{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Heo M"],"funding":["European Research Council"],"pagination":["614"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7589517"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["3(1)"],"pubmed_abstract":["Antibodies with antibacterial activity need to bind to the bacterial surface with affinity, specificity, and sufficient density to induce efficient elimination. To characterize the anti-bacterial antibody repertoire, we developed an in-droplet bioassay with single-antibody resolution. The assay not only allowed us to identify whether the secreted antibodies recognized a bacterial surface antigen, but also to estimate the apparent dissociation constant (K<sub>D app</sub>) of the interaction and the density of the recognized epitope on the bacteria. Herein, we found substantial differences within the K<sub>D app</sub>/epitope density profiles in mice immunized with various species of heat-killed bacteria. The experiments further revealed a high cross-reactivity of the secreted IgG repertoire"],"journal":["Communications biology"],"pubmed_title":["Deep phenotypic characterization of immunization-induced antibacterial IgG repertoires in mice using a single-antibody bioassay."],"pmcid":["PMC7589517"],"funding_grant_id":["616050","80336"],"pubmed_authors":["Bibette J","Bruhns P","Castrillon C","Chenon G","Baudry J","Heo M","Griffiths AD","Eyer K"],"additional_accession":[]},"is_claimable":false,"name":"Deep phenotypic characterization of immunization-induced antibacterial IgG repertoires in mice using a single-antibody bioassay.","description":"Antibodies with antibacterial activity need to bind to the bacterial surface with affinity, specificity, and sufficient density to induce efficient elimination. To characterize the anti-bacterial antibody repertoire, we developed an in-droplet bioassay with single-antibody resolution. The assay not only allowed us to identify whether the secreted antibodies recognized a bacterial surface antigen, but also to estimate the apparent dissociation constant (K<sub>D app</sub>) of the interaction and the density of the recognized epitope on the bacteria. Herein, we found substantial differences within the K<sub>D app</sub>/epitope density profiles in mice immunized with various species of heat-killed bacteria. The experiments further revealed a high cross-reactivity of the secreted IgG repertoire","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Oct","modification":"2026-07-16T02:33:27.059Z","creation":"2025-05-31T22:43:03.46Z"},"accession":"S-EPMC7589517","cross_references":{"pubmed":["33106526"],"doi":["10.1038/s42003-020-01296-3"]}}