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<dc:title>Activity of human serum antibodies in an influenza virus hemagglutinin stalk-based ADCC reporter assay correlates with activity in a CD107a degranulation assay</dc:title>
<dc:creator>Chromikova, Veronika</dc:creator>
<dc:creator>Tan, Jessica</dc:creator>
<dc:creator>Aslam, Sadaf</dc:creator>
<dc:creator>Rajabhathor, Arvind</dc:creator>
<dc:creator>Bermudez-Gonzalez, Maria</dc:creator>
<dc:creator>Ayllón Barasoain, Juan</dc:creator>
<dc:creator>Simon, Viviana</dc:creator>
<dc:creator>García Sastre, Adolfo</dc:creator>
<dc:creator>Salaun, Bruno</dc:creator>
<dc:creator>Nachbagauer, Raffael</dc:creator>
<dc:creator>Krammer, Florian</dc:creator>
<dc:subject>Influenza hemagglutinin</dc:subject>
<dc:subject>ADCC</dc:subject>
<dc:subject>ADCP</dc:subject>
<dc:subject>Effector functions</dc:subject>
<dc:subject>Stalk antibodies</dc:subject>
<dcterms:abstract>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.</dcterms:abstract>
<dcterms:dateAccepted>2025-10-03T11:16:48Z</dcterms:dateAccepted>
<dcterms:available>2025-10-03T11:16:48Z</dcterms:available>
<dcterms:created>2025-10-03T11:16:48Z</dcterms:created>
<dcterms:issued>2020-02</dcterms:issued>
<dc:type>info:eu-repo/semantics/article</dc:type>
<dc:identifier>0264-410X</dc:identifier>
<dc:identifier>https://hdl.handle.net/10259/10920</dc:identifier>
<dc:identifier>10.1016/j.vaccine.2020.01.008</dc:identifier>
<dc:identifier>1873-2518</dc:identifier>
<dc:language>eng</dc:language>
<dc:relation>Vaccine. 2020, V. 8, n. 38, p.1953–1961</dc:relation>
<dc:relation>https://doi.org/10.1016/j.vaccine.2020.01.008</dc:relation>
<dc:rights>http://creativecommons.org/licenses/by-nc-nd/4.0/</dc:rights>
<dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
<dc:rights>Attribution-NonCommercial-NoDerivatives 4.0 Internacional</dc:rights>
<dc:publisher>Elsevier</dc:publisher>
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