<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-06-26T19:32:41Z</responseDate><request verb="GetRecord" identifier="oai:riubu.ubu.es:10259/10920" metadataPrefix="marc">https://riubu.ubu.es/oai/request</request><GetRecord><record><header><identifier>oai:riubu.ubu.es:10259/10920</identifier><datestamp>2025-10-04T00:05:21Z</datestamp><setSpec>com_10259_4862</setSpec><setSpec>com_10259_5086</setSpec><setSpec>com_10259_2604</setSpec><setSpec>col_10259_4863</setSpec></header><metadata><record xmlns="http://www.loc.gov/MARC21/slim" xmlns:doc="http://www.lyncode.com/xoai" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:dcterms="http://purl.org/dc/terms/" xsi:schemaLocation="http://www.loc.gov/MARC21/slim http://www.loc.gov/standards/marcxml/schema/MARC21slim.xsd">
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<datafield tag="042" ind1=" " ind2=" ">
<subfield code="a">dc</subfield>
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<subfield code="a">Chromikova, Veronika</subfield>
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<subfield code="a">Tan, Jessica</subfield>
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<datafield tag="720" ind1=" " ind2=" ">
<subfield code="a">Aslam, Sadaf</subfield>
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<datafield tag="720" ind1=" " ind2=" ">
<subfield code="a">Rajabhathor, Arvind</subfield>
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<datafield tag="720" ind1=" " ind2=" ">
<subfield code="a">Bermudez-Gonzalez, Maria</subfield>
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<datafield tag="720" ind1=" " ind2=" ">
<subfield code="a">Ayllón Barasoain, Juan</subfield>
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<subfield code="a">Simon, Viviana</subfield>
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<subfield code="a">García Sastre, Adolfo</subfield>
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<subfield code="a">Salaun, Bruno</subfield>
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<subfield code="a">Nachbagauer, Raffael</subfield>
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<subfield code="a">Krammer, Florian</subfield>
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<subfield code="c">2020-02</subfield>
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<subfield code="a">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.</subfield>
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<subfield code="a">0264-410X</subfield>
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<subfield code="a">https://hdl.handle.net/10259/10920</subfield>
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<subfield code="a">10.1016/j.vaccine.2020.01.008</subfield>
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<datafield tag="024" ind2=" " ind1="8">
<subfield code="a">1873-2518</subfield>
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<subfield code="a">Influenza hemagglutinin</subfield>
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<subfield code="a">ADCC</subfield>
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<subfield code="a">Effector functions</subfield>
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<subfield code="a">Stalk antibodies</subfield>
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<datafield tag="245" ind1="0" ind2="0">
<subfield code="a">Activity of human serum antibodies in an influenza virus hemagglutinin stalk-based ADCC reporter assay correlates with activity in a CD107a degranulation assay</subfield>
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