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<title>Activity of human serum antibodies in an influenza virus hemagglutinin stalk-based ADCC reporter assay correlates with activity in a CD107a degranulation assay</title>
<creator>Chromikova, Veronika</creator>
<creator>Tan, Jessica</creator>
<creator>Aslam, Sadaf</creator>
<creator>Rajabhathor, Arvind</creator>
<creator>Bermudez-Gonzalez, Maria</creator>
<creator>Ayllón Barasoain, Juan</creator>
<creator>Simon, Viviana</creator>
<creator>García Sastre, Adolfo</creator>
<creator>Salaun, Bruno</creator>
<creator>Nachbagauer, Raffael</creator>
<creator>Krammer, Florian</creator>
<subject>Influenza hemagglutinin</subject>
<subject>ADCC</subject>
<subject>ADCP</subject>
<subject>Effector functions</subject>
<subject>Stalk antibodies</subject>
<description>The stalk of the influenza virus hemagglutinin (HA) is an attractive target for antibody-based universal influenza virus vaccine development. While antibodies that target this part of the virus can be neutralizing, it has been shown in recent years that Fc receptor-mediated effector functions are of significant importance for the protective effect of anti-stalk antibodies. Several assays to measure Fc-Fc receptor interaction-based effector functions like antibody-dependent cellular cytotoxicity and antibody-dependent cellular phagocytosis exist, but they suffer from limitations such as low throughput and high run-to-run variability. Reporter assays for antibody-dependent cellular cytotoxicity based on reporter cells that express luciferase upon engagement of human FcγRIIIa with the Fc of antigen-bound antibodies have been developed as well. These reporter assays can be used in a higher throughput setting with limited run-to-run assay variability but since they express only one Fc receptor, their biological relevance is unclear. Here we optimized an antibody-dependent cellular cytotoxicity reporter assay to measure the activity of antibodies to the conserved stalk domain of H1 hemagglutinin. The assay was then correlated to a CD107a-based degranulation assay, and a strong and significant correlation could be observed. This data suggests that the FcγRIIIa-based reporter assay is a good substitute for functional assays, especially in settings where larger sample numbers need to be analyzed.</description>
<date>2025-10-03</date>
<date>2025-10-03</date>
<date>2020-02</date>
<type>info:eu-repo/semantics/article</type>
<identifier>0264-410X</identifier>
<identifier>https://hdl.handle.net/10259/10920</identifier>
<identifier>10.1016/j.vaccine.2020.01.008</identifier>
<identifier>1873-2518</identifier>
<language>eng</language>
<relation>Vaccine. 2020, V. 8, n. 38, p.1953–1961</relation>
<relation>https://doi.org/10.1016/j.vaccine.2020.01.008</relation>
<rights>http://creativecommons.org/licenses/by-nc-nd/4.0/</rights>
<rights>info:eu-repo/semantics/openAccess</rights>
<rights>Attribution-NonCommercial-NoDerivatives 4.0 Internacional</rights>
<publisher>Elsevier</publisher>
</thesis></metadata></record></GetRecord></OAI-PMH>