<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><submitter>Kremer PG</submitter><funding>NIAID NIH HHS</funding><pubmed_abstract>Both endogenous antibodies and a subset of antibody therapeutics engage Fc gamma receptor (FcγR)IIIa / CD16a to stimulate a protective immune response. Increasing the FcγRIIIa/IgG1 interaction improves the immune response and thus represents a strategy to improve therapeutic efficacy. FcγRIIIa is a heavily glycosylated receptor and glycan composition affects antibody-binding affinity. Though our laboratory previously demonstrated that natural killer (NK) cell N-glycan composition affected the potency of one key protective mechanism, antibody-dependent cell-mediated cytotoxicity (ADCC), it was unclear if this effect was due to FcγRIIIa glycosylation. Furthermore, the structural mechanism linking glycan composition to affinity and cellular activation remained undescribed. To define the role </pubmed_abstract><journal>bioRxiv : the preprint server for biology</journal><pagination>2024.06.17.599285</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11212880</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>One N-glycan regulates natural killer cell antibody-dependent cell-mediated cytotoxicity and modulates Fc γ receptor IIIa / CD16a structure.</pubmed_title><pmcid>PMC11212880</pmcid><funding_grant_id>U01 AI148114</funding_grant_id><pubmed_authors>Kremer PG</pubmed_authors><pubmed_authors>Lampros EA</pubmed_authors><pubmed_authors>Blocker AM</pubmed_authors><pubmed_authors>Barb AW</pubmed_authors></additional><is_claimable>false</is_claimable><name>One N-glycan regulates natural killer cell antibody-dependent cell-mediated cytotoxicity and modulates Fc γ receptor IIIa / CD16a structure.</name><description>Both endogenous antibodies and a subset of antibody therapeutics engage Fc gamma receptor (FcγR)IIIa / CD16a to stimulate a protective immune response. Increasing the FcγRIIIa/IgG1 interaction improves the immune response and thus represents a strategy to improve therapeutic efficacy. FcγRIIIa is a heavily glycosylated receptor and glycan composition affects antibody-binding affinity. Though our laboratory previously demonstrated that natural killer (NK) cell N-glycan composition affected the potency of one key protective mechanism, antibody-dependent cell-mediated cytotoxicity (ADCC), it was unclear if this effect was due to FcγRIIIa glycosylation. Furthermore, the structural mechanism linking glycan composition to affinity and cellular activation remained undescribed. To define the role </description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Jun</publication><modification>2025-04-22T15:35:52.609Z</modification><creation>2025-04-06T01:24:20.488Z</creation></dates><accession>S-EPMC11212880</accession><cross_references><pubmed>38948809</pubmed><doi>10.1101/2024.06.17.599285</doi></cross_references></HashMap>