THE HUMAN PAPILLOMAVIRUS TYPE-6 AND 16-E5 PROTEINS ARE MEMBRANE-ASSOCIATED PROTEINS WHICH ASSOCIATE WITH THE 16-KILODALTON PORE-FORMING PROTEIN
THE HUMAN PAPILLOMAVIRUS TYPE-6 AND 16-E5 PROTEINS ARE MEMBRANE-ASSOCIATED PROTEINS WHICH ASSOCIATE WITH THE 16-KILODALTON PORE-FORMING PROTEIN
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DOI：
10.1128/jvi.67.10.6170-6178.1993
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发表时间：
1993-10-01
影响因子：
5.4
通讯作者：
SCHLEGEL, R
中科院分区：
文献类型：
--
作者：
CONRAD, M;BUBB, VJ;SCHLEGEL, R
DNA序列分析预测人乳头瘤病毒(HPV)E5蛋白为疏水小分子，HPV-6(HPV-6)和HPV-11 E5蛋白与牛乳头瘤病毒1型(BPV-1)E5蛋白在结构上有许多相似之处。同样类似于BPV-1E5蛋白，HPV-6和HPV-16E5蛋白在NIH 3T3和C127细胞上检测时显示出转化活性。在这项研究中，我们表达了低危型HPV-6和高危型HPV-16的表位标记的E5蛋白，以便进行免疫学鉴定和生化特性研究。虽然HPV-6和HPV-16E5蛋白不能形成二硫键连接的二聚体和寡聚体，但它们在细胞内定位于高尔基体、内质网和核膜方面与BPV-1E5蛋白相似。此外，HPV E5蛋白还与空泡ATPase的16 kDa成孔蛋白成分结合，这是BPV-1 E5蛋白的已知特征。这些研究揭示了BPV和HPVE5蛋白的共同的膜内定位和潜在的细胞蛋白靶标。
The human papillomavirus (HPV) E5 proteins are predicted from DNA sequence analysis to be small hydrophobic molecules, and the HPV type 6 (HPV-6) and HPV-11 E5 proteins share several structural similarities with the bovine papillomavirus type 1 (BPV-1) E5 protein. Also similar to the BPV-1 E5 protein, the HPV-6 and HPV-16 E5 proteins exhibit transforming activity when assayed on NIH 3T3 and C127 cells. In this study, we expressed epitope-tagged E5 proteins from both the ''low-risk'' HPV-6 and the ''high-risk'' HPV-16 in order to permit their immunologic identification and biochemical characterization. While the HPV-6 and HPV-16 E5 proteins fail to form disulfide-linked dimers and oligomers, they did resemble the BPV-1 E5 protein in their intracellular localization to the Golgi apparatus, endoplasmic reticulum, and nuclear membranes. In addition, the HPV E5 proteins also bound to the 16-kDa pore-forming protein component of the vacuolar ATPase, a known characteristic of the BPV-1 E5 protein. These studies reveal a common intramembrane localization and potential cellular protein target for both the BPV and HPV E5 proteins.