Enhanced Immunogenicity and Affinity with A35R-Fc-Based Chimeric Protein Compared to MPXV A35R Protein
The re-emergence of the mpox pandemic poses considerable challenges to human health and societal development. There is an urgent need for effective prevention and treatment strategies against the mpox virus (MPXV). In this study, we focused on the A35R protein and created a chimeric A35R-Fc protein...
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| Format: | Article |
| Language: | English |
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MDPI AG
2025-01-01
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| Series: | Viruses |
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| Online Access: | https://www.mdpi.com/1999-4915/17/1/116 |
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| author | Shimeng Bai Yanxin Cui Qibin Liao Hongyang Yi Zhonghui Liao Gengwei Zhang Fenfang Wu Hongzhou Lu |
| author_facet | Shimeng Bai Yanxin Cui Qibin Liao Hongyang Yi Zhonghui Liao Gengwei Zhang Fenfang Wu Hongzhou Lu |
| author_sort | Shimeng Bai |
| collection | DOAJ |
| description | The re-emergence of the mpox pandemic poses considerable challenges to human health and societal development. There is an urgent need for effective prevention and treatment strategies against the mpox virus (MPXV). In this study, we focused on the A35R protein and created a chimeric A35R-Fc protein by fusing the Fc region of IgG to its C-terminal. We then assessed its reactivity with A35R-specific antibodies and human convalescent plasma, as well as its immunogenicity. Our findings indicate that the A35R-Fc protein significantly enhances affinity to A35R antibodies compared to the commercially available A35R protein and exhibits considerable reactivity to human plasma. Additionally, mice immunized with A35R-Fc exhibited increased neutralizing antibody titers against the live MPXV. These results support the potential of Fc domain chimeric antigens as a strategy to enhance the efficacy of subunit vaccines targeting the MPXV. |
| format | Article |
| id | doaj-art-302f81013b4544ff8a34e7eb144ffc03 |
| institution | Kabale University |
| issn | 1999-4915 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj-art-302f81013b4544ff8a34e7eb144ffc032025-01-24T13:52:38ZengMDPI AGViruses1999-49152025-01-0117111610.3390/v17010116Enhanced Immunogenicity and Affinity with A35R-Fc-Based Chimeric Protein Compared to MPXV A35R ProteinShimeng Bai0Yanxin Cui1Qibin Liao2Hongyang Yi3Zhonghui Liao4Gengwei Zhang5Fenfang Wu6Hongzhou Lu7School of Public Health, Bengbu Medical University, Bengbu 233030, ChinaSchool of Public Health, Bengbu Medical University, Bengbu 233030, ChinaBio-Therapeutic Center, Shenzhen Clinical Research Center for Infectious Disease, State Key Discipline of Infectious Disease, Shenzhen Third People’s Hospital, Second Hospital Affiliated to Southern University of Science and Technology, Shenzhen 518112, ChinaBio-Therapeutic Center, Shenzhen Clinical Research Center for Infectious Disease, State Key Discipline of Infectious Disease, Shenzhen Third People’s Hospital, Second Hospital Affiliated to Southern University of Science and Technology, Shenzhen 518112, ChinaSchool of Public Health, Bengbu Medical University, Bengbu 233030, ChinaBio-Therapeutic Center, Shenzhen Clinical Research Center for Infectious Disease, State Key Discipline of Infectious Disease, Shenzhen Third People’s Hospital, Second Hospital Affiliated to Southern University of Science and Technology, Shenzhen 518112, ChinaBio-Therapeutic Center, Shenzhen Clinical Research Center for Infectious Disease, State Key Discipline of Infectious Disease, Shenzhen Third People’s Hospital, Second Hospital Affiliated to Southern University of Science and Technology, Shenzhen 518112, ChinaSchool of Public Health, Bengbu Medical University, Bengbu 233030, ChinaThe re-emergence of the mpox pandemic poses considerable challenges to human health and societal development. There is an urgent need for effective prevention and treatment strategies against the mpox virus (MPXV). In this study, we focused on the A35R protein and created a chimeric A35R-Fc protein by fusing the Fc region of IgG to its C-terminal. We then assessed its reactivity with A35R-specific antibodies and human convalescent plasma, as well as its immunogenicity. Our findings indicate that the A35R-Fc protein significantly enhances affinity to A35R antibodies compared to the commercially available A35R protein and exhibits considerable reactivity to human plasma. Additionally, mice immunized with A35R-Fc exhibited increased neutralizing antibody titers against the live MPXV. These results support the potential of Fc domain chimeric antigens as a strategy to enhance the efficacy of subunit vaccines targeting the MPXV.https://www.mdpi.com/1999-4915/17/1/116mpoxmpox virusMPXVA35R proteinFc fusion protein |
| spellingShingle | Shimeng Bai Yanxin Cui Qibin Liao Hongyang Yi Zhonghui Liao Gengwei Zhang Fenfang Wu Hongzhou Lu Enhanced Immunogenicity and Affinity with A35R-Fc-Based Chimeric Protein Compared to MPXV A35R Protein Viruses mpox mpox virus MPXV A35R protein Fc fusion protein |
| title | Enhanced Immunogenicity and Affinity with A35R-Fc-Based Chimeric Protein Compared to MPXV A35R Protein |
| title_full | Enhanced Immunogenicity and Affinity with A35R-Fc-Based Chimeric Protein Compared to MPXV A35R Protein |
| title_fullStr | Enhanced Immunogenicity and Affinity with A35R-Fc-Based Chimeric Protein Compared to MPXV A35R Protein |
| title_full_unstemmed | Enhanced Immunogenicity and Affinity with A35R-Fc-Based Chimeric Protein Compared to MPXV A35R Protein |
| title_short | Enhanced Immunogenicity and Affinity with A35R-Fc-Based Chimeric Protein Compared to MPXV A35R Protein |
| title_sort | enhanced immunogenicity and affinity with a35r fc based chimeric protein compared to mpxv a35r protein |
| topic | mpox mpox virus MPXV A35R protein Fc fusion protein |
| url | https://www.mdpi.com/1999-4915/17/1/116 |
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