Production of recombinant HPV11/16 E6/E7-MBP-His6 fusion proteins and their potential to induce cytokine secretion by immune cells in peripheral blood
Abstract 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. Conseque...
| Main Authors: | , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
BMC
2024-01-01
|
| Series: | Virology Journal |
| Subjects: | |
| Online Access: | https://doi.org/10.1186/s12985-023-02281-y |
| _version_ | 1797363683951640576 |
|---|---|
| author | Mei-nian Xu Mei-zhen Zhong Si-ning Feng Yan-qin Xu Xiao-ming Peng Kang Zeng Xiao-wen Huang |
| author_facet | Mei-nian Xu Mei-zhen Zhong Si-ning Feng Yan-qin Xu Xiao-ming Peng Kang Zeng Xiao-wen Huang |
| author_sort | Mei-nian Xu |
| collection | DOAJ |
| description | Abstract 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. |
| first_indexed | 2024-03-08T16:24:30Z |
| format | Article |
| id | doaj.art-a4e71e3abd0243c1a584207dd6f25cd9 |
| institution | Directory Open Access Journal |
| issn | 1743-422X |
| language | English |
| last_indexed | 2024-03-08T16:24:30Z |
| publishDate | 2024-01-01 |
| publisher | BMC |
| record_format | Article |
| series | Virology Journal |
| spelling | doaj.art-a4e71e3abd0243c1a584207dd6f25cd92024-01-07T12:11:09ZengBMCVirology Journal1743-422X2024-01-0121111110.1186/s12985-023-02281-yProduction of recombinant HPV11/16 E6/E7-MBP-His6 fusion proteins and their potential to induce cytokine secretion by immune cells in peripheral bloodMei-nian Xu0Mei-zhen Zhong1Si-ning Feng2Yan-qin Xu3Xiao-ming Peng4Kang Zeng5Xiao-wen Huang6Department of Dermatology, Nanfang Hospital, Southern Medical UniversityDepartment of Dermatology, Nanfang Hospital, Southern Medical UniversityDepartment of Dermatology, Nanfang Hospital, Southern Medical UniversityDepartment of Dermatology, Nanfang Hospital, Southern Medical UniversityDepartment of Dermatology, Nanfang Hospital, Southern Medical UniversityDepartment of Dermatology, Nanfang Hospital, Southern Medical UniversityDepartment of Dermatology, Nanfang Hospital, Southern Medical UniversityAbstract 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.https://doi.org/10.1186/s12985-023-02281-yHuman papillomavirusE6 proteinE7 proteinRecombinant proteinMaltose binding proteinCytokine |
| spellingShingle | Mei-nian Xu Mei-zhen Zhong Si-ning Feng Yan-qin Xu Xiao-ming Peng Kang Zeng Xiao-wen Huang Production of recombinant HPV11/16 E6/E7-MBP-His6 fusion proteins and their potential to induce cytokine secretion by immune cells in peripheral blood Virology Journal Human papillomavirus E6 protein E7 protein Recombinant protein Maltose binding protein Cytokine |
| title | Production of recombinant HPV11/16 E6/E7-MBP-His6 fusion proteins and their potential to induce cytokine secretion by immune cells in peripheral blood |
| title_full | Production of recombinant HPV11/16 E6/E7-MBP-His6 fusion proteins and their potential to induce cytokine secretion by immune cells in peripheral blood |
| title_fullStr | Production of recombinant HPV11/16 E6/E7-MBP-His6 fusion proteins and their potential to induce cytokine secretion by immune cells in peripheral blood |
| title_full_unstemmed | Production of recombinant HPV11/16 E6/E7-MBP-His6 fusion proteins and their potential to induce cytokine secretion by immune cells in peripheral blood |
| title_short | Production of recombinant HPV11/16 E6/E7-MBP-His6 fusion proteins and their potential to induce cytokine secretion by immune cells in peripheral blood |
| title_sort | production of recombinant hpv11 16 e6 e7 mbp his6 fusion proteins and their potential to induce cytokine secretion by immune cells in peripheral blood |
| topic | Human papillomavirus E6 protein E7 protein Recombinant protein Maltose binding protein Cytokine |
| url | https://doi.org/10.1186/s12985-023-02281-y |
| work_keys_str_mv | AT meinianxu productionofrecombinanthpv1116e6e7mbphis6fusionproteinsandtheirpotentialtoinducecytokinesecretionbyimmunecellsinperipheralblood AT meizhenzhong productionofrecombinanthpv1116e6e7mbphis6fusionproteinsandtheirpotentialtoinducecytokinesecretionbyimmunecellsinperipheralblood AT siningfeng productionofrecombinanthpv1116e6e7mbphis6fusionproteinsandtheirpotentialtoinducecytokinesecretionbyimmunecellsinperipheralblood AT yanqinxu productionofrecombinanthpv1116e6e7mbphis6fusionproteinsandtheirpotentialtoinducecytokinesecretionbyimmunecellsinperipheralblood AT xiaomingpeng productionofrecombinanthpv1116e6e7mbphis6fusionproteinsandtheirpotentialtoinducecytokinesecretionbyimmunecellsinperipheralblood AT kangzeng productionofrecombinanthpv1116e6e7mbphis6fusionproteinsandtheirpotentialtoinducecytokinesecretionbyimmunecellsinperipheralblood AT xiaowenhuang productionofrecombinanthpv1116e6e7mbphis6fusionproteinsandtheirpotentialtoinducecytokinesecretionbyimmunecellsinperipheralblood |