ArticleProceedings of the National Academy of Sciences of the United States of America2019
Differential requirements for FcγR engagement by protective antibodies against Ebola virus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 52 citations in OpenAlex.
- Fc-engineered antibodies enhance protection against SARS-CoV-2 lung infection and inflammation.mBio · 2026Article
- Review
- Protective effect and molecular mechanisms of human non-neutralizing cross-reactive spike antibodies elicited by SARS-CoV-2 mRNA vaccination.Cell reports · 2024Article
- Fc-FcγR interactions during infections: From neutralizing antibodies to antibody-dependent enhancement.Immunological reviews · 2024Review
- Protective effect and molecular mechanisms of human non-neutralizing cross-reactive spike antibodies elicited by SARS-CoV-2 mRNA vaccination.bioRxiv : the preprint server for biology · 2024Article
- Antiviral neutralizing antibodies: from in vitro to in vivo activity.Nature reviews. Immunology · 2023Review
- Human FcγRIIIa activation on splenic macrophages drives dengue pathogenesis in mice.Nature microbiology · 2023Article
- Complement contributes to antibody-mediated protection against repeated SHIV challenge.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Polyfunctional antibodies: a path towards precision vaccines for vulnerable populations.Frontiers in immunology · 2023Review
- Enhancing the therapeutic activity of hyperimmune IgG against chikungunya virus using FcγRIIIa affinity chromatography.Frontiers in immunology · 2023Article
- Engineering the supernatural: monoclonal antibodies for challenging infectious diseases.Current opinion in biotechnology · 2022Review
- Hybrid Immunity Shifts the Fc-Effector Quality of SARS-CoV-2 mRNA Vaccine-Induced Immunity.mBio · 2022Article
- Distinct impact of IgG subclass on autoantibody pathogenicity in different IgG4-mediated diseases.eLife · 2022Article
- The Role of Antibodies in the Treatment of SARS-CoV-2 Virus Infection, and Evaluating Their Contribution to Antibody-Dependent Enhancement of Infection.International journal of molecular sciences · 2022Review
- Development and Structural Analysis of Antibody Therapeutics for Filoviruses.Pathogens (Basel, Switzerland) · 2022Review
- A Fc-enhanced NTD-binding non-neutralizing antibody delays virus spread and synergizes with a nAb to protect mice from lethal SARS-CoV-2 infection.Cell reports · 2022Article
- Evaluation of strategies to modify Anti-SARS-CoV-2 monoclonal antibodies for optimal functionality as therapeutics.PloS one · 2022Article
- Vaccinal antibodies: Fc antibody engineering to improve the antiviral antibody response and induce vaccine-like effects.Human vaccines & immunotherapeutics · 2021Review
- Differential and sequential immunomodulatory role of neutrophils and Ly6CEmerging microbes & infections · 2021Article
- Building a better antibody through the Fc: advances and challenges in harnessing antibody Fc effector functions for antiviral protection.Human vaccines & immunotherapeutics · 2021Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ebola virus (EBOV) continues to pose significant threats to global public health, requiring ongoing development of multiple strategies for disease control. To date, numerous monoclonal antibodies (mAbs) that target the EBOV glycoprotein (GP) have demonstrated potent protective activity in animal disease models and are thus promising candidates for the control of EBOV. However, recent work in a variety of virus diseases has highlighted the importance of coupling Fab neutralization with Fc effector activity for effective antibody-mediated protection. To determine the contribution of Fc effector activity to the protective function of mAbs to EBOV GP, we selected anti-GP mAbs targeting representative, protective epitopes and characterized their Fc receptor (FcγR) dependence in vivo in FcγR humanized mouse challenge models of EBOV disease. In contrast to previous studies, we find that anti-GP mAbs exhibited differential requirements for FcγR engagement in mediating their protective activity independent of their distance from the viral membrane. Anti-GP mAbs targeting membrane proximal epitopes or the GP mucin domain do not rely on Fc-FcγR interactions to confer activity, whereas antibodies against the GP chalice bowl and the fusion loop require FcγR engagement for optimal in vivo antiviral activity. This complexity of antibody-mediated protection from EBOV disease highlights the structural constraints of FcγR binding for specific viral epitopes and has important implications for the development of mAb-based immunotherapeutics with optimal potency and efficacy.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.