Human papillomavirus (HPV) infection poses a significant threat to public health worldwide. Targeting the function of HPV E6 and E7 proteins and activating the host immune response against these proteins represent promising therapeutic strategies for combating HPV-related diseases. Consequently, the efficient production of soluble, high-purity E6 and E7 proteins is crucial for function and host immune response studies. In this context, we selected the pMCSG19 protein expression vector for Escherichia coli to produce soluble MBP-His6 tagged HPV11/16 E6/E7 proteins, achieving relatively high purity and yield. Notably, these proteins exhibited low toxicity to peripheral blood mononuclear cells (PBMCs) and did not compromise their viability. Additionally, the recombinant proteins were capable of inducing the secretion of multiple cytokines by immune cells in peripheral blood, indicating their potential to elicit immune responses. In conclusion, our study offers a novel approach for the production of HPV11/16 E6/E7 fusion proteins with relatively high purity and yield. The fusing HPV11/16 E6/E7 proteins to MBP-His6 tag may serve as a valuable method for large-scale protein production in future research endeavors.

中文翻译：

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重组 HPV11/16 E6/E7-MBP-His6 融合蛋白的产生及其诱导外周血中免疫细胞分泌细胞因子的潜力

人乳头瘤病毒（HPV）感染对全世界的公共卫生构成重大威胁。针对 HPV E6 和 E7 蛋白的功能并激活针对这些蛋白的宿主免疫反应代表了对抗 HPV 相关疾病的有前途的治疗策略。因此，有效生产可溶性高纯度 E6 和 E7 蛋白对于功能和宿主免疫反应研究至关重要。在此背景下，我们选择了大肠杆菌的pMCSG19蛋白表达载体来生产可溶性MBP-His6标记的HPV11/16 E6/E7蛋白，获得了相对较高的纯度和产量。值得注意的是，这些蛋白质对外周血单核细胞 (PBMC) 表现出低毒性，并且不会损害其活力。此外，重组蛋白能够诱导外周血中免疫细胞分泌多种细胞因子，这表明它们具有引发免疫反应的潜力。总之，我们的研究提供了一种生产具有相对高纯度和产量的 HPV11/16 E6/E7 融合蛋白的新方法。将 HPV11/16 E6/E7 蛋白融合到 MBP-His6 标签可能会成为未来研究中大规模蛋白生产的一种有价值的方法。