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<mods:namePart>Chromikova, Veronika</mods:namePart>
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<mods:namePart>Tan, Jessica</mods:namePart>
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<mods:namePart>García Sastre, Adolfo</mods:namePart>
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<mods:namePart>Salaun, Bruno</mods:namePart>
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<mods:namePart>Nachbagauer, Raffael</mods:namePart>
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<mods:namePart>Krammer, Florian</mods:namePart>
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<mods:dateAccessioned encoding="iso8601">2025-10-03T11:16:48Z</mods:dateAccessioned>
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<mods:dateIssued encoding="iso8601">2020-02</mods:dateIssued>
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<mods:identifier type="issn">0264-410X</mods:identifier>
<mods:identifier type="uri">https://hdl.handle.net/10259/10920</mods:identifier>
<mods:identifier type="doi">10.1016/j.vaccine.2020.01.008</mods:identifier>
<mods:identifier type="essn">1873-2518</mods:identifier>
<mods: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.</mods:abstract>
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<mods:accessCondition type="useAndReproduction">Attribution-NonCommercial-NoDerivatives 4.0 Internacional</mods:accessCondition>
<mods:subject>
<mods:topic>Influenza hemagglutinin</mods:topic>
</mods:subject>
<mods:subject>
<mods:topic>ADCC</mods:topic>
</mods:subject>
<mods:subject>
<mods:topic>ADCP</mods:topic>
</mods:subject>
<mods:subject>
<mods:topic>Effector functions</mods:topic>
</mods:subject>
<mods:subject>
<mods:topic>Stalk antibodies</mods:topic>
</mods:subject>
<mods:titleInfo>
<mods:title>Activity of human serum antibodies in an influenza virus hemagglutinin stalk-based ADCC reporter assay correlates with activity in a CD107a degranulation assay</mods:title>
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