pava-1 48小时的C127细胞显示出预期的bpv相关改变，感染Pava构建体的细胞在E5或E2基因中发生突变。然而，先前被忽略的开放阅读框（从核苷酸4013延伸到4170 (E5B)）的开始密码子突变消除了bpv相关的变化。用Pava突变体感染的COS细胞和全长突变BPV转化的C127细胞获得了类似的结果。尽管影响了细胞内质网蛋白的加工，但E5B的突变并未改变bpv的转化效率或转化子在软琼脂中形成菌落的能力。E5B开放阅读框编码一个疏水52氨基酸多肽，与HPV6 E5A和HPV16 E5具有结构相似性。对E5B在病毒生命周期中的作用进行了推测。
We have previously observed that bovine papillomavirus type 1 (BPV-1) induces the appearance of five cellular proteins in C127 mouse fibroblasts, four of which appear to arise by altered processing of resident endoplasmic reticulum proteins. Studies of various cell lines revealed that expression of the 3' end of the BPV early region was sufficient for induction of these changes. To identify the BPV gene responsible, we have utilized the simian virus 40 (SV40)/BPV-1 recombinant virus Pava-1, which expresses the 3' end of the BPV early region behind an SV40 early promoter. C127 cells infected with Pava-1 for 48 h show the expected BPV-associated alterations, as do cells infected with Pava constructs mutated in the E5 or E2 genes. However, a mutation in the start codon of a previously ignored open reading frame extending from nucleotides 4013 to 4170 (E5B) eliminated the BPV-associated changes. Similar results were obtained with COS cells infected with the Pava mutants and C127 cells transformed by full-length mutated BPV. Despite its influence on the processing of cellular endoplasmic reticulum proteins, this mutation in E5B did not alter BPV-transforming efficiency or the ability of transformants to form colonies in soft agar. The E5B open reading frame encodes a hydrophobic 52-amino-acid polypeptide that shares structural similarities with HPV6 E5A and HPV16 E5. Speculations on a role for E5B in the viral life cycle are discussed.