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Published on: May 6, 2015
Enhanced Immunogenicity and Affinity with A35R-Fc-Based Chimeric Protein Compared to MPXV A35R Protein
Shimeng Bai1,2, Yanxin Cui2, Qibin Liao1
1Bio-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, China.
Abstract:
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.
Insights
Developing a novel mpox virus (MPXV) vaccine component, researchers created an A35R-Fc chimeric protein. This enhanced antigen demonstrated improved antibody binding and increased neutralizing antibody responses in mice, suggesting potential for more effective mpox vaccines.
Area of Science:
- Virology
- Immunology
- Vaccine Development
Background:
- The mpox pandemic presents significant global health challenges, necessitating improved prevention and treatment strategies.
- The mpox virus (MPXV) requires effective countermeasures, particularly novel vaccine approaches.
Purpose of the Study:
- To develop and evaluate a chimeric A35R-Fc protein for enhanced immunogenicity against MPXV.
- To assess the reactivity and neutralizing capabilities of the novel A35R-Fc antigen.
Main Methods:
- Construction of a chimeric A35R-Fc protein by fusing the Fc region of IgG to the MPXV A35R protein.
- Assessment of the chimeric protein's reactivity with A35R-specific antibodies and human convalescent plasma.
- Evaluation of the immunogenicity in mice, measuring neutralizing antibody titers against live MPXV.
Main Results:
- The A35R-Fc protein showed significantly enhanced affinity for A35R antibodies compared to the standard A35R protein.
- Considerable reactivity was observed between the A35R-Fc protein and human plasma samples.
- Mice immunized with A35R-Fc developed increased neutralizing antibody titers against live MPXV.
Conclusions:
- Fc domain chimeric antigens represent a promising strategy for improving subunit vaccine efficacy against MPXV.
- The A35R-Fc protein holds potential as a component for next-generation mpox vaccines.
- Further research into Fc-fusion antigens could advance mpox prevention efforts.

