Biophysics Department, Faculty of Sciences, Cairo University, Giza, Egypt.
College of Applied Medical Sciences, University of Al-Jouf, Al-Jouf, Kingdom of Saudi Arabia.
J Med Virol. 2020 Dec;92(12):3759-3765. doi: 10.1002/jmv.25737. Epub 2020 Mar 11.
Human papillomavirus (HPV) is the main cervical cancer-promoting element that is transmitted through sexual routes. Anal, head, and throat cancers are also reported to be accompanied by HPV infection. E6 is one of the HPV nonstructural proteins, which is responsible for cell differentiation by targeting tumor suppressor genes, p105Rb and p53. E6 was reported to be stabilized by two chaperone proteins; glucose-regulated protein 78 (GRP78) and heat shock protein 90. GRP78 is responsible for the unfolded protein response of the cells, and it was reported to be upregulated in many cancers, including cervical cancer. It was reported that knocking out GRP78 destabilizes E6 leading to faster degradation of E6 in vivo. The current work predicts the possible binding mode between E6 and GRP78 based on sequence and structural similarities.
人乳头瘤病毒（HPV）是主要的宫颈癌促进因素，通过性途径传播。据报道，肛门、头部和咽喉癌也伴随着 HPV 感染。E6 是 HPV 非结构蛋白之一，通过靶向肿瘤抑制基因 p105Rb 和 p53 负责细胞分化。E6 被两种伴侣蛋白稳定；葡萄糖调节蛋白 78（GRP78）和热休克蛋白 90。GRP78 负责细胞的未折叠蛋白反应，据报道在许多癌症中上调，包括宫颈癌。据报道，敲除 GRP78 会使 E6 不稳定，导致 E6 在体内更快降解。目前的工作基于序列和结构相似性预测了 E6 和 GRP78 之间可能的结合模式。
