Oetke C, Auvinen E, Pawlita M, Alonso A
Angewandte Tumorvirologie, Deutsches Krebsforschungszentrum, Heidelberg, Germany.
Arch Virol. 2000;145(10):2183-91. doi: 10.1007/s007050070048.
The E5 protein of papillomaviruses is a strongly hydrophobic membrane protein that can associate with the 16 kDa protein subunit of the vacuolar proton ATPase in endosomes and the Golgi apparatus resulting in raise of intraorganelle pH. We demonstrate that E5 of human papillomavirus type 16 (HPV16) when transfected into human keratinocytes localizes to the Golgi. Using FACS analysis and western blotting with a variety of lectins as well as analysing the sialylation status of a specific cell surface glycoprotein CD95 (APO-1/Fas), we show that HPV16 E5 does not grossly affect cellular glycosylation, a main Golgi function.
乳头瘤病毒的E5蛋白是一种强疏水性膜蛋白，它可与内体和高尔基体中液泡质子ATP酶的16 kDa蛋白亚基结合，从而导致细胞器内pH值升高。我们证明，人乳头瘤病毒16型（HPV16）的E5转染到人角质形成细胞后定位于高尔基体。通过流式细胞术分析、使用多种凝集素进行蛋白质印迹以及分析特定细胞表面糖蛋白CD95（APO-1/Fas）的唾液酸化状态，我们发现HPV16 E5不会严重影响细胞糖基化这一主要的高尔基体功能。
